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(p-F)-FPRANSNH-C2H5 + H2O
(p-F)-FPR + ANSNH-C2H5
-
-
-
?
acetyl-FTAR-4-nitroanilide + H2O
acetyl-FTAR + 4-nitroaniline
-
-
-
?
acetyl-FYAR-4-nitroanilide + H2O
acetyl-FYAR + 4-nitroaniline
-
-
-
?
acetyl-GTAR-4-nitroanilide + H2O
acetyl-GTAR + 4-nitroaniline
-
-
-
?
acetyl-GTGR-4-nitroanilide + H2O
acetyl-GTGR + 4-nitroaniline
-
-
-
?
acetyl-QYAR-4-nitroanilide + H2O
acetyl-QYAR + 4-nitroaniline
-
-
-
?
Asp-Gly-Arg-p-nitroanilide + H2O
Asp-Gly-Arg + p-nitroaniline
-
-
-
?
benzyl-TAR-4-nitroanilide + H2O
benzyl-TAR + 4-nitroaniline
-
-
-
?
benzyloxycarbonyl-Asp(O-tert-butyl)-Gly-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Asp(O-tert-butyl)-Gly-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Asp-Gly-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Asp-Gly-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-D-Arg-Gly-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-D-Arg-Gly-Arg + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-D-Asp(O-tert-butyl)-Gly-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-D-Asp(O-tert-butyl)-Gly-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-D-Glu(O-tert-butyl)-Gly-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-D-Glu-Gly-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-D-Glu-Gly-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-D-Glu-Gly-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-D-Phe-Gly-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-D-Phe-Gly-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Glu(O-tert-butyl)-Gly-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Glu(O-tert-butyl)-Gly-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Glu-Gly-Arg-4-nitroanilide + H2O
benzyloxycarbonyl-Glu-Gly-Arg + 4-nitroaniline
-
-
-
-
?
benzyloxycarbonyl-pyroglutamic acid-Gly-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-pyroglutamic acid-Gly-Arg + p-nitroaniline
-
-
-
?
benzyloxycarbonyl-Val-Gly-Arg-p-nitroanilide + H2O
benzyloxycarbonyl-Val-Gly-Arg + p-nitroaniline
-
-
-
?
Boc-(p-F)-FPRANSNH-C2H5 + H2O
Boc-(p-F)-FPR + ANSNH-C2H5
-
-
-
?
Boc-D-FLRANSNH-C3H7 + H2O
Boc-D-FLR + ANSNH-C3H7
-
-
-
?
Boc-D-FPRANSNH-C6H11 + H2O
Boc-D-FPR + ANSNH-C6H11
-
-
-
?
Boc-D-FVRANSNH-C2H5 + H2O
Boc-D-FVR + ANSNH-C2H5
-
-
-
?
Boc-D-LGRANSNH-C6H11 + H2O
Boc-D-LGR + ANSNH-C6H11
-
-
-
?
Boc-D-LPRANSNH-C3H7 + H2O
Boc-D-LPR + ANSNH-C3H7
-
-
-
?
Boc-D-LSRANSNH-C3H7 + H2O
Boc-D-LSR + ANSNH-C3H7
-
-
-
?
Boc-D-VGRANSNH-C4H9 + H2O
Boc-D-VGR + ANSNH-C4H9
-
-
-
?
Boc-D-VPRANSNH-C4H9 + H2O
Boc-D-VPR + ANSNH-C4H9
-
-
-
?
Boc-L-FPRANSNH-C2H5 + H2O
Boc-L-FPR + ANSNH-C2H5
-
-
-
?
Boc-L-VGRANSNH-C4H9 + H2O
Boc-L-VGR + ANSNH-C4H9
-
-
-
?
cyclohexylglycyl-Gly-Arg-p-nitroanilide + H2O
cyclohexylglycyl-Gly-Arg + p-nitroaniline
-
-
-
?
D-Asp(O-tert-butyl)-Gly-Arg-4-nitroanilide + H2O
D-Asp(O-tert-butyl)-Gly-Arg + 4-nitroaniline
-
-
-
-
?
D-Asp-Gly-Arg-p-nitroanilide + H2O
D-Asp-Gly-Arg + p-nitroaniline
-
-
-
?
D-cyclohexylglycyl-Gly-Arg-p-nitroanilide + H2O
D-cyclohexylglycyl-Gly-Arg + p-nitroaniline
-
-
-
?
D-FLRANSNH-C3H7 + H2O
D-FLR + ANSNH-C3H7
-
-
-
?
D-FPR ANSNH-C6H11 + H2O
D-FPR + ANSNH-C6H11
-
-
-
?
D-FPRANSN-(CH2)6 + H2O
D-FPR + ANSN-(CH2)6
-
-
-
?
D-FPRANSN-C2H5 + H2O
D-FPR + ANSN-C2H5
-
-
-
?
D-FPRANSN-C2H5-C2H5 + H2O
D-FPR + ANSN-C2H5-C2H5
-
-
-
-
?
D-FPRANSNH-c-C6H11 + H2O
D-FPR + ANSNH-c-C6H11
-
-
-
?
D-FPRANSNH-C2H4OCH3 + H2O
D-FPR + ANSNH-C2H4OCH3
-
-
-
?
D-FPRANSNH-C6H5CH2 + H2O
D-FPR + ANSNH-C6H5CH2
-
-
-
?
D-FPRANSNH-CH2COOCH3 + H2O
D-FPR + ANSNH-CH2COOCH3
-
-
-
?
D-FPRANSNH-i-C3H7 + H2O
D-FPR + ANSNH-i-C3H7
-
-
-
?
D-FPRANSNH-n-C4H9 + H2O
D-FPR + ANSNH-n-C4H9
-
-
-
?
D-FPRANSNH-n-C6H13 + H2O
D-FPR + ANSN-H-n-C6H13
-
-
-
?
D-FPRANSNH-t-C4H9 + H2O
D-FPR + ANSNH-t-C4H9
-
-
-
?
D-FVRANSNH-C2H5 + H2O
D-FVR + ANSNH-C2H5
-
-
-
?
D-Glu-Gly-Arg-p-nitroanilide + H2O
D-Glu-Gly-Arg + p-nitroaniline
-
-
-
?
D-Glu-Phe-Lys-p-nitroanilide + H2O
D-Glu-Phe-Lys + p-nitroaniline
-
-
-
-
?
D-hexahydrotyrosyl-Gly-Arg-p-nitroanilide + H2O
D-hexahydrotyrosyl-Gly-Arg + p-nitroaniline
-
-
-
?
D-Ile-Pro-Arg-4-nitroanilide + H2O
D-Ile-Pro-Arg + 4-nitroaniline
-
-
-
?
D-Ile-Pro-Arg-p-nitroanilide + H2O
D-Ile-Pro-Arg + p-nitroaniline
-
-
-
-
?
D-LGRANSNH-C6H11 + H2O
D-LGR + ANSNH-C6H11
-
-
-
?
D-LPRANSNH-C3H7 + H2O
D-LPR + ANSNH-C3H7
-
-
-
?
D-LSRANSNH-C3H7 + H2O
D-LSR + ANSNH-C3H7
-
-
-
?
D-Lys-Gly-Arg-p-nitroanilide + H2O
D-Lys-Gly-Arg + p-nitroaniline
-
-
-
?
D-norleucyl-hexahydrotyrosol-lysine-p-nitroanilide + H2O
D-norleucyl-hexahydrotyrosol-lysine + p-nitroaniline
-
-
-
-
?
D-Phe-Gly-Arg-p-nitroanilide + H2O
D-Phe-Gly-Arg + p-nitroaniline
-
-
-
?
D-Val-L-Leu-L-Lys-p-nitroanilide + H2O
D-Val-L-Leu-L-Lys + p-nitroaniline
-
-
-
?
D-Val-Leu-Lys-7-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
D-Val-Leu-Lys-p-nitroanilide + H2O
D-Val-Leu-Lys + p-nitroaniline
-
-
-
-
?
D-valyl-L-leucyl-L-lysine 4-nitroanilide + H2O
D-valyl-L-leucyl-L-lysine + 4-nitroaniline
-
-
-
-
?
D-VGRANSNH-C4H9 + H2O
D-VGR + ANSNH-C4H9
-
-
-
?
D-VPRANSNH-C4H9 + H2O
D-VPR + ANSNH-C4H9
-
-
-
?
Glu-Gly-Arg-p-nitroanilide + H2O
Glu-Gly-Arg + p-nitroaniline
-
-
-
?
Glu-plasminogen + H2O
plasmin + ?
-
-
-
-
?
glutaryl-Gly-7-Arg-amido-4-methylcoumarin + H2O
?
-
-
-
-
?
L-FPRANSN-C2H5 + H2O
L-FPR + ANSN-C2H5
-
-
-
-
?
L-VGRANSNH-C4H9 + H2O
L-VGR + ANSNH-C4H9
-
-
-
?
Laminin + H2O
?
-
tPA amplifies excitotoxic neuronal death by degrading laminin and disruption of pro-survival cell-matrix signaling
-
-
?
Lys-Lys-Cys-Pro-Gly-Arg-Val-Val-Gly-Gly-Cys-Val-Ala-His + H2O
?
-
-
-
-
?
Lys-Lys-Ser-Pro-Gly-Arg-Val-Val-Gly-Gly-Ser-Val-Ala-His + H2O
?
-
-
-
-
?
Lys-plasminogen + H2O
plasmin + ?
-
-
-
?
methyloxycarbonyl-D-cyclohexylalanyl-Gly-Arg-p-nitroanilide + H2O
methyloxycarbonyl-D-cyclohexylglycyl-Gly-Arg + p-nitroaniline
-
-
-
?
methyloxycarbonyl-D-cyclohexylglycyl-Gly-Arg-p-nitroanilide + H2O
methyloxycarbonyl-D-cyclohexylglycyl-Gly-Arg + p-nitroaniline
-
-
-
?
methyloxycarbonyl-D-hexahydrotyrosyl-Gly-Arg-p-nitroanilide + H2O
methyloxycarbonyl-D-hexahydrotyrosyl-Gly-Arg + p-nitroaniline
-
-
-
?
methyloxycarbonyl-D-Leu-Gly-Arg-p-nitroanilide + H2O
methyloxycarbonyl-D-Leu-Gly-Arg + p-nitroaniline
-
-
-
?
methyloxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide + H2O
methyloxycarbonyl-D-Nle-Gly-Arg + p-nitroaniline
-
-
-
?
methyloxycarbonyl-D-Val-Gly-Arg-p-nitroanilide + H2O
methyloxycarbonyl-D-Nle-Gly-Arg + p-nitroaniline
-
-
-
?
methylsulfonyl-D-cyclohexylglycyl-Arg-7-amido-4-methylcoumarin + H2O
methylsulfonyl-D-cyclohexylglycyl-Arg + 7-amino-4-methylcoumarin
methylsulfonyl-D-cyclohexyltyrosyl-glycyl-arginine-p-nitroanilide + H2O
methylsulfonyl-D-cyclohexyltyrosyl-glycyl-arginine + p-nitroaniline
a chromogenic substrate
-
-
?
methylsulfonyl-D-Phe-Gly-Arg-7-amido-4-methylcoumarin + H2O
methylsulfonyl-D-Phe-Gly-Arg + 7-amino-4-methylcoumarin
methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide + H2O
methylsulfonyl-D-Phe-Gly-Arg + p-nitroaniline
-
-
-
?
MMP-9 + H2O
?
-
tPA directly or by activation of MMP-9, can have beneficial effects on recovery after stroke by promoting neurovascular repair through vascular endothelial growth factor
-
-
?
N-methyl-D-aspartate receptor + H2O
?
usage of total rat brain lysates or MBP-ATD2B fusion proteins, the recombinant human enzyme shows cleavage of the ATD sequence in the NR2B subunit N-terminus of N-methyl-D-aspartate (NMDA) receptor. Enzyme-mediated degradation of NR2B is plasmin-independent. The enzyme cleaves the MBP-ATD2B fusion protein
an Arg27-Arg67-truncated NR2B-containing NMDA receptor might be formed
-
?
N-methyl-D-aspartate receptor NR1 subunit + H2O
?
PAR-1 + H2O
?
-
toxic effects of tPA in stroke can be mediated through activation of PAR-1
-
-
?
Peptide S-2288 + H2O
?
-
chromogenic substrate
-
-
?
pGlu-Gly-Arg-4-nitroanilide + H2O
pGlu-Gly-Arg + 4-nitroaniline
-
-
-
-
?
Phe-Gly-Arg-p-nitroanilide + H2O
Phe-Gly-Arg + p-nitroaniline
-
-
-
?
plasminogen + H2O
plasmin + ?
plasminogen + H2O
plasminon + ?
-
-
-
-
?
Plasminogen-activator-inhibitor 1 + H2O
?
platelet-derived growth factor C + H2O
?
-
-
-
?
pyro-Glu-Pro-Arg-4-nitroanilide + H2O
pyro-Glu-Pro-Arg + 4-nitroaniline
-
-
-
?
S-2288TM + H2O
?
-
amidolytic activity of recombinant tPA bound to polyacrylic acid-coated magnetite is 87% of that of free recombinant tPA. Amidolytic activity of recombinant tPA immobilized on magnetic nanoparticles coated with dextran is only 11-24% of recombinant tPA bound to polyacrylic acid-coated magnetite
-
-
?
spectrozyme tPA + H2O
?
-
-
-
?
tert-butyloxycarbonyl-Gly-Gly-Arg-p-nitroanilide + H2O
tert-butyloxycarbonyl-Gly-Gly-Arg + p-nitroaniline
-
-
-
?
Val-Leu-Lys-p-nitroanilide + H2O
p-nitroaniline + ?
Z-Pyr-Gly-Arg-7-amido-4-methylcoumarin + H2O
Z-Pyr-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
?
[SNase]-PFGRSA + H2O
[SNase]-PFGR + [SNase]-Ser-Ala
-
staphylococcal nuclease with substitutions for amino acids 44-51
-
?
[SNase]-PFGRSAG + H2O
[SNase]-PFGR + [SNase]-Ser-Ala-Gly
-
staphylococcal nuclease with substitutions for amino acids 44-51
-
?
[SNase]-PGPFGRSAG + H2O
[SNase]-PGPFGR + [SNase]-Ser-Ala-Gly
-
staphylococcal nuclease with substitutions for amino acids 44-51
-
?
[SNase]-PGPFGRSAGG + H2O
[SNase]-PGPFGR + [SNase]-Ser-Ala-Gly-Gly
-
staphylococcal nuclease with substitutions for amino acids 44-51
-
?
[SNase]-PGSGRSAG + H2O
[SNase]-PGSGR + [SNase]-Ser-Ala-Gly
-
staphylococcal nuclease with substitutions for amino acids 44-51
-
?
[SNase]-PHYGRSGG + H2O
[SNase]-PHYGR + [SNase]-Ser-Gly-Gly
-
staphylococcal nuclease with substitutions for amino acids 44-51
-
?
[SNase]-PPFGRSAG + H2O
[SNase]-PPFGR + [SNase]-Ser-Ala-Gly
-
staphylococcal nuclease with substitutions for amino acids 44-51
-
?
[SNase]-PQRGRSAG + H2O
[SNase]-PQRGR + [SNase]-Ser-Ala-Gly
-
staphylococcal nuclease with substitutions for amino acids 44-51
-
?
additional information
?
-
casein + H2O
?
-
-
-
-
?
casein + H2O
?
-
casein zymography assay
-
-
?
casein + H2O
?
-
endogenous TPA activities in the ipsilateral ischemic hemisphere are measured using casein-zymography
-
-
?
casein + H2O
?
-
endogenous TPA activities in the ipsilateral ischemic hemisphere are measured using casein-zymography
-
-
?
casein + H2O
?
-
casein zymography assay
-
-
?
methylsulfonyl-D-cyclohexylglycyl-Arg-7-amido-4-methylcoumarin + H2O
methylsulfonyl-D-cyclohexylglycyl-Arg + 7-amino-4-methylcoumarin
chromogenic substrate
-
-
?
methylsulfonyl-D-cyclohexylglycyl-Arg-7-amido-4-methylcoumarin + H2O
methylsulfonyl-D-cyclohexylglycyl-Arg + 7-amino-4-methylcoumarin
-
chromogenic substrate
-
-
?
methylsulfonyl-D-Phe-Gly-Arg-7-amido-4-methylcoumarin + H2O
methylsulfonyl-D-Phe-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
methylsulfonyl-D-Phe-Gly-Arg-7-amido-4-methylcoumarin + H2O
methylsulfonyl-D-Phe-Gly-Arg + 7-amino-4-methylcoumarin
-
-
-
-
?
N-methyl-D-aspartate receptor NR1 subunit + H2O
?
-
-
-
-
?
N-methyl-D-aspartate receptor NR1 subunit + H2O
?
-
-
-
-
?
plasminogen + H2O
?
-
-
-
-
?
plasminogen + H2O
?
-
responsible for practically all vascular fibrinolysis through activation of plasminogen
-
-
?
plasminogen + H2O
?
-
participation in the destruction of the follicle wall
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
plasmin is a potent broad-spectrum protease that cleaves fibrin and is able to degrade several components of the extracellular matrix by activating procollagenases and matrix metalloproteinases
-
?
plasminogen + H2O
plasmin + ?
-
cleavage of an Arg-Val bond near the carboxy-terminal end
Glu-plasmin consists of two polypeptides, MW 25000 and 65000, linked together by two disulfide bonds
?
plasminogen + H2O
plasmin + ?
-
cleavage of Arg560-Val561
-
?
plasminogen + H2O
plasmin + ?
-
Glu-plasminogen is the native form of human plasminogen
-
?
plasminogen + H2O
plasmin + ?
-
Glu-plasminogen is the native form of human plasminogen
Glu-plasmin consists of two polypeptides, MW 25000 and 65000, linked together by two disulfide bonds
?
plasminogen + H2O
plasmin + ?
-
cleavage of the Arg561-Val562 bond of plasminogen, converting the zymogen into the active serine protease plasmin
-
?
plasminogen + H2O
plasmin + ?
-
single-chain tPA mediated activation
-
?
plasminogen + H2O
plasmin + ?
-
critical role in fibrinolysis
-
?
plasminogen + H2O
plasmin + ?
-
activation
-
-
?
plasminogen + H2O
plasmin + ?
activation
-
-
?
plasminogen + H2O
plasmin + ?
-
activation
-
-
?
plasminogen + H2O
plasmin + ?
activation
-
-
?
plasminogen + H2O
plasmin + ?
37°C, pH 7.6
-
-
?
plasminogen + H2O
plasmin + ?
37°C, pH 8.0
-
-
?
plasminogen + H2O
plasmin + ?
pH 7.4, 37°C
-
-
?
plasminogen + H2O
plasmin + ?
-
patients suffering intracranial hemorrhage or cerebral infarction after receiving 100 mg t-PA for acute myocardial infarction
-
-
?
plasminogen + H2O
plasmin + ?
-
the tPA plasminogen proteolytic cascade is involved in the cleavage of probrain-derived neurotrophic factor to brain-derived neurotrophic factor, by which the direction of brain-derived neurotrophic factor action is controlled. Brain-derived neurotrophic factor is important for the pathogenesis of major depressive disorder
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
in situ zymography assay
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
in situ zymography assay
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
plasminogen + H2O
plasmin + ?
-
-
-
-
?
Plasminogen-activator-inhibitor 1 + H2O
?
-
treatment with 0.1% SDS, PAI-1 loses its inhibitory activity and is cleaved as a substrate in the reactive centre
-
-
?
Plasminogen-activator-inhibitor 1 + H2O
?
-
PAI-1 may occur in three interconvertible conformations: latent, inhibitor and substrate
-
-
?
Val-Leu-Lys-p-nitroanilide + H2O
p-nitroaniline + ?
-
i.e. S-2251
-
?
Val-Leu-Lys-p-nitroanilide + H2O
p-nitroaniline + ?
-
i.e. S-2251
-
?
additional information
?
-
-
cleaves linear and cyclic peptides containing its normal target sequence from plasminogen
-
-
?
additional information
?
-
-
single-chain t-PA, sct-PA can be converted to two-chain forrm, tct-PA, by activation cleavage at the arg275-Ile276 peptide bond
-
?
additional information
?
-
-
single-chain t-PA, sct-PA can be converted to two-chain forrm, tct-PA, by activation cleavage at the arg275-Ile276 peptide bond, no hydrolysis of Boc-L-FLRANSNH-C3H7, L-FLRANSNH-C3H7, Boc-D-VSRANSNH-(i-C3H7), D-VSRANSNH-(i-C3H7), BOC-D-VLRANSN-H4H9, D-VLRANSN-H4H9, Boc-D-PGRANSNH-(i-C3H7), D-PGRANSNH-(i-C3H), Boc-D-PPRANSNH-(i-C3H7), D-PPRANSNH-(i-C3H7), Boc-D-SPRANSNH-CH2C6H5, D-SPRANSNH-CH2C6H5, Boc-L-SPRANSNH-CH2C6H5, L-SPRANSNH-CH2C6H5, Boc-L-(Obz)SPRANSNH-CH2C6H5, L-(Obz)SPRANSNH-CH2C6H5, (Z)-L-(Boc)EGRANSNH-C3H7, (Z)-L-EGRANSNH-CH7, L-EGRANSNH-C3H7, (Z)-L-(Boc)EPRANSNH-C3H7, (Z)-L-EPR-ANSNH-C3H7, and L-EPRANSNH-C3H7
-
?
additional information
?
-
-
addition of human recombinant tPA after ischemia, in a mouse model of transient 30-min-suture middle cerebral artery occlusion, enhances ischemic damage both in vitro and in vivo, but XG-102 is able to induce a significant neuroprotection. Addition of recombinant tPA after oxygen and glucose deprivation enhances neuronal death in CA1
-
-
?
additional information
?
-
-
tPA facilitates Ca2+ influx via NMDA receptors and dopaminergic transmission via D1 receptors and long-term potentiation in the hippocampus. tPA promotes degradation of the extracellular matrix, which is important for synaptic remodeling and formation of new axonal varicosities
-
-
?
additional information
?
-
-
tPA is a survival factor that prevents renal interstitial fibroblasts (cell line NRK-49F) and myofibroblasts from apoptosis induced by staurosporine and oxidative stress through an LRP-1-, Erk1/2-, p90RSK-, and Bad-dependent mechanism. Antiapoptotic effect of tPA is independent of its protease activity
-
-
?
additional information
?
-
-
the kringle domains 1 and 2 of tissue-type plasminogen activator, TK12, interact with endothelial vein cells via integrin and the kringle domain DGDA amino acid sequence, overview
-
-
?
additional information
?
-
-
both plasminogen activation and fibrin lysis by tPA. Lysis of fibrin clots performed using confocal microscopy in conjunction with tPA-GFP added to clots formed of fibrin100 and fibrin5. The front of the fibrin clot moves faster in fibrin5 than in fibrin100. There are also morphologic differences that develop in the 2 fibrins as indicated by the pattern of fluorescence, which reflects tPA distribution. Specifically, it can be seen that a granular pattern develops in the fibrin5 lysis series in contrast to the homogeneous fluorescence pattern that is maintained in the fibrin100 series. Binding analysis of tPA to aggregates formed in fibrin5, using orange fluorescent fibrinogen converted to fluorescent fibrin100 and fibrin5
-
-
?
additional information
?
-
-
assay on fibrinolytic activity
-
-
?
additional information
?
-
-
assay on fibrinolytic activity
-
-
?
additional information
?
-
-
the fibrinolytic activity of tPA is determined by the fibrin clot lysis assay using fibrin-containing agarose plates
-
-
?
additional information
?
-
the enzyme converts plasminogen into plasmin
-
-
?
additional information
?
-
-
the enzyme converts plasminogen into plasmin
-
-
?
additional information
?
-
measurement of the remaining activity of immobilized enzyme tPA by two different assays: the S-2288TM assay, which measures the amidolytic activity towards chromogenic substrate, and the fibrinolytic activity assay in fibrin-containing agarose gels
-
-
?
additional information
?
-
-
measurement of the remaining activity of immobilized enzyme tPA by two different assays: the S-2288TM assay, which measures the amidolytic activity towards chromogenic substrate, and the fibrinolytic activity assay in fibrin-containing agarose gels
-
-
?
additional information
?
-
substrate specificity of enzyme tissue-type plasminogen activator, comparison with urokinase-type plasminogen activator, EC 3.4.21.73. The urokinase-type plasminogen activator shows much higher activity towards the peptide substrates
-
-
?
additional information
?
-
-
ZIP4 physically interacts with tPA, immunohistochemic analysis, overview
-
-
?
additional information
?
-
-
the amidolytic assay can be adapted to accurately detect changes in net tPA activity in mouse brain tissues, examination of differences in net tPA activity in the cerebral cortex, sub-cortical structures and cerebellum in wild-type and tPA knockout mice, and in transgenic T4 mice selectively overexpressing tPA in neurons, overview
-
-
?
additional information
?
-
-
the amidolytic assay can be adapted to accurately detect changes in net tPA activity in mouse brain tissues, examination of differences in net tPA activity in the cerebral cortex, sub-cortical structures and cerebellum in wild-type and tPA knockout mice, and in transgenic T4 mice selectively overexpressing tPA in neurons, overview
-
-
?
additional information
?
-
-
ZIP4 physically interacts with tPA, immunohistochemic analysis, overview
-
-
?
additional information
?
-
-
t-PA treatment promotes metalloproteinase-9, metalloproteinase-8, and tissue inhibitor metalloproteinase-2 release from human neutrophils ex vivo within 10 and 30 min. t-PA treatment also promotes metalloproteinase-9 release in formyl peptide-preactivated neutrophils. t-PA treatment stimulates neutrophil degranulation
-
-
?
additional information
?
-
-
tPA induces N27 neuroblast cell death in a dose-and time-dependent manner
-
-
?
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1,5-dansyl-L-glutamylglycyl-L-arginine chloromethyl ketone
-
-
2,5-Bis(4-amidinobenzylidene)cyclopentanone
-
-
2,6-Bis(4-amidinobenzylidene)cyclohexanone
-
-
2,7-Bis(4-amidinobenzylidene)cycloheptanone
-
-
2,7-bis-(4-amidinobenzylidene)-cycloheptanone-(1)dihydrochloride
2,8-Bis(4-amidinobenzylidene)cyclooctanone
-
-
2-([6-[(3'-carbamimidoylbiphenyl-3-yl)oxy]-3,5-difluoro-4-methylpyridin-2-yl]oxy)-4-(dimethylamino)benzoic acid
-
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
-
2-[(6-[[5-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
-
4-(2-aminoethoxy)-N-[3-chloro-2-ethoxy-5-(piperidin-1-yl)phenyl]-3,5-dimethylbenzamide
-
4-[(E)-(5-oxo-2-phenyl-1,3-oxazol-4(5H)-ylidene)methyl]benzenecarboximidamide
-
6-carbamimidoyl-N-(3,5-dimethoxyphenyl)-2-naphthamide
-
6-carbamimidoyl-N-phenyl-2-naphthamide
-
6-methoxy-N-(3'-(trifluoromethyl)biphenyl-4-yl)-2-naphthamide
-
6-methoxy-N-(3'-(trifluoromethyl)biphenyl-4-yl)naphthalene-2-sulfonamide
-
6-methoxy-N-(3'-methoxybiphenyl-4-yl)-2-naphthamide
-
6-methoxy-N-(3'-nitrobiphenyl-4-yl)-2-naphthamide
-
alpha-1-Proteinase inhibitor
-
-
-
alpha-2-Antiplasmin
-
-
-
alpha-2-Macroglobulin
-
-
-
alpha-antiplasmin
alpha-PL
-
bis[(phenylamino)acetyl] [2-(4-carbamimidamidophenyl)-1-[(methoxycarbonyl)amino]ethyl]phosphonate
-
bivalirudin
-
does not exert any protective effect when added at concentrations of 20-200 microg/ml (cell viability of 51.8%)
Cd2+
-
inhibition of amidolytic activity
Cell/platelet-type plasminogen activator inhibitor
-
from bovine aortic endothelial
-
Chi-tPA 1
specific aptamers are designed using SELEX method, possesses high affinity for the chimeric mutant enzyme
-
Chi-tPA 2
specific aptamers are designed using SELEX method, possesses good affinity for the chimeric mutant enzyme
-
Chi-tPA 3
specific aptamers are designed using SELEX method, possesses good affinity for the chimeric mutant enzyme
-
Chi-tPA 4
specific aptamers are designed using SELEX method, possesses good affinity for the chimeric mutant enzyme
-
Chi-tPA 5
specific aptamers are designed using SELEX method, possesses good affinity for the chimeric mutant enzyme
-
Co2+
-
inhibition of amidolytic activity
Cu2+
-
inhibition of amidolytic activity
diphenyl [2-(4-carbamimidamidophenyl)-1-[(methoxycarbonyl)amino]ethyl]phosphonate
-
epsilon-aminocaproic acid
ethyl 4-(3-carbamimidoyl-N-[[2,4,6-tri(propan-2-yl)phenyl]sulfonyl]-L-phenylalanyl)piperazine-1-carboxylate
-
Fast-acting plasminogen activator inhibitor in plasma
-
-
-
Glu-Gly-Arg-chlormethylketone
-
directly binds to the catalytic site of tPA. 100 microg/ml given before tPA exposure, reduces cell death (cell viability of 80.5%)
H89
-
inhibits dibutyryl-cAMP-mediated changes in tPA activity without affecting metalloproteinase-9 activity
Hg2+
-
inhibition of amidolytic activity
Human plasminogen activator inhibitors
-
lipopolysaccharide
-
decreases tPA activity. Co-treatment with dibutyryl-cAMP and lipopolysaccharide dose-dependently prevents lipopolysaccharide-induced downregulation of tPA activity
methyl 4'-(6-carbamoyl-2-naphthamido)biphenyl-3-carboxylate
-
methyl 4'-(6-methoxy-2-naphthamido)biphenyl-3-carboxylate
-
methyl 4'-(6-methoxynaphthalene-2-sulfonamido)biphenyl-3-carboxylate
-
Myxoma virus serine proteinase inhibitor
-
-
-
N-((2-(iodoacetoxy)ethyl)-N-methyl)amino-7-nitrobenz-2-oxa-3-diazole
P9 plasminogen activator inhibitor-1
N-(4-(aminomethyl)phenyl)-6-carbamimidoyl-2-naphthamide trifluoro acetate
-
N-(benzylsulfonyl)-D-seryl-N-(4-carbamimidoylbenzyl)-L-alaninamide
-
N2-(2,4'-dimethoxybiphenyl-4-yl)naphthalene-2,6-dicarboxamide
-
N2-(3'-(trifluoromethyl)biphenyl-4-yl)naphthalene-2,6-dicarboxamide
-
N2-(3'-methoxybiphenyl-4-yl)naphthalene-2,6-dicarboxamide
-
NaCl
-
high concentrations inhibit the binding of beta2-glycoprotein I to tPA
neuroserpin
-
endogenous inhibitor, regulating tPA activity
-
Ni2+
-
inhibition of amidolytic activity
PAI-1
-
ethanol can downregulate the expression of PAI-1, a main inhibitor of tPA in the CNS
-
Phe-Pro-Arg-chlormethylketone
-
directly binds to the catalytic site of tPA. 100 microg/ml given before tPA exposure, reduces cell death (cell viability of 85.7%)
Placental-type plasminogen activator inhibitor
-
-
-
plasminogen
-
substrate inhibition, at low concentrations of t-PA and D-dimer of fibrin containing the D-domain of fibrin in the presence of physiological concentrations of plasminogen
-
plasminogen activator inhibitor
-
PAI-1
-
plasminogen activator inhibitor 1
plasminogen activator inhibitor PAI-1
-
-
-
plasminogen activator inhibitor PAI-2
-
-
-
plasminogen activator inhibitor type 1
-
plasminogen activator inhibitor type 1 (PAI-1)
-
plasminogen activator inhibitor type 2
-
can inhibit cell-bound tPA activity in vitro and thus prevents plasmin formation. Plasminogen activator inhibitor type 2 prevents annexin II heterotetramer/tPA-mediated plasminogen activation by its classic serpin inhibitory activity rather than through competition with tPA/plasminogen for binding. It inhibits cell bound tPA-induced plasmin activity in both an annexin II heterotetramer-dependent and -independent manner
-
plasminogen activator inhibitor type-1
-
major inhibitor of tissue-type plasminogen activator in the blood
-
plasminogen activator inhibitor-1
plasminogen activator inhibitor-1 (PAI-1)
-
sctPA is more susceptible to PAI-1 in buffer solution and in the presence of fibrinogen. In the presence of fibrin there is no difference between single-chain enzyme tPA (sctPA) and two chain tPA (tctPA)
-
plasminogen activator inhibitor-I
-
rapidly inactivates the catalytic activity of tPA in the blood stream
-
propanolol
-
in normotensive subjects, t-PA release by epinephrine is abolished in the presence of propanolol (10 microg/100 ml per minute). In essential hypertensive patients, the response to isoproterenol is impaired as compared with normotensive subjects and is unaffected by NG-monomethyl-L-arginine coinfusion
Protease nexin-like plasminogen activator inhibitor
-
-
-
Rp-cAMP
-
inhibits dibutyryl-cAMP-mediated changes in tPA activity without affecting metalloproteinase-9 activity
serpin plasminogen activator inhibitor (PAI)-1
-
primary physiological inhibitor
-
tPA-STOP
a synthetic specific inhibitor to tissue plasminogen activator
transforming growth factor-beta1
-
partially inhibits interleukin-1alpha induced expression of tPA mRNA in a dose-dependent manner, maximal inhibition at 60 ng/ml
-
Zn2+
-
inhibition of amidolytic activity
2,7-bis-(4-amidinobenzylidene)-cycloheptanone-(1)dihydrochloride
-
2,7-bis-(4-amidinobenzylidene)-cycloheptanone-(1)dihydrochloride
-
Aprotinin
-
Aprotinin
-
mitigates tPA-induced neuronal injury. Pre-treatment of N27 cells with aprotinin for 30 min before tPA exposure is protective against cell death, increasing the cell viability to 91.8% at a tPA concentration of 20 microg/ml. When aprotinin treatment follows tPA exposure, cell death is proportional to the length of tPA exposure
epsilon-aminocaproic acid
-
-
epsilon-aminocaproic acid
EACA
epsilon-aminocaproic acid
-
mitigates tPA-induced neuronal injury
Human plasminogen activator inhibitors
-
after treatment with 0.01% SDS, active PAI-1 is converted to an inactive form that does not form complexes with PA, after treatment with 0.1% SDS, PAI-1 loses its inhibitory activity and is cleaved as a substrate in the reactive centre; PAI-1
-
Human plasminogen activator inhibitors
-
-
-
Human plasminogen activator inhibitors
-
and PAI-1 mutant containing substitutions at the P1 and P1' positions; PAI-1
-
Human plasminogen activator inhibitors
-
PAI-1; PAI-1 may occur in three interconvertible conformations: latent, inhibitor and substrate
-
Human plasminogen activator inhibitors
-
inhibits the fibrin binding of both the single chain and two chain forms of tPA; PAI-1
-
Human plasminogen activator inhibitors
-
PAI-1; purification and characterization of recombinant rabbit plasminogen activator inhibitor-1 expressed in Saccharomyces cerevisiae
-
Human plasminogen activator inhibitors
-
PAI-1; PAI-2 (biochemical characterization)
-
leupeptin
-
-
plasminogen activator inhibitor 1
physiological inhibitor
plasminogen activator inhibitor 1
-
PAI-1, specific endogenous inhibitor, in vivo, administration of mesenchymal stromal cells to mice subjected to middle cerebral artery occlusion significantly increases activation of tPA and downregulates PAI-1 levels in the ischemic boundary zone compared with control PBS treated mice, concurrently with increases of myelinated axons and synaptophysin
plasminogen activator inhibitor type 1
-
pregnant women have higher plasma plasminogen activator inhibitor type 1 antigen concentrations that result in lower basal t-PA/plasminogen activator inhibitor type 1 ratios and plasma t-PA activity concentrations
-
plasminogen activator inhibitor type 1
an important inhibitor of plasminogen activators
-
plasminogen activator inhibitor type 1 (PAI-1)
-
-
-
plasminogen activator inhibitor type 1 (PAI-1)
-
-
-
plasminogen activator inhibitor-1
-
is the major inhibitor of tPA-plasminogen signaling. Evidence for an association between plasminogen activator inhibitor-1 and cardiovascular disease pathogenesis
plasminogen activator inhibitor-1
-
astrocyte-derived
plasminogen activator inhibitor-1
PAI-1, the recombinant chimeric t-PA/b-PA mutant enzyme is 44% less sensitive compared to wild-type tissue plasminogen activator, t-PA
plasminogen activator inhibitor-1
PAI
plasminogen activator inhibitor-1
PAI-1, endogenous PAI-1 inactivates the enzyme. Physiologically, PAI-1 inhibits plasminogen activators rapidly and irreversibly, PAI-1 inhibitory mechanism. Analysis of the overall structure of tPA-PAI-1 Michaelis complex, structure-function relationship, overview. The PAI-1 reactive center loop adopts a unique kinked conformation, and on the tPA side, the S2 and S1beta pockets open up to accommodate PAI-1. The deterined crystal structure provides detailed interactions between tPA 37- and 60-loops with PAI-1, overview Comparison to urokinase-type plasminogen activator (uPA, EC 3.4.21.73) structure with bound plasminogen activator inhibitor-1. As a result of the complex formation, an interface of 1202 A2 (solvent-inaccessible area) between PAI-1 and tPA-SPD is formed, which is higher than that of the uPA-SPDx02PAI-1 complex (1058 A2). Of the total area of PAI-1, 8% is involved in interacting with tPA, whereas for uPA, only 6.9% is at the interface. As a protease inhibitor, PAI-1 is very specific to tPA and uPA. Analysis of PAI-1 mutant 14-1B (N150H/K154T/Q319L/M354I)
plasminogen activator inhibitor-1
-
-
plasminogen activator inhibitor-1
-
plays a major role in the regulation of tPA activity
plasminogen activator inhibitor-1
-
PAI-1, astrocyte-derived, induction of PAI-1 by lipopolysaccharide stimulation in astrocytes
plasminogen activator inhibitor-1
-
PAI-1, endogenous inhibitor of tPA in the cell
xenon
intraischemic xenon dose-dependently inhibits tissue-type plasminogen activator-induced thrombolysis and subsequent reduction of ischemic brain damage, postischemic xenon virtually suppresses ischemic brain damage and tissue-type plasminogen activator-induced brain hemorrhages and disruption of the blood-brain barrier, therefore xenon should not be administered before or together with a tissue-type plasminogen activator therapy
xenon
-
intraischemic xenon dose-dependently inhibits tissue-type plasminogen activator-induced thrombolysis and subsequent reduction of ischemic brain damage, postischemic xenon virtually suppresses ischemic brain damage and tissue-type plasminogen activator-induced brain hemorrhages and disruption of the blood-brain barrier, therefore xenon should not be administered before or together with a tissue-type plasminogen activator therapy
additional information
-
stimulation of tPA-mediated plasminogen activity by beta2-glycoprotein I is inhibited by monoclonal anti-beta2GPI antibodies as well as by anti-beta2GPI antibodies from patients with antiphospholipid syndrome. Binding to beta2-glycoprotein I is competitively inhibited by fluid-phase tPA
-
additional information
-
inhibition of NO synthase with NG-monomethyl-L-arginine (100 microg/100 ml per minute) infusion blunts epinephrine-induced t-PA release in normotensive subjects but not in essential hypertensive patients. In normotensive subjects, t-PA release by epinephrine is not affected by phentolamine coinfusion
-
additional information
synthesis and evaluation of a series of naphthamide and naphthalene sulfonamides as enzyme inhibitors containing non-basic groups as substitute for amidine or guanidine groups, overview
-
additional information
no inhibition of cleavage of the N-methyl-D-aspartate receptor NR2B domain by alpha2-antiplasmin, but by a commercial tissue plasminogen activator inhibitor
-
additional information
-
no inhibition of cleavage of the N-methyl-D-aspartate receptor NR2B domain by alpha2-antiplasmin, but by a commercial tissue plasminogen activator inhibitor
-
additional information
screening of a peptide aldehyde library against tPA, inhibitory potencies of compounds at 0.01 mM, analysis of effects of different amino acids on positions P4, P3, P2, and P1, overview
-
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adenosine
-
potentiates mast cell tPA activity and tPA gene expression, abolished in the presence of adenosine deaminase
bradykinin
-
endothelium-dependent vasodilator that stimulates the release of t-PA. Causes a dose-dependent increase in plasma t-PA antigen and activity concentrations in the infused arm of both pregnant and non-pregnant women. The increase in t-PA activity is greater in the nonpregnant women. Bradykinin increases the net release of t-PA antigen and activity in both pregnant women and non-pregnant women. Both net release of active t-PA and plasma t-PA/plasminogen activator inhibitor type 1 ratios are markedly reduced in pregnant women
cyanogen bromide fibrinogen digest (FIBGN)
-
FIBGN is required for the detection of tPA activity chromogenically
-
cyanogen bromide-treated fibrinogen (CNBr-Fbg)
-
CNBr-Fbg (50 microgram/ml) give a 10-fold enhancement of activation, and addition of 2.86 microg/ml oversulfated chondroitin-6-sulfate or oversulfated fucoidan amplified this to 15-fold. A 25-fold to 35-fold enhancement of activation of glutamic plasminogen by tPA is obtained when 2.86 microgram/ml oversulfated compounds are combined with 16.2 mmol/l lysine and 50 microgram/ml CNBr-Fbg
-
dibutyryl-cAMP
-
slightly increases level of tPA mRNA expression. Concentration-dependently increases tPA activity in both basal and lipopolysaccharide-stimulated rat primary astrocytes. Treatment with 100 micromol increases tPA activity by 757.9% compared with lipopolysaccharide treatment. Differentially modulates MMP-9 and tPA activity through a mechanism related to PKA activation. Co-treatment with lipopolysaccharide and dibutyryl-cAMP does not have an additive effect on tPA mRNA induction
epinephrine
-
intrabrachial infusion of epinephrine (0.1 to 0.3 microg/100 ml per minute) induces greater t-PA release in normotensive subjects as compared with essential hypertensive patients
IBMX
-
increases tPA activity in lipopolysaccharide-stimulated rat primary astrocytes
interleukin-1alpha
-
increases mRNA and protein expression of tPA in a time- and dose-dependent manner. Maximal stimulation at 72 h and 100 U/ml
-
isoproterenol
-
intrabrachial isoproterenol (0.03 mcirog/100 ml per minute) induces a significant increase in t-PA release, an effect blunted by NG-monomethyl-L-arginine
L-lysine
-
addition of 16.2 mmol/l L-lysine give 3fold to 4fold enhancement of activation, which is further enhanced to 5fold to 6fold by addition of 2.86 microgram/ml oversulfated chondroitin-6-sulfate or oversulfated fucoidan
lipopolysaccharide
-
slightly increases level of tPA mRNA expression. Co-treatment with lipopolysaccharide and dibutyryl-cAMP does not have an additive effect on tPA mRNA induction
oversulfated chondroitin-6-sulfate
-
addition of 28.6 microgram/ml gives 2-fold to 4-fold increase in the rate of enhancement of activation of glutamic plasminogen by tPA using 0.05 mol/l Tris buffer (pH 7.35) containing NaCl (0.9%)
-
oversulfated fucoidan
-
addition of 28.6 microgram/ml gives 2-fold to 4-fold increase in the rate of enhancement of activation of glutamic plasminogen by tPA using 0.05 mol/l Tris buffer (pH 7.35) containing NaCl (0.9%)
-
plasminogen activator inhibitor-1
-
dose-dependently facilitates the dissociation of membrane-retained tPA and increases the amounts of tPA-plasminogen activator inhibitor-1 high-molecular-weight complexes in the medium
Polymerized fibrin
-
enhances amidolytic activity of both one-chain tPA forms but not of two-chain tPA
-
rolipram
-
increases tPA activity in lipopolysaccharide-stimulated rat primary astrocytes
statins
-
can induce tPA and inhibits plasminogen activator inhibitor-1
-
Fibrin
-
-
Fibrin
-
enhances activity
Fibrin
-
or fibrin derivatives
Fibrin
-
fibrin-binding induces an activated state of the intact one-chain form
Fibrin
-
activity of wild-type t-PA is stimulated by
Fibrin
activates the wild-type enzyme, and also the chimeric mutant enzyme, the latter to an extremely higher degree, overview
fibrinogen
-
activation induced by
-
fibrinogen
-
activation induced by
-
additional information
-
adrenergic-induced t-PA release is mediated by beta-adrenoreceptors via a mechanism involving the NO pathway. No significant difference in net t-PA release after ouabain infusion. No significant increase in t-PA release during sodium nitroprusside infusion
-
additional information
-
neither human albumin nor control human IgG affect tPA-dependent plasminogen activation
-
additional information
-
nitroprusside, which is an endothelium-independent vasodilator, does not stimulate release of t-PA
-
additional information
enzyme-mediated degradation of NR2B is plasmin-independent
-
additional information
-
enzyme-mediated degradation of NR2B is plasmin-independent
-
additional information
-
in mice subjected to acute restraint stress, tPA activity is rapidly up-regulated in the amygdala
-
additional information
-
in vivo, administration of mesenchymal stromal cells to mice subjected to middle cerebral artery occlusion significantly increases activation of tPA and downregulates PAI-1 levels in the ischemic boundary zone compared with control PBS treated mice, concurrently with increases of myelinated axons and synaptophysin
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.0004 - 0.39
(p-F)-FPRANSNH-C2H5
0.48
acetyl-FTAR-4-nitroanilide
pH and temperature not specified in the publication
0.59
acetyl-FYAR-4-nitroanilide
pH and temperature not specified in the publication
1.1
acetyl-GTAR-4-nitroanilide
pH and temperature not specified in the publication
0.76
acetyl-GTGR-4-nitroanilide
pH and temperature not specified in the publication
1.3
acetyl-QYAR-4-nitroanilide
pH and temperature not specified in the publication
0.86
Asp-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
2.3
benzyloxycarbonyl-Asp(O-tert-butyl)-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.72
benzyloxycarbonyl-Asp-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.52
benzyloxycarbonyl-D-Arg-Gly-Arg-4-nitroanilide
-
pH 8.0, 25°C
1.8
benzyloxycarbonyl-D-Asp(O-tert-butyl)-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
1.2
benzyloxycarbonyl-D-Glu(O-tetr-butyl)-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
2.6
benzyloxycarbonyl-D-Glu-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.3
benzyloxycarbonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.9
benzyloxycarbonyl-Glu-(O-tert-butyl)Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
2.2
benzyloxycarbonyl-Glu-Gly-Arg-4-nitroanilide
-
pH 8.0, 25°C
-
1.36
benzyloxycarbonyl-Val-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.0004 - 0.071
Boc-(p-F)-FPRANSNH-C2H5
0.013 - 0.03
Boc-D-FLRANSNH-C3H7
0.0008
Boc-D-FLRANSNHC3H7
-
pH 7.4, 25°C, ratio tc/sc
0.0026 - 0.047
Boc-D-FPRANSNH-C6H11
0.0027 - 0.091
Boc-D-FVRANSNH-C2H5
0.0004 - 0.023
Boc-D-LGRANSNH-C6H11
0.0006 - 0.066
Boc-D-LPRANSNH-C3H7
0.0006 - 0.36
Boc-D-LSRANSNH-C3H7
0.0007 - 0.14
Boc-D-VGRANSNH-C4H9
0.0005
Boc-D-VPR-ANSNHC4H9
-
pH 7.4, 25°C, ratio tc/sc
0.015 - 0.029
Boc-D-VPRANSNH-C4H9
0.1
Boc-L-VGRANSNHC4H9
-
pH 7.4, 25°C
5.32
cyclohexylglycyl-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
1.7
D-Asp(O-tert-butyl)-Gly-Arg-4-nitroanilide
-
pH 8.0, 25°C
-
1.53
D-cyclohexylglycyl-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.0074 - 0.01
D-FLRANSNH-C3H7
0.00078
D-FPR-ANSNH-C2H4OCH3
-
pH 7.4, 25°C, ratio tc/sc
0.00046
D-FPR-ANSNH-CH2COOCH3
-
pH 7.4, 25°C, ratio tc/sc
0.099
D-FPR-ANSNH-n-C6H13
-
pH 7.4, 25°C, sc-tPA
0.00038 - 0.25
D-FPRANSN-(CH2)6
0.00037 - 0.32
D-FPRANSN-C2H5-C2H5
0.00059 - 0.15
D-FPRANSNH-c-C6H11
0.14 - 0.18
D-FPRANSNH-C2H4OCH3
0.0057 - 0.077
D-FPRANSNH-C6H11
0.0004 - 0.063
D-FPRANSNH-C6H5CH2
0.029 - 0.063
D-FPRANSNH-CH2COOCH3
0.00022 - 0.33
D-FPRANSNH-i-C3H7
0.0004 - 0.12
D-FPRANSNH-n-C4H9
0.095 - 0.096
D-FPRANSNH-n-C6H13
0.0011 - 0.084
D-FPRANSNH-t-C4H9
0.0011 - 0.016
D-FVRANSNH-C2H5
2.9
D-Glu-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.83
D-hexahydrotyrosyl-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.000086 - 0.694
D-Ile-Pro-Arg-p-nitroanilide
0.001 - 0.041
D-LGRANSNH-C6H11
0.0003 - 0.098
D-LPRANSNH-C3H7
0.0012 - 0.069
D-LSRANSNH-C3H7
2.1
D-Lys-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.7
D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.0015 - 0.058
D-VGRANSNH-C4H9
0.0003 - 0.11
D-VPRANSNH-C4H9
3.2
Glu-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.00002 - 0.065
Glu-plasminogen
-
0.036 - 0.97
L-FPRANSNH-C2H5
0.46
L-VGRANSNH-C4H9
-
pH 7.4, 25°C
5.9
Lys-Lys-Cys-Pro-Gly-Arg-Val-Val-Gly-Gly-Cys-Val-Ala-His
-
-
3.6
Lys-Lys-Ser-Pro-Gly-Arg-Val-Val-Gly-Gly-Ser-Val-Ala-His
-
-
0.00001 - 0.019
Lys-plasminogen
-
0.34
methyloxycarbonyl-D-cyclohexylalanyl-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.42
methyloxycarbonyl-D-cyclohexylglycyl-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.39
methyloxycarbonyl-D-hexahydrotyrosyl-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.62
methyloxycarbonyl-D-Leu-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.99
methyloxycarbonyl-D-Nle-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.8
methyloxycarbonyl-D-Val-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.1
methylsulfonyl-D-Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.000017
Peptide S-2288
-
-
3.15
pGlu-Gly-Arg-4-nitroanilide
-
pH 8.0, 25°C
-
2
Phe-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.000018 - 0.065
plasminogen
-
0.4 - 4.6
spectrozyme tPA
3.5
tert-butoxycarbonyl-Gly-Gly-Arg-p-nitroanilide
-
pH 8.0, 25°C
0.14
[SNase]-PFGRSA
-
pH 7.4, 37°C
-
0.079
[SNase]-PFGRSAG
-
pH 7.4, 37°C
-
0.0099
[SNase]-PGPFGRSAG
-
pH 7.4, 37°C
-
0.0093
[SNase]-PGPFGRSAGG
-
pH 7.4, 37°C
-
0.017
[SNase]-PGSGRSAG
-
pH 7.4, 37°C
-
0.018
[SNase]-PHYGRSGG
-
pH 7.4, 37°C
-
0.0099
[SNase]-PPFGRSAG
-
pH 7.4, 37°C
-
0.0089
[SNase]-PQRGRSAG
-
pH 7.4, 37°C
-
additional information
additional information
-
0.0004
(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, ratio tc/sc
0.011
(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, tc-tPA
0.026
(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, sc-tPA
0.39
(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C
0.0004
Boc-(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, ratio tc/sc
0.0004
Boc-(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, sc-tPA
0.0066
Boc-(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, tc-tPA
0.016
Boc-(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, sc-tPA
0.071
Boc-(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C
0.013
Boc-D-FLRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
0.017
Boc-D-FLRANSNH-C3H7
-
pH 7.4, 25°C, sc-tPA
0.03
Boc-D-FLRANSNH-C3H7
-
pH 7.4, 25°C
0.0026
Boc-D-FPRANSNH-C6H11
-
pH 7.4, 25°C, tc-tPA
0.047
Boc-D-FPRANSNH-C6H11
-
pH 7.4, 25°C
0.0027
Boc-D-FVRANSNH-C2H5
-
pH 7.4, 25°C, ratio tc/sc
0.012
Boc-D-FVRANSNH-C2H5
-
pH 7.4, 25°C, sc-tPA
0.032
Boc-D-FVRANSNH-C2H5
-
pH 7.4, 25°C, tc-tPA
0.091
Boc-D-FVRANSNH-C2H5
-
pH 7.4, 25°C
0.0004
Boc-D-LGRANSNH-C6H11
-
pH 7.4, 25°C, ratio tc/sc
0.0085
Boc-D-LGRANSNH-C6H11
-
pH 7.4, 25°C, tc-tPA
0.015
Boc-D-LGRANSNH-C6H11
-
pH 7.4, 25°C
0.023
Boc-D-LGRANSNH-C6H11
-
pH 7.4, 25°C, sc-tPA
0.0006
Boc-D-LPRANSNH-C3H7
-
pH 7.4, 25°C, ratio tc/sc
0.0088
Boc-D-LPRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
0.015
Boc-D-LPRANSNH-C3H7
-
pH 7.4, 25°C, sc-tPA
0.066
Boc-D-LPRANSNH-C3H7
-
pH 7.4, 25°C
0.0006
Boc-D-LSRANSNH-C3H7
-
pH 7.4, 25°C, ratio tc/sc
0.013
Boc-D-LSRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
0.02
Boc-D-LSRANSNH-C3H7
-
pH 7.4, 25°C, sc-tPA
0.36
Boc-D-LSRANSNH-C3H7
-
pH 7.4, 25°C
0.0007
Boc-D-VGRANSNH-C4H9
-
pH 7.4, 25°C, ratio tc/sc
0.014
Boc-D-VGRANSNH-C4H9
-
pH 7.4, 25°C, tc-tPA
0.019
Boc-D-VGRANSNH-C4H9
-
pH 7.4, 25°C, sc-tPA
0.022
Boc-D-VGRANSNH-C4H9
-
pH 7.4, 25°C, sc-tPA
0.14
Boc-D-VGRANSNH-C4H9
-
pH 7.4, 25°C
0.015
Boc-D-VPRANSNH-C4H9
-
pH 7.4, 25°C, tc-tPA
0.026
Boc-D-VPRANSNH-C4H9
-
pH 7.4, 25°C
0.029
Boc-D-VPRANSNH-C4H9
-
pH 7.4, 25°C, sc-tPA
0.0074
D-FLRANSNH-C3H7
-
pH 7.4, 25°C
0.01
D-FLRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
0.00038
D-FPRANSN-(CH2)6
-
pH 7.4, 25°C, ratio tc/sc
0.096
D-FPRANSN-(CH2)6
-
pH 7.4, 25°C, tc-tPA
0.25
D-FPRANSN-(CH2)6
-
pH 7.4, 25°C, sc-tPA
0.00037
D-FPRANSN-C2H5-C2H5
-
pH 7.4, 25°C, ratio tc/sc
0.12
D-FPRANSN-C2H5-C2H5
-
pH 7.4, 25°C, tc-tPA
0.32
D-FPRANSN-C2H5-C2H5
-
pH 7.4, 25°C, sc-tPA
0.00059
D-FPRANSNH-c-C6H11
-
pH 7.4, 25°C, ratio tc/sc
0.088
D-FPRANSNH-c-C6H11
-
pH 7.4, 25°C, tc-tPA
0.15
D-FPRANSNH-c-C6H11
-
pH 7.4, 25°C, sc-tPA
0.14
D-FPRANSNH-C2H4OCH3
-
pH 7.4, 25°C, tc-tPA
0.18
D-FPRANSNH-C2H4OCH3
-
pH 7.4, 25°C, tc-tPA
0.0057
D-FPRANSNH-C6H11
-
pH 7.4, 25°C, sc-tPA
0.013
D-FPRANSNH-C6H11
-
pH 7.4, 25°C, ratio tc/sc
0.077
D-FPRANSNH-C6H11
-
pH 7.4, 25°C, tc-tPA
0.0004
D-FPRANSNH-C6H5CH2
-
pH 7.4, 25°C, ratio tc/sc
0.025
D-FPRANSNH-C6H5CH2
-
pH 7.4, 25°C, tc-tPA
0.063
D-FPRANSNH-C6H5CH2
-
pH 7.4, 25°C, tc-tPA
0.029
D-FPRANSNH-CH2COOCH3
-
pH 7.4, 25°C, tc-tPA
0.063
D-FPRANSNH-CH2COOCH3
-
pH 7.4, 25°C, sc-tPA
0.00022
D-FPRANSNH-i-C3H7
-
pH 7.4, 25°C, ratio tc/sc
0.074
D-FPRANSNH-i-C3H7
-
pH 7.4, 25°C, tc-tPA
0.33
D-FPRANSNH-i-C3H7
-
pH 7.4, 25°C, tc-tPA
0.0004
D-FPRANSNH-n-C4H9
-
pH 7.4, 25°C, ratio tc/sc
0.048
D-FPRANSNH-n-C4H9
-
pH 7.4, 25°C, tc-tPA
0.12
D-FPRANSNH-n-C4H9
-
pH 7.4, 25°C, sc-tPA
0.095
D-FPRANSNH-n-C6H13
-
pH 7.4, 25°C, tc-tPA
0.096
D-FPRANSNH-n-C6H13
-
pH 7.4, 25°C, ratio tc/sc
0.0011
D-FPRANSNH-t-C4H9
-
pH 7.4, 25°C, ratio tc/sc
0.079
D-FPRANSNH-t-C4H9
-
pH 7.4, 25°C, sc-tPA
0.084
D-FPRANSNH-t-C4H9
-
pH 7.4, 25°C, tc-tPA
0.0011
D-FVRANSNH-C2H5
-
pH 7.4, 25°C, ratio tc/sc
0.0073
D-FVRANSNH-C2H5
-
pH 7.4, 25°C, sc-tPA
0.0078
D-FVRANSNH-C2H5
-
pH 7.4, 25°C, tc-tPA
0.016
D-FVRANSNH-C2H5
-
pH 7.4, 25°C
0.000086
D-Ile-Pro-Arg-p-nitroanilide
-
value for sctPA, in the presence of stimulater Fibrin P (treated with plasmin-Sepharose)
0.000087
D-Ile-Pro-Arg-p-nitroanilide
-
value for sctPA, in the presence of stimulater Fibrin normal
0.000109
D-Ile-Pro-Arg-p-nitroanilide
-
value for tctPA, in the presence of stimulater Fibrin N
0.000119
D-Ile-Pro-Arg-p-nitroanilide
-
value for tctPA, in the presence of stimulater Fibrin P (treated with plasmin-Sepharose)
0.000341
D-Ile-Pro-Arg-p-nitroanilide
-
value for sctPA, in the presence of stimulater Fibrin C (with cleaved C-terminal lysines)
0.000362
D-Ile-Pro-Arg-p-nitroanilide
-
value for tctPA, in the presence of stimulater Fibrin C (with cleaved C-terminal lysines)
0.694
D-Ile-Pro-Arg-p-nitroanilide
-
value for sctPA
0.694
D-Ile-Pro-Arg-p-nitroanilide
-
value for tctPA
0.001
D-LGRANSNH-C6H11
-
pH 7.4, 25°C, ratio tc/sc
0.011
D-LGRANSNH-C6H11
-
pH 7.4, 25°C, tc-tPA and sc-tPA
0.041
D-LGRANSNH-C6H11
-
pH 7.4, 25°C
0.0003
D-LPRANSNH-C3H7
-
pH 7.4, 25°C, ratio tc/sc
0.012
D-LPRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
0.04
D-LPRANSNH-C3H7
-
pH 7.4, 25°C, sc-tPA
0.098
D-LPRANSNH-C3H7
-
pH 7.4, 25°C
0.0012
D-LSRANSNH-C3H7
-
pH 7.4, 25°C, ratio tc/sc
0.014
D-LSRANSNH-C3H7
-
pH 7.4, 25°C, sc-tPA
0.017
D-LSRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
0.069
D-LSRANSNH-C3H7
-
pH 7.4, 25°C
0.0015
D-VGRANSNH-C4H9
-
pH 7.4, 25°C, ratio tc/sc
0.033
D-VGRANSNH-C4H9
-
pH 7.4, 25°C, tc-tPA
0.058
D-VGRANSNH-C4H9
-
pH 7.4, 25°C
0.0003
D-VPRANSNH-C4H9
-
pH 7.4, 25°C, ratio tc/sc
0.0081
D-VPRANSNH-C4H9
-
pH 7.4, 25°C, tc-tPA
0.025
D-VPRANSNH-C4H9
-
pH 7.4, 25°C, sc-tPA
0.11
D-VPRANSNH-C4H9
-
pH 7.4, 25°C
0.00002
Glu-plasminogen
-
with fibrinogen activation
-
0.065
Glu-plasminogen
-
without fibrin
-
0.036
L-FPRANSNH-C2H5
-
pH 7.4, 25°C
0.97
L-FPRANSNH-C2H5
-
pH 7.4, 25°C
0.00001
Lys-plasminogen
-
pH 7.2, 37°C, mutant R275E and P422A/R275E, single-chain form, presence of soluble fibrin
-
0.000011
Lys-plasminogen
-
pH 7.2, 37°C, wild-type, two-chain form, presence of soluble fibrin
-
0.000013
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422A, two-chain form, presence of soluble fibrin
-
0.000014
Lys-plasminogen
-
pH 7.2, 37°C, two-chain form of mutant F423A, single-chain form of mutant L420A/R275E, presence of soluble fibrin
-
0.000015
Lys-plasminogen
-
pH 7.2, 37°C, mutant F423E/R275E, single-chain form, presence of soluble fibrin
-
0.000016
Lys-plasminogen
-
pH 7.2, 37°C, mutant S421G, two-chain form, presence of soluble fibrin
-
0.000018
Lys-plasminogen
-
pH 7.2, 37°C, two-chain form of mutant S421E, single-chain form of mutant L420E/R275E, presence of soluble fibrin
-
0.000019
Lys-plasminogen
-
pH 7.2, 37°C, mutant L420A, two-chain form, presence of soluble fibrin
-
0.000021
Lys-plasminogen
-
pH 7.2, 37°C, mutant L420E, two-chain form, presence of soluble fibrin
-
0.000022
Lys-plasminogen
-
pH 7.2, 37°C, mutant F423A/R275E, single-chain form, presence of soluble fibrin
-
0.000023
Lys-plasminogen
-
pH 7.2, 37°C, two-chain form of mutant F423E, single-chain form of mutant S421E/R275E, presence of soluble fibrin
-
0.000026
Lys-plasminogen
-
pH 7.2, 37°C, two-chain form of mutant P422G, single-chain form of mutant S421G/R275E, presence of soluble fibrin
-
0.000027
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422G/R275E, single-chain form, presence of soluble fibrin
-
0.000028
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422E/R275E, single-chain form, presence of soluble fibrin
-
0.000029
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422E, two-chain form, presence of soluble fibrin
-
0.00016
Lys-plasminogen
-
with fibrinogen activation
-
0.0006
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422G, two-chain form, absence of soluble fibrin
-
0.0007
Lys-plasminogen
-
pH 7.2, 37°C, mutant L420E and P422E, two-chain form, absence of soluble fibrin
-
0.001
Lys-plasminogen
-
pH 7.2, 37°C, mutant L420A, two-chain form, absence of soluble fibrin
-
0.003
Lys-plasminogen
-
pH 7.2, 37°C, mutant S421E, two-chain form, absence of soluble fibrin
-
0.004
Lys-plasminogen
-
pH 7.2, 37°C, two-chain form of mutant S421G, F423A and P422A, single chain form of mutant S421G/R275E and P422G/R275E, absence of soluble fibrin
-
0.005
Lys-plasminogen
-
pH 7.2, 37°C, mutant L420E/R275E, single-chain form, absence of soluble fibrin
-
0.005
Lys-plasminogen
-
pH 7.2, 37°C, two-chain form of wild-type and mutant F423E, single-chain form of mutant P422E/R275E, absence of soluble fibrin
-
0.007
Lys-plasminogen
-
pH 7.2, 37°C, mutant S421E/R275E, single-chain form, absence of soluble fibrin
-
0.008
Lys-plasminogen
-
pH 7.2, 37°C, mutant F423E/R275E, single-chain form, absence of soluble fibrin
-
0.009
Lys-plasminogen
-
pH 7.2, 37°C, mutant L420A/R275E, single-chain form, absence of soluble fibrin
-
0.01
Lys-plasminogen
-
pH 7.2, 37°C, mutant F423A/R275E, single-chain form, absence of soluble fibrin
-
0.013
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422A/R275E, single-chain form, absence of soluble fibrin
-
0.017
Lys-plasminogen
-
pH 7.2, 37°C, mutant R275E, single-chain form, absence of soluble fibrin
-
0.019
Lys-plasminogen
-
without fibrin
-
0.000018
plasminogen
-
activated with fibrin
-
0.0000464
plasminogen
-
in the presence of beta2-glycoprotein I
-
0.0001
plasminogen
-
pH 7.4, 37°C
-
0.0001
plasminogen
-
pH 7.4, 37°C
-
0.0003148
plasminogen
-
in the presence of beta2-glycoprotein I domain V
-
0.0004538
plasminogen
-
in the presence of bovine serum albumin
-
0.005
plasminogen
-
pH 7.4, 37°C, absence of fibrinogen
-
0.0076
plasminogen
-
without fibrin
-
0.065
plasminogen
-
pH 7.4, 37°C
-
3.5
S-2288TM
-
recombinant tPA
-
4.1
S-2288TM
-
recombinant tPA bound to polyacrylic acid-coated magnetite
-
0.4
spectrozyme tPA
-
pH 7.2, 37°C, wild-type t-PA, mutant L420A, L420E, S421G, S421E, P422A, P422E, two-chain form
0.5
spectrozyme tPA
-
pH 7.2, 37°C, mutant F423A, F422E, two-chain form
0.6
spectrozyme tPA
-
pH 7.2, 37°C, P422G, two-chain form
0.9
spectrozyme tPA
-
pH 7.2, 37°C, mutant L420E/R275E, F423E/R275E, single chain form
1
spectrozyme tPA
-
pH 7.2, 37°C, mutant R275E, F423A/R275E, single-chain form
1.1
spectrozyme tPA
-
pH 7.2, 37°C, mutant P422E/R275E, single chain form
1.2
spectrozyme tPA
-
pH 7.2, 37°C, mutant P422A/R275E, single chain form
1.3
spectrozyme tPA
-
pH 7.2, 37°C, mutant L420A/R275E, single chain form
1.7
spectrozyme tPA
-
pH 7.2, 37°C, mutant P422G/R275E, single chain form
2.3
spectrozyme tPA
-
pH 7.2, 37°C, mutant S421E/R275E, single chain form
4.6
spectrozyme tPA
-
pH 7.2, 37°C, mutant L420A/R275E, single chain form
additional information
additional information
-
Km values of different glycoforms of plasminogen by tPA variants
-
additional information
additional information
Michaelis-Menten kinetics
-
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
0.099 - 6.08
(p-F)-FPRANSNH-C2H5
0.24
acetyl-FTAR-4-nitroanilide
pH and temperature not specified in the publication
0.86
acetyl-FYAR-4-nitroanilide
pH and temperature not specified in the publication
0.36
acetyl-GTAR-4-nitroanilide
pH and temperature not specified in the publication
0.21
acetyl-GTGR-4-nitroanilide
pH and temperature not specified in the publication
0.46
acetyl-QYAR-4-nitroanilide
pH and temperature not specified in the publication
0.11 - 6.08
Boc-(p-F)-FPRANSNH-C2H5
0.01 - 4.7
Boc-D-FLRANSNH-C3H7
0.017 - 0.15
Boc-D-FPRANSNH-C6H11
7.9
Boc-D-FVR-ANSNH-C2H5
-
pH 7.4, 25°C, ratio tc/sc
0.019 - 0.49
Boc-D-FVRANSNH-C2H5
0.012 - 3.3
Boc-D-LGRANSNH-C6H11
0.038 - 6.08
Boc-D-LPRANSNH-C3H7
0.022 - 6.08
Boc-D-LSRANSNH-C3H7
0.036 - 5
Boc-D-VGRANSNH-C4H9
0.065 - 3.8
Boc-D-VPRANSNH-C4H9
0.084
Boc-L-VGRANSNHC4H9
-
pH 7.4, 25°C
0.018
D-FLRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
0.016
D-FPR-ANSNH-C6H11
-
pH 7.4, 25°C, sc-tPA
0.45
D-FPR-ANSNH-C6H5CH2
-
pH 7.4, 25°C, sc-tPA
0.47
D-FPR-ANSNH-n-C4H9
-
pH 7.4, 25°C, tc-tPA
3.3 - 3.6
D-FPR-ANSNH-n-C6H13
3.8
D-FPR-ANSNH-t-C4H9
-
pH 7.4, 25°C, ratio tc/sc
0.51 - 6.08
D-FPR-ANSNHC6H11
0.13 - 1.7
D-FPRANSN-(CH2)6
0.09 - 1.6
D-FPRANSN-C2H5-C2H5
0.15
D-FPRANSN-H-c-C6H11
-
pH 7.4, 25°C, sc-tPA
0.2
D-FPRANSN-H-i-C3H7
-
pH 7.4, 25°C, tc-tPA
0.25 - 6.08
D-FPRANSN-H-t-C4H9
0.32 - 2.1
D-FPRANSNH-c-C6H11
0.27 - 6.08
D-FPRANSNH-C2H4OCH3
32
D-FPRANSNH-C6H11
-
pH 7.4, 25°C, ratio tc/sc
0.54 - 6.08
D-FPRANSNH-C6H5CH2
0.083 - 1.8
D-FPRANSNH-CH2COOCH3
0.29 - 6.08
D-FPRANSNH-i-C3H7
0.33 - 1.4
D-FPRANSNH-n-C4H9
1.1
D-FPRANSNH-n-C6H13
-
pH 7.4, 25°C, sc-tPA
0.025
D-FVR-ANSNH-C2H5
-
pH 7.4, 25°C, tc-tPA
0.011 - 2.3
D-FVRANSNH-C2H5
0.026 - 10.7
D-Ile-Pro-Arg-p-nitroanilide
0.034 - 4
D-LGR-ANSNH-C6H11
0.0084 - 0.057
D-LGRANSNH-C6H11
0.061 - 2.8
D-LPRANSNH-C3H7
0.019 - 5.3
D-LSRANSNH-C3H7
89
D-LSRANSNHC3H7
-
pH 7.4, 25°C
0.021 - 9
D-VGRANSNH-C4H9
0.059 - 2.7
D-VPRANSNH-C4H9
0.04
L-FPRANSNH-C2H5
-
pH 7.4, 25°C
0.08
L-VGRANSNH-C4H9
-
pH 7.4, 25°C
0.009
Lys-Lys-Cys-Pro-Gly-Arg-Val-Val-Gly-Gly-Cys-Val-Ala-His
-
-
0.0012
Lys-Lys-Ser-Pro-Gly-Arg-Val-Val-Gly-Gly-Ser-Val-Ala-His
-
-
0.0005 - 0.21
Lys-plasminogen
-
0.0025 - 0.4718
plasminogen
-
0.0041
[SNase]-PFGRSA
-
pH 7.4, 37°C
-
0.018
[SNase]-PFGRSAG
-
pH 7.4, 37°C
-
0.0075
[SNase]-PGPFGRSAG
-
pH 7.4, 37°C
-
0.01
[SNase]-PGPFGRSAGG
-
pH 7.4, 37°C
-
0.012
[SNase]-PHYGRSGG
-
pH 7.4, 37°C
-
0.011
[SNase]-PPFGRSAG
-
pH 7.4, 37°C
-
0.006
[SNase]-PQRGRSAG
-
pH 7.4, 37°C
-
additional information
additional information
-
-
-
0.099
(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, tc-tPA
0.37
(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, tc-tPA
1.47
(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C
3.7
(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, ratio tc/sc
6.08
(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C
0.11
Boc-(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, sc-tPA
0.44
Boc-(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, tc-tPA
1.03
Boc-(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C
4
Boc-(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C, ratio tc/sc
6.08
Boc-(p-F)-FPRANSNH-C2H5
-
pH 7.4, 25°C
0.01
Boc-D-FLRANSNH-C3H7
-
pH 7.4, 25°C, sc-tPA
0.021
Boc-D-FLRANSNH-C3H7
-
pH 7.4, 25°C
0.047
Boc-D-FLRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
0.1
Boc-D-FLRANSNH-C3H7
-
pH 7.4, 25°C
4.7
Boc-D-FLRANSNH-C3H7
-
pH 7.4, 25°C, ratio tc/sc
0.017
Boc-D-FPRANSNH-C6H11
-
pH 7.4, 25°C, tc-tPA
0.15
Boc-D-FPRANSNH-C6H11
-
pH 7.4, 25°C
0.019
Boc-D-FVRANSNH-C2H5
-
pH 7.4, 25°C, tc-tPA
0.044
Boc-D-FVRANSNH-C2H5
-
pH 7.4, 25°C
0.15
Boc-D-FVRANSNH-C2H5
-
pH 7.4, 25°C, tc-tPA
0.49
Boc-D-FVRANSNH-C2H5
-
pH 7.4, 25°C
0.012
Boc-D-LGRANSNH-C6H11
-
pH 7.4, 25°C, sc-tPA
0.04
Boc-D-LGRANSNH-C6H11
-
pH 7.4, 25°C, tc-tPA
0.097
Boc-D-LGRANSNH-C6H11
-
pH 7.4, 25°C
3.3
Boc-D-LGRANSNH-C6H11
-
pH 7.4, 25°C, ratio tc/sc
0.038
Boc-D-LPRANSNH-C3H7
-
pH 7.4, 25°C, sc-tPA
0.2
Boc-D-LPRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
0.54
Boc-D-LPRANSNH-C3H7
-
pH 7.4, 25°C
5.3
Boc-D-LPRANSNH-C3H7
-
pH 7.4, 25°C, ratio tc/sc
6.08
Boc-D-LPRANSNH-C3H7
-
pH 7.4, 25°C
0.022
Boc-D-LSRANSNH-C3H7
-
pH 7.4, 25°C, sc-tPA
0.097
Boc-D-LSRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
0.53
Boc-D-LSRANSNH-C3H7
-
pH 7.4, 25°C
4.4
Boc-D-LSRANSNH-C3H7
-
pH 7.4, 25°C, ratio tc/sc
6.08
Boc-D-LSRANSNH-C3H7
-
pH 7.4, 25°C
0.036
Boc-D-VGRANSNH-C4H9
-
pH 7.4, 25°C, tc-tPA
0.082
Boc-D-VGRANSNH-C4H9
-
pH 7.4, 25°C
0.18
Boc-D-VGRANSNH-C4H9
-
pH 7.4, 25°C, tc-tPA
0.34
Boc-D-VGRANSNH-C4H9
-
pH 7.4, 25°C
5
Boc-D-VGRANSNH-C4H9
-
pH 7.4, 25°C, ratio tc/sc
0.065
Boc-D-VPRANSNH-C4H9
-
pH 7.4, 25°C, sc-tPA
0.25
Boc-D-VPRANSNH-C4H9
-
pH 7.4, 25°C
0.25
Boc-D-VPRANSNH-C4H9
-
pH 7.4, 25°C, tc-tPA
3.8
Boc-D-VPRANSNH-C4H9
-
pH 7.4, 25°C, ratio tc/sc
3.3
D-FPR-ANSNH-n-C6H13
-
pH 7.4, 25°C, ratio tc/sc
3.6
D-FPR-ANSNH-n-C6H13
-
pH 7.4, 25°C, tc-tPA
0.51
D-FPR-ANSNHC6H11
-
pH 7.4, 25°C, tc-tPA
6.08
D-FPR-ANSNHC6H11
-
pH 7.4, 25°C, tc-tPA
0.13
D-FPRANSN-(CH2)6
-
pH 7.4, 25°C, sc-tPA
0.22
D-FPRANSN-(CH2)6
-
pH 7.4, 25°C, tc-tPA
1.7
D-FPRANSN-(CH2)6
-
pH 7.4, 25°C, ratio tc/sc
0.09
D-FPRANSN-C2H5-C2H5
-
pH 7.4, 25°C, sc-tPA
0.14
D-FPRANSN-C2H5-C2H5
-
pH 7.4, 25°C, sc-tPA
1.6
D-FPRANSN-C2H5-C2H5
-
pH 7.4, 25°C, ratio tc/sc
0.25
D-FPRANSN-H-t-C4H9
-
pH 7.4, 25°C, sc-tPA
0.94
D-FPRANSN-H-t-C4H9
-
pH 7.4, 25°C, tc-tPA
6.08
D-FPRANSN-H-t-C4H9
-
pH 7.4, 25°C, tc-tPA
0.32
D-FPRANSNH-c-C6H11
-
pH 7.4, 25°C, tc-tPA
2.1
D-FPRANSNH-c-C6H11
-
pH 7.4, 25°C, ratio tc/sc
0.27
D-FPRANSNH-C2H4OCH3
-
pH 7.4, 25°C, sc-tPA
0.66
D-FPRANSNH-C2H4OCH3
-
pH 7.4, 25°C, tc-tPA
2.4
D-FPRANSNH-C2H4OCH3
-
pH 7.4, 25°C, ratio tc/sc
6.08
D-FPRANSNH-C2H4OCH3
-
pH 7.4, 25°C, tc-tPA
0.54
D-FPRANSNH-C6H5CH2
-
pH 7.4, 25°C, tc-tPA
1.2
D-FPRANSNH-C6H5CH2
-
pH 7.4, 25°C, ratio tc/sc
6.08
D-FPRANSNH-C6H5CH2
-
pH 7.4, 25°C, tc-tPA
0.083
D-FPRANSNH-CH2COOCH3
-
pH 7.4, 25°C, sc-tPA
0.15
D-FPRANSNH-CH2COOCH3
-
pH 7.4, 25°C, tc-tPA
1.8
D-FPRANSNH-CH2COOCH3
-
pH 7.4, 25°C, ratio tc/sc
0.29
D-FPRANSNH-i-C3H7
-
pH 7.4, 25°C, sc-tPA
0.69
D-FPRANSNH-i-C3H7
-
pH 7.4, 25°C, ratio tc/sc
6.08
D-FPRANSNH-i-C3H7
-
pH 7.4, 25°C, ratio tc/sc
0.33
D-FPRANSNH-n-C4H9
-
pH 7.4, 25°C, tc-tPA
1.4
D-FPRANSNH-n-C4H9
-
pH 7.4, 25°C, ratio tc/sc
0.011
D-FVRANSNH-C2H5
-
pH 7.4, 25°C, sc-tPA
2.3
D-FVRANSNH-C2H5
-
pH 7.4, 25°C, ratio tc/sc
0.026
D-Ile-Pro-Arg-p-nitroanilide
-
value for tctPA, in the presence of stimulater Fibrin C (with cleaved C-terminal lysines)
0.027
D-Ile-Pro-Arg-p-nitroanilide
-
value for tctPA, in the presence of stimulater Fibrin normal
0.028
D-Ile-Pro-Arg-p-nitroanilide
-
value for tctPA, in the presence of stimulater Fibrin P (treated with plasmin-Sepharose)
0.0341
D-Ile-Pro-Arg-p-nitroanilide
-
value for sctPA, in the presence of stimulater Fibrin C (with cleaved C-terminal lysines)
0.086
D-Ile-Pro-Arg-p-nitroanilide
-
value for sctPA, in the presence of stimulater Fibrin P (treated with plasmin-Sepharose)
0.087
D-Ile-Pro-Arg-p-nitroanilide
-
value for sctPA, in the presence of stimulater Fibrin normal
7.3
D-Ile-Pro-Arg-p-nitroanilide
-
value for sctPA
10.7
D-Ile-Pro-Arg-p-nitroanilide
-
value for tctPA
0.034
D-LGR-ANSNH-C6H11
-
pH 7.4, 25°C, tc-tPA
4
D-LGR-ANSNH-C6H11
-
pH 7.4, 25°C, ratio tc/sc
0.0084
D-LGRANSNH-C6H11
-
pH 7.4, 25°C, sc-tPA
0.057
D-LGRANSNH-C6H11
-
pH 7.4, 25°C
0.061
D-LPRANSNH-C3H7
-
pH 7.4, 25°C, sc-tPA
0.17
D-LPRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
0.31
D-LPRANSNH-C3H7
-
pH 7.4, 25°C
2.8
D-LPRANSNH-C3H7
-
pH 7.4, 25°C, ratio tc/sc
0.019
D-LSRANSNH-C3H7
-
pH 7.4, 25°C, sc-tPA
0.1
D-LSRANSNH-C3H7
-
pH 7.4, 25°C, tc-tPA
5.3
D-LSRANSNH-C3H7
-
pH 7.4, 25°C, ratio tc/sc
0.021
D-VGRANSNH-C4H9
-
pH 7.4, 25°C, sc-tPA
0.19
D-VGRANSNH-C4H9
-
pH 7.4, 25°C, tc-tPA
9
D-VGRANSNH-C4H9
-
pH 7.4, 25°C, ratio tc/sc
0.059
D-VPRANSNH-C4H9
-
pH 7.4, 25°C, sc-tPA
0.16
D-VPRANSNH-C4H9
-
pH 7.4, 25°C, tc-tPA
0.7 - 1
D-VPRANSNH-C4H9
-
pH 7.4, 25°C
0.71
D-VPRANSNH-C4H9
-
pH 7.4, 25°C
2.7
D-VPRANSNH-C4H9
-
pH 7.4, 25°C, ratio tc/sc
0.0005
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422E/R275E, single-chain form, absence of soluble fibrin
-
0.0008
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422G/R275E, single-chain form, absence of soluble fibrin
-
0.001
Lys-plasminogen
-
pH 7.2, 37°C, mutant S421G/R275E, single-chain form, absence of soluble fibrin
-
0.0015
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422E, two-chain form, absence of soluble fibrin
-
0.002
Lys-plasminogen
-
pH 7.2, 37°C, mutant L420E/R275E and S421E/R275E, single-chain form, absence of soluble fibrin
-
0.0028
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422G, two-chain form, absence of soluble fibrin
-
0.003
Lys-plasminogen
-
pH 7.2, 37°C, mutant F423E/R275E, single-chain form, absence of soluble fibrin
-
0.004
Lys-plasminogen
-
pH 7.2, 37°C, mutant F423A/R275E, single-chain form, absence of soluble fibrin
-
0.005
Lys-plasminogen
-
pH 7.2, 37°C, mutant L420E, two-chain form, absence of soluble fibrin
-
0.007
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422A/R275E, single-chain form, absence of soluble fibrin
-
0.008
Lys-plasminogen
-
pH 7.2, 37°C, mutant L420A/R275E, single-chain form, absence of soluble fibrin
-
0.014
Lys-plasminogen
-
pH 7.2, 37°C, mutant L420A, two-chain form, absence of soluble fibrin
-
0.016
Lys-plasminogen
-
pH 7.2, 37°C, mutant S421E, two-chain form, absence of soluble fibrin
-
0.017
Lys-plasminogen
-
pH 7.2, 37°C, mutant F423E, two-chain form, absence of soluble fibrin
-
0.018
Lys-plasminogen
-
pH 7.2, 37°C, mutant S421G, two-chain form, absence of soluble fibrin
-
0.02
Lys-plasminogen
-
pH 7.2, 37°C, mutant F423A, two-chain form, absence of soluble fibrin
-
0.024
Lys-plasminogen
-
pH 7.2, 37°C, mutant R275E, single-chain form, absence of soluble fibrin
-
0.028
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422A, two-chain form, absence of soluble fibrin
-
0.068
Lys-plasminogen
-
pH 7.2, 37°C, wild-type, two-chain form, absence of soluble fibrin
-
0.1
Lys-plasminogen
-
pH 7.2, 37°C, wild-type, two-chain form, presence of soluble fibrin
-
0.11
Lys-plasminogen
-
pH 7.2, 37°C, mutant S421G and P422A, two-chain form, presence of soluble fibrin
-
0.12
Lys-plasminogen
-
pH 7.2, 37°C, two-chain form of mutant F423A, presence of soluble fibrin
-
0.13
Lys-plasminogen
-
pH 7.2, 37°C, mutant R275E, single-chain form, presence of soluble fibrin
-
0.15
Lys-plasminogen
-
pH 7.2, 37°C, two-chain form of mutant S421E, P422E and P422G, single chain form of mutant L420E/R275E, P422A/R275E and F423E/R275E, presence of soluble fibrin
-
0.17
Lys-plasminogen
-
pH 7.2, 37°C, two-chain form of mutant L420E and L420A, single chain form of mutant P422E/R275E, presence of soluble fibrin
-
0.18
Lys-plasminogen
-
pH 7.2, 37°C, two-chain form of mutant F423E, single-chain form of mutant L420A/R275E, presence of soluble fibrin
-
0.19
Lys-plasminogen
-
pH 7.2, 37°C, mutant S421G/R275E, single-chain form, presence of soluble fibrin
-
0.2
Lys-plasminogen
-
pH 7.2, 37°C, mutant F423A/R275E, single-chain form, presence of soluble fibrin
-
0.21
Lys-plasminogen
-
pH 7.2, 37°C, mutant P422G/R275E and S421E/R275E, single-chain form, presence of soluble fibrin
-
0.0025
plasminogen
-
pH 7.4, 37°C, absence of fibrinogen
-
0.06
plasminogen
-
pH 7.4, 37°C
-
0.1149
plasminogen
-
in the presence of bovine serum albumin
-
0.2
plasminogen
-
without fibrin and activated with fibrin
-
0.231
plasminogen
-
in the presence of beta2-glycoprotein I
-
0.4718
plasminogen
-
in the presence of beta2-glycoprotein I domain V
-
2 - 8
spectrozyme tPA
-
pH 7.2, 37°C, mutant F423E/R275E, single chain form
3 - 6
spectrozyme tPA
-
pH 7.2, 37°C, mutant S421G, two-chain form
14
spectrozyme tPA
-
pH 7.2, 37°C, mutant P422G/R275E, single chain form
23
spectrozyme tPA
-
pH 7.2, 37°C, mutant S421G/R275E, single chain form
26
spectrozyme tPA
-
pH 7.2, 37°C, mutant S421E/R275E, single chain form
27
spectrozyme tPA
-
pH 7.2, 37°C, mutant F423A/R275E, single chain form
29
spectrozyme tPA
-
pH 7.2, 37°C, mutant L420E/R275E, single chain form
31
spectrozyme tPA
-
pH 7.2, 37°C, mutant P422E/R275E, single chain form
32
spectrozyme tPA
-
pH 7.2, 37°C, mutant P422A/R275E, single chain form
33
spectrozyme tPA
-
pH 7.2, 37°C, mutant R275E, single chain form
42
spectrozyme tPA
-
pH 7.2, 37°C, mutant L420A/R275E, single chain form
45
spectrozyme tPA
-
pH 7.2, 37°C, mutant L420A, L420E, two-chain form
46
spectrozyme tPA
-
pH 7.2, 37°C, mutant S421E, two-chain form
47
spectrozyme tPA
-
pH 7.2, 37°C, wild-type t-PA, mutant P422A, two-chain form
49
spectrozyme tPA
-
pH 7.2, 37°C, mutant L420A/R275E, two-chain form
57
spectrozyme tPA
-
pH 7.2, 37°C, mutant F423E, two-chain form
60
spectrozyme tPA
-
pH 7.2, 37°C, mutant P422E, F423A, two-chain form
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0.0039
2-([6-[(3'-carbamimidoylbiphenyl-3-yl)oxy]-3,5-difluoro-4-methylpyridin-2-yl]oxy)-4-(dimethylamino)benzoic acid
Homo sapiens
pH 7.4-8.3, 37°C
0.022
2-[(6-[[3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
Homo sapiens
pH 7.4-8.3, 37°C
0.03
2-[(6-[[5-amino-3'-(aminomethyl)biphenyl-3-yl]oxy]-3,5-difluoropyridin-2-yl)oxy]-4-methylbenzoic acid
Homo sapiens
pH 7.4-8.3, 37°C
0.0036
4-(2-aminoethoxy)-N-[3-chloro-2-ethoxy-5-(piperidin-1-yl)phenyl]-3,5-dimethylbenzamide
Homo sapiens
pH 7.4-8.3, 37°C
0.1
4-[(E)-(5-oxo-2-phenyl-1,3-oxazol-4(5H)-ylidene)methyl]benzenecarboximidamide
Homo sapiens
pH 7.4-8.3, 37°C
0.062
6-carbamimidoyl-N-(3,5-dimethoxyphenyl)-2-naphthamide
Homo sapiens
pH 7.4-8.3, 37°C
0.125
6-carbamimidoyl-N-phenyl-2-naphthamide
Homo sapiens
pH 7.4-8.3, 37°C
0.0053
6-methoxy-N-(3'-(trifluoromethyl)biphenyl-4-yl)-2-naphthamide
Homo sapiens
pH 7.4-8.3, 37°C
0.013
6-methoxy-N-(3'-(trifluoromethyl)biphenyl-4-yl)naphthalene-2-sulfonamide
Homo sapiens
pH 7.4-8.3, 37°C
0.021
6-methoxy-N-(3'-methoxybiphenyl-4-yl)-2-naphthamide
Homo sapiens
pH 7.4-8.3, 37°C
0.0086
6-methoxy-N-(3'-nitrobiphenyl-4-yl)-2-naphthamide
Homo sapiens
pH 7.4-8.3, 37°C
0.0061
bis[(phenylamino)acetyl] [2-(4-carbamimidamidophenyl)-1-[(methoxycarbonyl)amino]ethyl]phosphonate
Homo sapiens
pH 7.4-8.3, 37°C
0.0000289
Chi-tPA 1
Homo sapiens
pH 7.4-8.5, 37°C, recombinant chimeric enzyme
-
0.0000223
Chi-tPA 2
Homo sapiens
pH 7.4-8.5, 37°C, recombinant chimeric enzyme
-
0.000197
Chi-tPA 3
Homo sapiens
pH 7.4-8.5, 37°C, recombinant chimeric enzyme
-
0.0002
Chi-tPA 4
Homo sapiens
pH 7.4-8.5, 37°C, recombinant chimeric enzyme
-
0.00021
Chi-tPA 5
Homo sapiens
pH 7.4-8.5, 37°C, recombinant chimeric enzyme
-
0.023
diphenyl [2-(4-carbamimidamidophenyl)-1-[(methoxycarbonyl)amino]ethyl]phosphonate
Homo sapiens
pH 7.4-8.3, 37°C
0.011
methyl 4'-(6-carbamoyl-2-naphthamido)biphenyl-3-carboxylate
Homo sapiens
pH 7.4-8.3, 37°C
0.0084
methyl 4'-(6-methoxy-2-naphthamido)biphenyl-3-carboxylate
Homo sapiens
pH 7.4-8.3, 37°C
0.026
methyl 4'-(6-methoxynaphthalene-2-sulfonamido)biphenyl-3-carboxylate
Homo sapiens
pH 7.4-8.3, 37°C
0.062
N-(4-(aminomethyl)phenyl)-6-carbamimidoyl-2-naphthamide trifluoro acetate
Homo sapiens
pH 7.4-8.3, 37°C
0.0097
N2-(2,4'-dimethoxybiphenyl-4-yl)naphthalene-2,6-dicarboxamide
Homo sapiens
pH 7.4-8.3, 37°C
0.0034
N2-(3'-(trifluoromethyl)biphenyl-4-yl)naphthalene-2,6-dicarboxamide
Homo sapiens
pH 7.4-8.3, 37°C
0.0057
N2-(3'-methoxybiphenyl-4-yl)naphthalene-2,6-dicarboxamide
Homo sapiens
pH 7.4-8.3, 37°C
additional information
xenon
additional information
xenon
Homo sapiens
although xenon at 25% (v/v) has no effect, xenon at higher concentrations of 37.5, 50 and 75% inhibit the catalytic efficiencies of human enzyme, IC50 is 34.85% (v/v)
additional information
xenon
Homo sapiens
-
although xenon at 25% (v/v) has no effect, xenon at higher concentrations of 37.5, 50 and 75% inhibit the catalytic efficiencies of human enzyme, IC50 is 34.85% (v/v)
additional information
xenon
Rattus norvegicus
-
although xenon at 25% (v/v) has no effect, xenon at higher concentrations of 37.5, 50 and 75% inhibit the catalytic efficiencies of murine enzyme, IC50 is 37.39% (v/v)
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evolution
human tissue plasminogen activator belongs to the serine protease family
malfunction
-
decreased serotonin levels associated with behavioral disinhibition in tissue plasminogen activator deficient -/- mice, the tPA-/- mice demonstrate an enhanced tendency to actively explore and engage in behaviors involving more exposure in the open field, O-maze and elevated plus maze
malfunction
-
the concentrations of t-PA and PAI-1 in the plasma have been identified as variables contributing to the risk of arterial thrombosis
malfunction
-
altered tPA activity levels in mouse models of Alzheimer's disease and spinocerebellar ataxia type-1, SCA1. Decreased tPA activity is detected in the cortex and subcortex of Alzheimer's disease mice, whereas increased tPA activity is found in the cerebellum of SCA1 mice
malfunction
-
tissue-plasminogen activator and plasminogen activator inhibitor, PAI-1, polymorphisms play a role in myocardial infarction within the Pakistanian population. The PAI-1 gene polymorphism has a gender specific role in the female myocardial infarction patients
malfunction
tPA-deficient ALBPLG1 mice show no difference in survival, bacterial dissemination or the pathology of GAS infection in the absence of tPA in AlbPLG1/tPA-/- mice compared to wild-type AlbPLG1 mice
malfunction
-
altered tPA activity levels in mouse models of Alzheimer's disease and spinocerebellar ataxia type-1, SCA1. Decreased tPA activity is detected in the cortex and subcortex of Alzheimer's disease mice, whereas increased tPA activity is found in the cerebellum of SCA1 mice
-
metabolism
-
tissue-type plasminogen activator functions as the main activator of the fibrinolytic process in the intravascular compartment
metabolism
the plasminogen-plasmin (PLG-PLA) system plays a role in thrombolysis, being capable of degrading blood clots. THe system consists of plasminogen, the inactive zymogen produced principally in the liver, its activators (tissue plasminogen activator, tPA and uroquinase plasminogen activator, uPA (EC 3.4.21.73)), their inhibitors (belonging to the serpin gene superfamily, named PAI-1, PAI-2, PAI-3 and protease nexin I), the uPA receptor and, finally, the active enzyme plasmin and its inhibitor, alpha-antiplasmin (alpha-PL). Apart from its fibrinolytic function, the PLG-PLA system is important in degrading the extracellular matrix in multiple tissues contributing to cell migration, angiogenesis, tissue repair and remodelling or tumour invasion
metabolism
urokinase-type plasminogen activator (uPA) and tissue-type plasminogen activator (tPA) are two serine proteases that contribute to initiating fibrinolysis by activating plasminogen. uPA is also an important tumour-associated protease due to its role in extracellular matrix remodelling
metabolism
-
the plasminogen-plasmin (PLG-PLA) system plays a role in thrombolysis, being capable of degrading blood clots. THe system consists of plasminogen, the inactive zymogen produced principally in the liver, its activators (tissue plasminogen activator, tPA and uroquinase plasminogen activator, uPA (EC 3.4.21.73)), their inhibitors (belonging to the serpin gene superfamily, named PAI-1, PAI-2, PAI-3 and protease nexin I), the uPA receptor and, finally, the active enzyme plasmin and its inhibitor, alpha-antiplasmin (alpha-PL). Apart from its fibrinolytic function, the PLG-PLA system is important in degrading the extracellular matrix in multiple tissues contributing to cell migration, angiogenesis, tissue repair and remodelling or tumour invasion
-
physiological function
-
enzyme is a serine protease
physiological function
-
serine protease
physiological function
serine protease
physiological function
-
serine protease, which converts plasminogen into plasmin, which in turn degrades fibrin and other extracellular matrix components, tPA plays an important role in the processes of learning and memory, demonstrated at the level of behavior and synaptic plasticity, role in neurodegeneration
physiological function
tissue plasminogen activator and plasminogen activator inhibitor type 1 are the major regulators of plasmin generation, tissue plasminogen activator plays a pivotal role in the fibrinolytic system by converting the proenzyme plasminogen into the active enzyme plasmin
physiological function
-
tissue-type plasminogen activator is a serine protease that converts plasminogen into the active enzyme plasmin, which in turn degrades the fibrin of the forming thrombus
physiological function
-
antiangiogenic activity can be elicited by the kringle domains 1 and 2 of tissue-type plasminogen activator, TK12, or the kringle 2 domain alone, overview. The anti-migratory effect of TK12 is mediated in part by its interference with integrin alpha2beta1, which is blocked by the Asp-Gly-Glu-Ala, DGDA, amino acid sequence, the DGDA peptide alone shows antiangiogenic activity and effectively inhibites VEGF-induced migration of HUVECs
physiological function
-
despite its pro-fibrinolytic activity, tPA is a serine protease known to influence a number of physiological and pathological functions in the central nervous system. Accordingly, tPA mediates some of its functions in the central nervous system through N-methyl-D-aspartate receptors, low-density lipoprotein receptor-related protein, or annexin II. tPA can mediate proteolysis and subsequent delocalization of neuronal nitric oxide synthase, nNOS, thereby reducing endogenous neuronal nitric oxide release, independent of NMDA receptors, calpains, and low-density lipoprotein receptor-related proteins. tPA promotes proteolysis of nNOS through a plasmin-dependent mechanism, which is prevented in the presence of aprotinin and alpha2-antiplasmin, two blockers of the proteolytic activity of plasmin, overview
physiological function
-
ethanol exposure during developmental synaptogenesis can lead to brain defects referred to as fetal alcohol syndrome, which can include mental health problems such as cognitive deficits and mental retardation. Tissue plasminogen activator is implicated in neurodegeneration and is a critical signaling component in FAS. In wild-type mice, ethanol elicits caspase-3 activation, significant forebrain neurodegeneration, and decreases contextual fear conditioning in adults. However, tPA-deficient mice are protected from these neurotoxicities, and this protection can be abrogated by exogenous tPA. The effects of tPA are mediated by the NR2B subunit of the NMDA receptor, but tPA catalytic activity Is not required to promote ethanol-induced neurodegenration
physiological function
-
human tissue-plasminogen activator is a thrombolytic protein that plays an active role in dissolving fibrin clots by fibrinolysis and in activating plasminogen to plasmin in blood vessels
physiological function
-
mechanism of action of tPA on oligodendrocyte survival and on the extent of white matter lesions in stroke, overview. tPA protects oligodendrocytes from apoptosis through an unexpected cytokine-like effect by the virtue of its epidermal growth factor-like domain, and tPA protects white matter from stroke-induced lesions. Aging differentially influences gray and white matter susceptibility to stroke. tPA, via extracellular regulated kinase 1/2 and Akt intracellular pathways, regulates the balance between proand antiapoptotic factors and reduces the activity of caspase 3
physiological function
-
mechanism of action of tPA on oligodendrocyte survival and on the extent of white matter lesions in stroke, overview. tPA protects oligodendrocytes from apoptosis through an unexpected cytokine-like effect by the virtue of its epidermal growth factor-like domain, and tPA protects white matter from stroke-induced lesions. Aging differentially influences gray and white matter susceptibility to stroke. tPA, via extracellular regulated kinase 1/2 and Akt intracellular pathways, regulates the balance between proand antiapoptotic factors and reduces the activity of caspase 3
physiological function
-
regulatory mechanism of the plasminogen activator system in astrocytes, overview
physiological function
-
the interplay between tissue plasminogen activator domains and fibrin structures plays a role in the regulation of fibrinolysis, kinetics, overview. The regulation of fibrinolysis depends on the starting nature of fibrin fibers and complex dynamic interaction between tPA and fibrin structures that vary over time. Fine fibrin is a better surface for plasminogen activation but more resistant to lysis
physiological function
-
the Kringle-2 domain, residues 176-262 of TPA, is the essential structure required for the brain-protective activity of TPA, employing the rat middle cerebral artery occlusion, MCAO, model. The Kringle-2 domain of tissue plasminogen activator significantly reduces mortality and brain infarction in middle cerebral artery occlusion rats. Tissue plasminogen activator shows brainprotective activity within the first 15 min after cerebral ischemia in rats
physiological function
-
tissue plasminogen activator is a secreted serine protease and is also proepileptic and excitotoxic. Wild-type tPA and S481A catalytically inactive tPA mutant mediate zinc uptake via the zinc influx transporter, ZIP4, overview. ZIP4 is upregulated after excitotoxin stimulation of the mouse, male and female, hippocampus. ZIP4 physically interacts with tPA, correlating with an increased intracellular zinc influx and lysosomal sequestration. This sequestration might result in neuroprotection. tPA mutants with deletion of the second kringle domain, DELTAK2, or deletion of the growth factor domain, DELTAGF, are less effective
physiological function
-
tissue plasminogen activator is a thrombolytic protein that plays a key role in fibrinolysis by converting the plasminogen into plasmin which degrades fibrin clots in blood vessels
physiological function
-
tissue plasminogen activator, t-PA, plays a pivotal role in the treatment of acute myocardial infarction, ischemic stroke, and deep vein thrombosis
physiological function
-
tissue plasminogen activator, tPA, and its inhibitors contribute to neurite outgrowth in the central nervous system after treatment of stroke with multipotent mesenchymal stromal cells. Critical role of tPA in facilitating neurite outgrowth. Bone marrow stromal cells modulate endogenous tPA level and activity in the ischemic boundary zone, IBZ
physiological function
-
tissue plasminogen activator, tPA, is the primary source of plasminogen activator in the brain, and is a member of the fibrinolytic system and a serine protease that converts the zymogen plasminogen into the active protease plasmin, and thus cleaves fibrin and dissolves newly formed clots. Bone marrow stromal cells significantly improve functional recovery from stroke dependent on tPA function, overview. In tPA knockout mice, no bone marrow stromal cell effect is observed on functional recovery
physiological function
-
tissue type plasminogen activator regulates myeloid-cell dependent neoangiogenesis during tissue regeneration. Serpin-resistant form of tPA expands the myeloid cell pool and mobilizes CD45+ CD11b+ proangiogenic, myeloid cells, by activating the extracellular proteases matrix metalloproteinase-9 and plasmin, a process dependent on vascular endothelial growth factor-A and Kit ligand signaling. tPA improves the incorporation of CD11b+ cells into ischemic tissues and increases expression of neoangiogenesis-related genes, including VEGF-A, kinetics and mechanism, overview. tPA can induce cell migration by binding to CD11b and degrading fibrin. Batroxobin, a drug that reduces circulating fibrinogen, prevents the tPA-mediated WBC and CD11b+ cell increase. Inhibition of VEGF signaling suppresses tPA-induced neovascularization in a model of hind limb ischemia
physiological function
-
tPA is a pivotal player in slowly progressing activity deprivation-induced neurodegeneration, e.g. induced by blockade of neuronal activity using tetrodotoxin, TTX. Neurons degenerate slowly and die in a manner resembling neurodegenerative diseases-induced neuronal cell death. Transfection of an endogenous tPA inhibitor, plasminogen activator inhibitor-1, protected the TTX-exposed neurons from dying
physiological function
-
tPA is an initiator of intravascular fibrinolysis and is a complex mediator of brain function and dysfunction. tPA participates in various forms of chronic neurodegeneration, and plays a functional role following morphine administration, epileptic seizures, traumatic brain injury and ischaemic stroke-neurological settings
physiological function
-
tPA potentiates excitotoxicity by interacting with and cleaving the N-terminal end of the NR1 subunit of N-methyl-D-aspartate receptors, leading to an increased calcium influx, Erk1/2 activation, and neurotoxicity, mechanism, overview
physiological function
-
tPA shows fibrinolytic activity and is used for fibrin clot-lysis
physiological function
the enzyme may directly interact with NR2B subunits of N-methyl-D-aspartate receptors leading to a change in pharmacological properties of NR2B-containing NMDA receptors
physiological function
the human tissue plasminogen activator is a serine protease known as the key component of the fibrinolytic system. t-PA converts the proenzyme plasminogen to plasmin, which in turn mediates the degradation of fibrin
physiological function
plasmin(ogen) acquisition is critical for invasive disease initiation by Streptococcus pyogenes (GAS), limited role of tissue-type plasminogen activator in a mouse model of Group A streptococcal infection
physiological function
tissue plasminogen activator (tPA) of paternal origin is necessary for the success of in vitro but not of in vivo fertilisation in the mouse. The presence of exogenous plasminogen drastically reduces the fertilisation rate under in vitro conditions. When plasminogen is present in combination with inhibitors (e.g. alpha-PL or EACA), the fertilisation rate is partially restored
physiological function
tissue-type plasminogen activator (tPA) is a serine protease that plays a crucial role in the fibrinolytic system
physiological function
-
the Kringle-2 domain, residues 176-262 of TPA, is the essential structure required for the brain-protective activity of TPA, employing the rat middle cerebral artery occlusion, MCAO, model. The Kringle-2 domain of tissue plasminogen activator significantly reduces mortality and brain infarction in middle cerebral artery occlusion rats. Tissue plasminogen activator shows brainprotective activity within the first 15 min after cerebral ischemia in rats
-
physiological function
-
regulatory mechanism of the plasminogen activator system in astrocytes, overview
-
physiological function
-
tPA potentiates excitotoxicity by interacting with and cleaving the N-terminal end of the NR1 subunit of N-methyl-D-aspartate receptors, leading to an increased calcium influx, Erk1/2 activation, and neurotoxicity, mechanism, overview
-
physiological function
-
tissue plasminogen activator (tPA) of paternal origin is necessary for the success of in vitro but not of in vivo fertilisation in the mouse. The presence of exogenous plasminogen drastically reduces the fertilisation rate under in vitro conditions. When plasminogen is present in combination with inhibitors (e.g. alpha-PL or EACA), the fertilisation rate is partially restored
-
physiological function
-
mechanism of action of tPA on oligodendrocyte survival and on the extent of white matter lesions in stroke, overview. tPA protects oligodendrocytes from apoptosis through an unexpected cytokine-like effect by the virtue of its epidermal growth factor-like domain, and tPA protects white matter from stroke-induced lesions. Aging differentially influences gray and white matter susceptibility to stroke. tPA, via extracellular regulated kinase 1/2 and Akt intracellular pathways, regulates the balance between proand antiapoptotic factors and reduces the activity of caspase 3
-
physiological function
-
tPA is an initiator of intravascular fibrinolysis and is a complex mediator of brain function and dysfunction. tPA participates in various forms of chronic neurodegeneration, and plays a functional role following morphine administration, epileptic seizures, traumatic brain injury and ischaemic stroke-neurological settings
-
physiological function
-
tissue type plasminogen activator regulates myeloid-cell dependent neoangiogenesis during tissue regeneration. Serpin-resistant form of tPA expands the myeloid cell pool and mobilizes CD45+ CD11b+ proangiogenic, myeloid cells, by activating the extracellular proteases matrix metalloproteinase-9 and plasmin, a process dependent on vascular endothelial growth factor-A and Kit ligand signaling. tPA improves the incorporation of CD11b+ cells into ischemic tissues and increases expression of neoangiogenesis-related genes, including VEGF-A, kinetics and mechanism, overview. tPA can induce cell migration by binding to CD11b and degrading fibrin. Batroxobin, a drug that reduces circulating fibrinogen, prevents the tPA-mediated WBC and CD11b+ cell increase. Inhibition of VEGF signaling suppresses tPA-induced neovascularization in a model of hind limb ischemia
-
physiological function
-
tissue plasminogen activator is a secreted serine protease and is also proepileptic and excitotoxic. Wild-type tPA and S481A catalytically inactive tPA mutant mediate zinc uptake via the zinc influx transporter, ZIP4, overview. ZIP4 is upregulated after excitotoxin stimulation of the mouse, male and female, hippocampus. ZIP4 physically interacts with tPA, correlating with an increased intracellular zinc influx and lysosomal sequestration. This sequestration might result in neuroprotection. tPA mutants with deletion of the second kringle domain, DELTAK2, or deletion of the growth factor domain, DELTAGF, are less effective
-
physiological function
-
tissue plasminogen activator, tPA, is the primary source of plasminogen activator in the brain, and is a member of the fibrinolytic system and a serine protease that converts the zymogen plasminogen into the active protease plasmin, and thus cleaves fibrin and dissolves newly formed clots. Bone marrow stromal cells significantly improve functional recovery from stroke dependent on tPA function, overview. In tPA knockout mice, no bone marrow stromal cell effect is observed on functional recovery
-
additional information
-
alteplase is the full-length recombinant human TPA, while reteplase, K2P, is the domain deletion mutant comprising only the Kringle-2 domain and protease domain of TPA. Reteplase shows a better protective effect than alteplase, suggesting that F, P, or K1 domain in TPA diminishes the brain-protective effect
additional information
-
production of active K2S in Escherichia coli without the requirements of in vitro refolding process, method optimization, overview
additional information
-
t-PA is a serine-protease enzyme containing 527 amino acid residues in five structural domains
additional information
-
the DGDA sequence presents a functional epitope of TK12 and can be used as a potential novel antiangiogenic peptide
additional information
-
the synthetic deca-peptide corresponding to the amino acid sequence Arg54-Trp63 of human tissue-type plasminogen activator kringle 2 domain, i.e. TKII-10, effectively inhibits VEGF-stimulated HUVECs migration and tube formation, but it demonstrats no inhibitory effect on VEGF-stimulated HUVECs proliferation, overview. TKII-10 effectively inhibits angiogenesis in vivo
additional information
tPA is active in solution
additional information
-
tPA is active in solution
additional information
-
alteplase is the full-length recombinant human TPA, while reteplase, K2P, is the domain deletion mutant comprising only the Kringle-2 domain and protease domain of TPA. Reteplase shows a better protective effect than alteplase, suggesting that F, P, or K1 domain in TPA diminishes the brain-protective effect
-
additional information
-
tPA is active in solution
-
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147000
-
by Western blot analysis or by anti-GFP antibody, tPA-GFP-plasminogen activator inhibitor-1 complex
20000
-
two-kringle domain mutant N117Q/N184Q, monomer, SDS-PAGE
21590
monomer, kringle domain of tissue-type plasminogen activator, glycosylated, MALDI analysis
23940
monomer, kringle domain of tissue-type plasminogen activator, glycosylated, MALDI analysis
28126
-
1 * 30882 + 1 * 28126, human, calculation from amino acid sequence
30882
-
1 * 30882 + 1 * 28126, human, calculation from amino acid sequence
32000
single-chain tPA, monomer, SDS-PAGE
39590
-
human, recombinant domain-deletion mutant BM 06.022, calculation from amino acid sequence
53000
-
x * 63000, full-length t-PA, SDS-PAGE, x * 53000, truncated 650 bp t-PA, SDS-PAGE
59010
-
human, calculation from amino acid sequence
60000
-
naked tPA amino acid chain
60800
recombinant soluble detagged enzyme, gel filtration
63000
-
x * 63000, full-length t-PA, SDS-PAGE, x * 53000, truncated 650 bp t-PA, SDS-PAGE
63500
x * 63500, SDS-PAGE
66000
-
mouse, gel filtration
69000 - 72000
-
human, gel filtration
72000
-
x * 72000, wild-type enzyme
75000
x * 75000, recombinant chimeric enzyme mutant, SDS-PAGE, x * 70000, wild-type t-PA, SDS-PAGE, the wild-type enzyme holds five domains including finger, epidermal growth factor, kringle 1, kringle 2 and protease
80000
-
mass spectroscopy, SDS-PAGE
9556
-
calculated from amino acid sequence
19950
monomer, kringle domain of tissue-type plasminogen activator, calculated from amino acid sequence
19950
-
two-kringle domain mutant N117Q/N184Q, monomer, mass spectroscopy
59000
-
x * 59000, recombinant enzyme, SDS-PAGE
59000
-
x * 59000, recombinant t-PA, SDS-PAGE
65000
-
human, sedimentation equilibrium, one-chain form
65000
two-chain tPA, monomer, SDS-PAGE
68000
-
natively glycosylated tPA
68000
-
casein zymography or gel filtration
68000
x * 68000, recombinant enzyme, SDS-PAGE
70000
-
x * 70000, human, SDS-PAGE
70000
x * 75000, recombinant chimeric enzyme mutant, SDS-PAGE, x * 70000, wild-type t-PA, SDS-PAGE, the wild-type enzyme holds five domains including finger, epidermal growth factor, kringle 1, kringle 2 and protease
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F423A
-
two chain form, site-directed mutagenesis
F423A/R275E
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single-chain form, site-directed mutagenesis
F423E
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two chain form, site-directed mutagenesis
F423E/R275E
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single-chain form, site-directed mutagenesis
K213A/H214A/R215A/R216A
construction of a chimeric tissue plasminogen activator (t-PA) through kringle 2 domain removal and replacement of t-PA finger domain with the Vampire bat plasminogen activator one. Vampire bat plasminogen activator (b-PA) is a plasminogen activator with higher fibrin affinity and specificity in comparison to t-PA resulting in reduced probability of hemorrhage. b-PA is also resistant to plasminogen activator inhibitor-1 showing higher half-life compared to other variants of t-PA. The KHRR sequence at the initial part of protease domain is replaced by four alanine residues. The activity of therecombinant protein in the presence of fibrin is 1560 times more than its activity in the absence of fibrin, showing its higher specificity to fibrin. The chimeric enzyme shows 1.2fold higher fibrin binding in comparison to full-length enzyme
L420A
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two chain form, site-directed mutagenesis
L420A/R275E
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single-chain form, site-directed mutagenesis
L420E
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two chain form, site-directed mutagenesis
L420E/R275E
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single-chain form, site-directed mutagenesis
P422A
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two chain form, site-directed mutagenesis
P422A/R275E
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single-chain form, site-directed mutagenesis
P422E/R275E
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single-chain form, site-directed mutagenesis
P422G/R275E
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single-chain form, site-directed mutagenesis
R275E
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single-chain form, site-directed mutagenesis
R275E/P422E
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site-directed mutagenesis
R275E/P422G
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site-directed mutagenesis
S421E
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two chain form, site-directed mutagenesis
S421E/R275E
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single-chain form, site-directed mutagenesis
S421G
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two chain form, site-directed mutagenesis
S421G/R275E
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single-chain form, site-directed mutagenesis
S478A
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efficacy of expression of the mutant and wild-type is similar, but the mutant does not appear in the culture medium after 24 h either complexed with plasminogen activator inhibitor-1 or in the free form. Intracellular distribution is indistinguishable to the wild-type, but it is present at higher concentrations than the wild-type near the plasma membrane
S478A/C395A/N448Q
site-directed mutagenesis in the serine protease domain
N117Q/N184Q
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results in a non-glycosylated protein, inhibits endothelial cell proliferation and migration stimulated by bFGF and VEGF, respectively
S481A
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catalytically inactive tPA
S481A
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catalytically inactive tPA mutant
S481A
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catalytically inactive tPA mutant
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S478A
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non-proteolytic TPA full-length mutant
S478A
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non-proteolytic TPA full-length mutant
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additional information
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it is shown that tPA induces a rapid and transient phosphorylation of the epidermal growth factor receptor. Specific EGFR kinase inhibitors abolish the tPA induced phosphorylation of the extracellular activated kinases 1/2 and cell proliferation. Mitogenic activity of tPA is inhibited by siRNA depletion of EGFR, thus confirming the involvement of this receptor in tPA triggered signalling. It is shown that the signalling and mitogenic effects of tPA require its proteolytic activity, the activity of the metalloprotease-9 and active heparin binding-epidermal growth factor
additional information
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recombinant human tissue-type plasminogen activator derivative (r-PA) (deletion mutant lacking the 4th-175th amino acid residues of t-PA), fused with thioredoxin (Trx), is expressed in Escherichia coli. Trx-r-PA fusion protein is almost completely expressed in the form of inclusion bodies and without activity. An optimized on-column refolding process for Trx-r-PA inclusion bodies is established: The collected Trx-r-PA inclusion bodies are dissolved in 6 M guanidine hydrochloride, and the denatured protein is separated from dithiothreitol and guanidine hydrochloride with a G25 column and simultaneously dissolved in 8 M urea containing oxidized glutathione. Refolding of Trx-r-PA protein on Sephacryl S-200 column with a decreasing urea gradient combined with two-stage temperature control is employed, and the activity recovery of refolded protein is increased from 3.6 to 13.8% in comparison with the usual dilution refolding
additional information
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a synthetic deca-peptide corresponding to the amino acid sequence Arg54-Trp63 of human tissue-type plasminogen activator kringle 2 domain, named TKII-10, is produced and tested for its ability to inhibit endothelial cell proliferation, migration, tube formation in vitro, and angiogenesis in vivo. Another peptide TKII-10S, composed of the same 10 amino acids as TKII-10 but in a different sequence, is also produced and tested, showing that TKII-10 potently inhibits VEGF-stimulated endothelial cell migration and tube formation in a dose-dependent, as well as sequence-dependent manner in vitro while it is inactive in inhibiting endothelial cell proliferation. Furthermore, TKII-10 potently inhibits angiogenesis in chick chorioallantoic membrane and mouse cornea. The middle four amino acids DGDA in their sequence play an important role in TKII-10 angiogenesis inhibition
additional information
construction of a chimeric-truncated form of tissue-type plasminogen activator with improved fibrin affinity and resistance to plasminogen activator inhibitor-1
additional information
construction of a truncated form of the tissue plasminogen activator, K2S, which has a longer plasma half-life, better diffusion into the clot, and higher fibrinolytic activity
additional information
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construction of a truncated form of the tissue plasminogen activator, K2S, which has a longer plasma half-life, better diffusion into the clot, and higher fibrinolytic activity
additional information
construction of tissue plasminogen activator (tPA)-loaded iron oxide nanoparticles (SPIONDex-COOH-tPA) which can target blood clots via magnetic guidance and induce local fibrinolysis, overview. tPA is bound to the particles via adsorption or covalent binding due to a 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)/N-hydroxysuccinimide (NHS) ester. The hydrodynamic size of carboxymethylated SPIONs depends on covalently bound or adsorbed tPA. In case of covalent immobilization, the supernatants exhibit only minimal activity below 10%, while the supernatant of the adsorptive approach shows an activity of approx. 15% for all tPA concentrations. Analysis of biocompatibility of the particles
additional information
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construction of tissue plasminogen activator (tPA)-loaded iron oxide nanoparticles (SPIONDex-COOH-tPA) which can target blood clots via magnetic guidance and induce local fibrinolysis, overview. tPA is bound to the particles via adsorption or covalent binding due to a 1-ethyl-3-(3-dimethylaminopropyl) carbodiimide (EDC)/N-hydroxysuccinimide (NHS) ester. The hydrodynamic size of carboxymethylated SPIONs depends on covalently bound or adsorbed tPA. In case of covalent immobilization, the supernatants exhibit only minimal activity below 10%, while the supernatant of the adsorptive approach shows an activity of approx. 15% for all tPA concentrations. Analysis of biocompatibility of the particles
additional information
engineering on tPA to reduce its inhibition by PAI-1 without compromising its thrombolytic effect is a continuous effort
additional information
the activity of tPA is increased by splicing the active site of dodder-cuscutain gene to human tPA. The chimeric cDNA of tPA is constructed through splicing by overlap extension PCR (SOEing-PCR) method and transferred to the hairy roots of tobacco using different strains of Agrobacterium rhizogenes. Agrobacterium rhizogenes strain ATCC 15834 is the most favorable strain for the induction of hairy roots in tobacco, overview
additional information
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the activity of tPA is increased by splicing the active site of dodder-cuscutain gene to human tPA. The chimeric cDNA of tPA is constructed through splicing by overlap extension PCR (SOEing-PCR) method and transferred to the hairy roots of tobacco using different strains of Agrobacterium rhizogenes. Agrobacterium rhizogenes strain ATCC 15834 is the most favorable strain for the induction of hairy roots in tobacco, overview
additional information
the RGDS motif is fused to the enzyme's C-terminus. RGDS, as the binding motif of integrin, improves the specific affinity of the recombinant tPA to substrate. The similar diameter of the halo patterns of His-tag-PSP-tPA-RGDS and tPA-RGDS suggests that they exhibit similar amidolytic activities in vitro
additional information
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the RGDS motif is fused to the enzyme's C-terminus. RGDS, as the binding motif of integrin, improves the specific affinity of the recombinant tPA to substrate. The similar diameter of the halo patterns of His-tag-PSP-tPA-RGDS and tPA-RGDS suggests that they exhibit similar amidolytic activities in vitro
additional information
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mice double deficient for urokinase-type (uPA) and tissue-type plasminogen activator (tPA) show a substantial delay in wound healing compared to mice single deficient in either uPA or tPA
additional information
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compared with wild-type, apoptosis of interstitial myofibroblasts is increased in tPA-/- mice after obstructive injury
additional information
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mice in which the tPA gene has been disrupted do not show anxiety after repeated stress
additional information
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tPA knockout mice are protected against kainic acid-induced hippocampal damage and are resistant to focal cerebral ischemic injury. Exogenous tPA exacerbates ischemic injury in both wild-type and tPA-null mice
additional information
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construction of tPA knockout mice, and of transgenic T4 mice selectively overexpressing tPA in neurons
additional information
tPA-deficient ALBPLG1 mice show no difference in survival, bacterial dissemination or the pathology of GAS infection in the absence of tPA in AlbPLG1/tPA-/- mice compared to wild-type AlbPLG1 mice
additional information
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tPA-deficient ALBPLG1 mice show no difference in survival, bacterial dissemination or the pathology of GAS infection in the absence of tPA in AlbPLG1/tPA-/- mice compared to wild-type AlbPLG1 mice
additional information
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construction of tPA knockout mice, and of transgenic T4 mice selectively overexpressing tPA in neurons
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additional information
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a much lower uptake clearance is found in the liver for lanoteplase compared to wild-type t-PA. Rate constants for cell surface binding, internalization, and degradation of lanoteplase are also lower than those for t-PA in primary cultured rat hepatocytes. Results suggest that the improved stability of lanoteplase in vivo is due to the delay in the receptor-mediated endocytosis of lanoteplase. Uptake clearance in liver decreases with coadministration of lactoferrin, a ligand for low-density lipoprotein receptor-related protein (LRP) and the asialoglycoprotein receptors (ASGP) and in Irpap1-/- mice, which have a hereditary deficiency of lipoprotein receptor-related protein. Uptake clearance is not affected by mannose, whereas that of t-PA decreases with both ligands and in Irpap1(-/-) mice. Hepatic disposition of lanoteplase seems to be mediated by common specific receptors for t-PA, including LRP and the ASGP receptors
additional information
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disposition profile of lanoteplase, a recombinant mutant of t-PA, in vivo and the kinetics of receptor-mediated endocytosis of this recombinant t-PA in vitro is examined to kinetically characterize the mechanism underlying its tissue distribution and elimination
additional information
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reteplase is a bacterially expressed TPA deletion mutant comprising residues 176-527 of wild-type TPA. Plasminogen is activated to plasmin by reteplase, and then reteplase is completely cleaved by plasmin into a two-chain form, which is composed of Kringle-2 and P domain linked by a disulfide bond
additional information
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reteplase is a bacterially expressed TPA deletion mutant comprising residues 176-527 of wild-type TPA. Plasminogen is activated to plasmin by reteplase, and then reteplase is completely cleaved by plasmin into a two-chain form, which is composed of Kringle-2 and P domain linked by a disulfide bond
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additional information
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disseminated intravascular coagulation is induced in 27 neonatal pigs (7 to 14 days of age) by intravenous administration of Escherichia coli endotoxin (800 microgram/kg over 30 min). Pigletes are treated with A: supportive care alone, B: antithrombin III (50 microgram/kg bolus, 25 microgram/kg per h continuous infusion) and supportive care, C: recombinant tissue plasminogen activator (R-TPA, 25 mcrogram/kg per h continuous infusion) and supportive care; D: antithrombin III, R-TPA and supportive care. Compared with supportive care alone, combination therapy with antithrombin III and R-TPA results in a significant improvement of survival time, hematocrit, antithrombin III level, macroscopic and microscopic organ involvement. Compared with supportive care alone, R-TPA alone significantly reduces macroscopic organ involvement
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a truncated version of tPA is fused to the N terminus of the phasin protein with a thrombin cleavage site as the linker, and then expressed in Escherichia coli strain XL1-Blue on the surface of polyhydroxybutyrate granules using phasin as the affinity tag. Untreate enzyme is expressed in inactive inclusion bodies in the bacteria. The in vivo surface display strategy for functional rPA expression in Escherichia coli is distinct for its efficient folding and easier purification, method optimization, overview. Subcloning in Escherichia coli strain DH5alpha
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astrocytes co-transfected with metalloproteinase-9 or tPA luciferase reporter plasmid and pCMV-beta-galactosidase reporter plasmid
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cDNA expressed in Escherichia coli in the form of inclusion body
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construction of an oviduct-specific vector containing tissue plasminogen activator protein and green fluorescent protein (pL-2.8OVtPAGFP), and expression in vitro and in vivo in hen eggs, and in oviduct epithelial and 3T3 cells, compared to control vector pEGP-N1. The oviduct-specific vector pL-2.8OVtPAGFP is expressed only in oviduct epithelial cells, no detection in heart, muscle, liver and intestine, whereas pEGP-N1 is detected in oviduct epithelial and 3T3 cells. tPA expressed in egg white and oviduct epithelial cells shows fibrinolytic activity. Subcloning in Escherichia coli
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construction of plastid transformation vector pKCZK2S for expressing the K2S gene in Nicotiana tabacum chloroplast genome under the control of the constitutive Prrn promoter, and the 3' UTR of the Chlamydomonas rbcl gene as a terminator, recombinant expression of His6-tagged truncated form of the tissue plasminogen activator, K2S, in Nicotiana tabacum leaf chloroplasts
evaluation of expression methods, overview. Recombinant expression of active full-length and active truncated 650 bp enzymes in Nicotiana tabacum
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expressed in HeLa cells and MCF-7 cells
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expressed in SF9 cells using the Bac-to-Bac baculovirus system
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expression in Escherichia coli
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expression in Escherichia coli and Saccharomyces cerevisiae
functional expression under transcriptional control of single and multiple rooting loci promoter rolD promoters in hairy roots of Cucumis melon, the t-PA gene is integrated in the genome of hairy roots using Agrobacterium-mediated transformation of melon cotyledons. Highest levels of the recombinant t-PA accumulation in transgenic hairy roots carrying the t-PA transgene occur under the control of single and dual rolD promoters compared to triple and quadruple rolD promoters, method evaluation and optimization, overview
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gene K2S, expression of a His-tagged truncated enzyme form in Leishmania tarentolae using an expression cassette containing kringle 2 and serine protease domains, tissue plasminogen activator, together with a signal sequence derived from Leishmania tarentolae and two fragments of the small subunit ribosomal RNA locus. The recombinant enzyme is functional and secreted to the cell culture medium. Replacement of the human signal sequence tPA with the signal sequence derived from Leishmania increases the secretion of recombinant protein up to 30times
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gene PLAT, functional expression of His-tagged soluble full-length tPA, that contains multiple disulfide bonds and the RGDS, as the integrin binding motif, fused in C-terminus, on an industrial scale using autoinduction in Escherichia coli strains BL21 (DE3), Rosetta, and Origami 2, method optimization and evaluation, overview. Strain Origami 2 can increase disulfide bond formation in cytoplasmic tPA and produce purified soluble recombinant protein
gene PLAT, recombinant human tPA (residue 297-562) is expressed in Expi293 cells
heterologously expressed in the methylotrophic yeast Pichia pastoris GS115
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high-level expression of the kringle 2 plus serine protease domains, K2S, of human tissue plasminogen activator in Escherichia coli strain BL21 as active fusion protein, in which the His-tagged K2S domains are fused to the disulfide isomerase DsbC from Escherichia coli, the recombinant fusion protein is soluble. The active K2S domains are liberated by cleavage through factor Xa. Subcloning in Escherichia coli strain DH5alpha
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hybridoma cell lines expressing Mabs 364, 623, 663, and 700, all directed to wtr-K2 tPA, cDNA cloning, recombinant kringle 2 domain r-K2 tPA expressed in Pichia pastoris cells
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hybridoma cell lines expressing Mabs expression of wild-type and mutant enzyme cDNA by transient transfection of COS cells
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nucleoprotein derived from H5N1 influenza virus fused with a tPA signal sequence, amplified, digested with Hind III and XhoI, cloned into pVAX1 and transfected into Vero cells. 293T cells transiently transfected with ptPAs/nucleoprotein
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recobinant expression of wild-type and mutant enzymes in Pichia pastoris strain GS115, cloning in Escherichia coli strain Top10F
recombinant expression and large-scale production of biochemically active wild-type human enzyme and os a synthetic enzyme in hairy roots of Cucumis melo cv. Geumssaragi-euncheon using binary vector p221 and Agrobacterium rhizogenes strain K599-mediated transformation of cotyledons, method evaluation, overview. WPM medium is found to be more suitable for rapid growth of hairy roots among all the seven media types tested, total yield of hairy roots grown on WPM medium is 621.8 g/L at pH 7.0
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recombinant expression of active and soluble enzyme in leaves of Nicotiana tabacum cv. Xathi under the control of CaMV35S promoter and NOS terminator and with high-expression Kozak sequence and KDEL signal for endoplasmic reticulum retention linked to N- and C-termini of t-PA gene, respectively, using the Agrobacterium tumefaciens transfection method
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recombinant expression of active chimeric mutant of tissue plasminogen activator in Nicotiana tabacum hairy roots
recombinant expression of the chimeric truncated mutant enzyme using the CHO ATCC CRL9606 expression system, and as soluble His-tagged enzyme in Escherichia coli BL21(DE3) strain with F- dcm ompT hsdS (rB- mB-) gal genotype, comparison of protein potency in batch and fed-batch processes of the two methods, overview
recombinant expression of the isolated serine protease domain (residues 276-527) wild-type and mutant S478A/C395A/N448Q of enzyme tPA in Pichia pastoris strain X-33. The Pichia pastoris Kex2p protease can cleave the secreted tPA-serine protease domain
recombinant kringle 1 domain from tissue-type plasminogen activator
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recombinant overexpression of the enzyme in CHO ATCC CRL-9606 cells and secretion to the cell culture medium, co-expression with CERT S132A, a mutant form of CERT that is resistant to phosphorylation, and XBP1s, method optimization and evaluation, overview. Overexpression of CERT S132A increases the specific productivity of t-PA-producing CHO cells up to 35%, while the heterologous expression of XBP1s does not affect the t-PA expression rate
recombinant tPA from Genentech, 80% sc-tPA, 20% tc-tPA
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rt-PA is produced by recombinant DNA technology in Chinese hamster ovary cell lines
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subcloned into NheI/BamHI sites in GFP3.1
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t-PA and synthetic t-PA genes, expression as active enzyme in Curcumis melo cv. Geumssaragi-euncheon hairy roots using Agrobacterium rhizogenes transfection, insertion of the t-PA genes in genomic DNA of transgenic hairy roots. Selection of optimum media for the mass-production of transgenic hairy root and fibrinolytic activity of cultured transgenic hairy roots using the bioreactor
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the gene encoding full-length human t-PA is cloned into pPICZalphaA expression vector downstream of alcohol oxidase promoter and alpha-mating signal sequence from Saccharomyces cerevisiae and flush with the kex2 cleavage site to express the protein with a native N-terminus. Pichia pastoris strain GS115 is transformed with this cassette, and methanol utilizing (mut+) transformants are selected for production and secretion of functional human t-PA into culture media. Subcloning in Escherichia coli strain Top10 F'
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additional information
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tPA can act as a cytokine, executing its cytoprotective actions via activation of a survival signaling hierarchy in interstitial fibroblasts
diagnostics
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alterations in tPA activity levels can be used as a biomarker for perturbations in brain homeostasis
diagnostics
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alterations in tPA activity levels can be used as a biomarker for perturbations in brain homeostasis
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drug development
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antifibrinolytic agents may be useful for protecting neurons when tPA-mediated damage is anticipated
drug development
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both TPA-antibiotic locks and heparin-antibiotic locks used in conjunction with systemic antibiotics can effectively clear catheter-related bacteraemia in children without significant late recurrence at 6 weeks. The mean infection-free survival of the catheters following TPA-antibiotic locks treatment is shorter than that following heparinantibiotic locks treatment, but is not statistically significant
drug development
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neutrophils are good candidates to be the main source of metalloproteinase-9 following t-PA stroke treatment and in consequence, are partially responsible for thrombolysis-related brain bleedings. Combined therapy of t-PA with a metalloproteinase-9 or a neutrophil degranulation inhibitor may improve safety and efficacy of thrombolytic therapy in the acute phase of stroke
medicine
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t-PA has been widely and successfully used as a therapeutic fibrinolytic agent to treat acute myocardial infarction and pulmonary embolism
medicine
-
non-glycosylated TK1-2 useful for the treatment of cancer can be efficiently produced in Pichia, with retaining its activity
medicine
the kringle domain of tissue-type plasminogen activator inhibits in vivo tumor growth by suppression of angiogenesis without interfering with fibrinolysis
medicine
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combining antithrombin III, R-TPA and supportive care is more advantageous in treating the clinical manifestations of disseminated intravascular coagulation in this neonatal pig model than either single modality or supportive care alone
medicine
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dogs with femoral artery thrombosis are given either M5, a single site mutant of prourkinase or tPA by i.v. infusion. Thrombolysis is comparably effective by both activators. Blood loss is 10-fold higher with t-PA than with M5 and occurred at more multiple sites. This effect is postulated to be related to differences in the mechanism of plasminogen activation by t-PA and M5 in which the latter is promoted by degraded rather than intact (hemostatic) fibrin
medicine
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effects of intravenous administration of tPA on serum levels of IGF-1 and IGF-binding protein-3 in patients with acute ischemic stroke are investigated by radioimmunoassay in 10 patients. During tPA treatment, total IGF-1 and IGFBP-3 serum levels do not change, but there was an 70% increase in free IGF-1 serum levels at the end of the 1-h infusion. Intravenous therapy with tPA enhances the bioavailability of IGF-1
medicine
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establishment of a global assay of overall haemostasis potential: coagulation cascade in platelet-poor plasma is triggered by adding a minimal dose of recombinant tissue factor together with purified phospholipids and calcium; fibrinolysis is initiated by adding recombinant tPA in a concentration similar to what can be obtained during thrombolysis. Numerical differentials of optical densities reflecting rates of fibrin formation and degradation are calculated, and the Coagulation Profile (Cp) and the Fibrinolysis Profile (Fp) are determined. The combined effect of these counteractive systems is expressed as a ratio of Cp to Fp, called the Overall Haemostasis Index
medicine
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it is shown that exogenous tPA or tPA/plasminogen promotes axonal regeneration, remyelination, and functional recovery after sciatic nerve injury in the mouse, probably through removal of fibrin deposition and activation of MMP-9-positive macrophages, which may be responsible for myelin debris clearance and preventing collagen scar formation. Therefore, tPA may be useful for treatment of peripheral nerve injury
medicine
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medical case report of a 14-year-old male with Down syndrome and acute myeloblastic leukemia, diagnosed with infective endocarditis characterized by two large vegetations on aortic and mitral valves, who is successfully treated with r-tPA
medicine
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the present data support a model in which amyloid deposition in Alzheimer's disease induces a decrease in tPA activity through the overproduction of PAI-1 by activated glial cells
medicine
-
the present data support a model in which amyloid deposition in Alzheimer's disease induces a decrease in tPA activity through the overproduction of PAI-1 by activated glial cells
medicine
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thromboelastography shows the clots formed from procine whole blood to be highly resistant to human tPA-catalyzed lysis, indicating a poor activation of porcine plasminogen by human rtPA. The results suggest caution in using the pig as an experimental model when studying the effects of various agents on fibrolysis
medicine
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although rtPA enhances ischemic damage, the dose of recombinant tPA used in clinics does not affect the powerful neuroprotection by the JNK inhibitor XG-102
medicine
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desmoteplase has additional advantages to human tPA, it is not neurotoxic and is unaffected by beta-amyloid. Desmoteplase antagonizes the neurotoxicity induced by vascular tPA possibly by competing with tPA for the low-density lipoprotein receptorrelated protein-1 binding at the BBB and thus preventing tPA access to the brain parenchyma. A phase III clinical trial of desmoteplase is halted since it has failed to demonstrate any beneficial effects in terms of neurological improvements and survival
medicine
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excellent outcome (remarkable recovery 6 h after onset of symptoms) after the use of intravenous t-PA approximately 4 h after onset of symptoms for vertebrobasilar stroke
medicine
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in comparison with t-PA, plasmin shows a distinct benefit-to-risk advantage. Plasmin is equally effective as t-PA in thrombolysis and may be superior for treating thrombi in totally-occluded vessels. Whereas t-PA causes bleeding from vascular trauma sites in animals when infused at dosages used for thrombolysis (0.5-1 mg/kg), plasmin exhibits safety at therapeutic dosages. Plasmin can be used at several fold higher concentrations than is needed for thrombolysis, thereby providing a significant safety margin that is not attainable for t-PA
medicine
-
ischemic stroke patients weighing more than 100 kg seem to derive less benefit from IV t-PA than their lighter counterparts
medicine
-
no evidence of hemorrhage or any adverse effect due to topical application of t-PA. Control and t-PA treated rats show fibrosis inhibition 6 weeks after surgery and show no significant difference in inflammation or with regard to necrosis and abscess formation
medicine
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plasmin is a suitable alternative to t-PA as it causes less bleeding but has equivalent or greater thrombolytic efficacy
medicine
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pregnancy is associated with major perturbations of endogenous fibrinolytic capacity with an overwhelming increase in plasma plasminogen activator inhibitor type 1 concentrations and an inadequate release of active t-PA, i.e., these prothrombotic effects may, in part, explain the increased risk of arterial and venous thrombosis in pregnant women
medicine
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t-PA therapy has a clinically important and statistically significant benefit in spite of subgroup imbalances in baseline stroke severity and an increased risk of symptomatic intracerebral hemorrhage in patients receiving t-PA
medicine
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tPA generation in wound epidermis is at least partially controlled by changes in local interleukin-1alpha activity
medicine
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tPA is used as a thrombolytic agent for treatment of ischemic stroke and is the only agent that has been shown to improve stroke outcome in clinical trials. Patients receive little or no benefit if tPA therapy is initiated more than 3 h after the onset of stroke, which excludes most stroke patients from tPA treatment due to the time required for transportation to medical facilities and proper diagnosis. tPA may damage the basal lamina of the blood vessels, resulting in edema, disruption of the blood-brain barrier, or hemorrhage, thus any patients with evidence of hemorrhage or who have been taking any anti-coagulant medication such as aspirin are not candidates for tPA therapy
medicine
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tPA-plasmin pathway dysfunction may play a role in the link between major depressive disorder and cardiovascular disease. Agents that modulate tPA-plasminogen activity may be potential drugs for the treatment of patients with both major depressive disorder and cardiovascular disease
medicine
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tPA-plasmin pathway dysfunction may play a role in the link between major depressive disorder and cardiovascular disease. Agents that modulate tPA-plasminogen activity may be potential drugs for the treatment of patients with both major depressive disorder and cardiovascular disease
medicine
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type 2 diabetes mellitus patients with periodontal disease and otherwise healthy periodontally diseased patients tend to exhibit higher total amounts of t-PA than systemically and periodontally healthy control subjects, thus type 2 diabetes seems not to increase gingival crevicular fluid levels of inflammatory mediators like t-PA
medicine
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vaccination with a nucleoprotein with a tPA signal sequence efficiently clears homologous H5N1 influenza virus in infected lungs and induces partial cross-protection against heterologous, highly pathogenic H5N1 strains in mice. IFN-gamma producing T cells are more efficiently induced and expanded in mice immunized with ptPAs/nucleoprotein vaccine
medicine
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working strategy for targeted delivery of recombinant tPA bound to magnetic nanoparticles with less than 20% of a regular dose under magnetic guidance, resulting in effective thrombolysis and restore of hemodynamics in the rat embolic model
medicine
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enzyme has important thrombolytic properties due to its high fibrin affinity, it is approved for treating acute myocardial infarction, or heart attacks, and later for acute ischemic stroke, and acute, massive pulmonary embolism
medicine
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in the rabbit small clot embolic stroke model, which is a useful translational model and possibly a predictor of treatments that may show efficacy in human clinical trials, in combination with the thrombolytic, tissue plasminogen activator using a standard intravenous dose of 3.3 mg/kg (20% bolus, 80% infused), simvastatin can be safely administered with tissue plasminogen activator to improve clinical scores
medicine
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it is used clinically to dissolve
medicine
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therapy for acute ischemic stroke
medicine
therapy for acute ischemic stroke
medicine
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tissue plasminogen activator is the first-line treatment for stroke patients
medicine
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putative interaction and cleavage of NR1 subunit of N-methyl-D-aspartate receptors by a tPA-dependent mechanism can be a relevant therapeutic target for stroke treatment in humans
medicine
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the kringle 2 plus serine protease domains, K2S, of human tissue plasminogen activator is an efficacious thrombolytic drug, which is used to treat heart attacks and strokes by breaking up the fibrin clots that cause them
medicine
recombinant human t-PA is extensively used as a therapeutic agent for the treatment of thrombotic diseases owing to its greater safety and efficiency compared with other plasminogen activators like urokinase and streptokinase. CERTS132A-based secretion engineering can be an effective strategy for enhancing recombinant enzyme production in CHO cells
medicine
intensive care medication of ischemic stroke, thrombus targeting nanosystems could serve as carriers for enhanced delivery of enzyme tPA to the thrombi in order to increase its effective local concentrations. Biocompatible magnetite drug carriers, stabilized by a dextran shell, are developed to carry tissue plasminogen activator (tPA) for targeted thrombolysis under an external magnetic field, method evaluation, overview. Superparamagnetic iron oxide nanoparticles (SPIONs) have attracted great attention in many biomedical fields and are used in preclinical/experimental drug delivery, hyperthermia and medical imaging. All synthesized types of nanoparticles are well tolerated in cell culture experiments with human umbilical vein endothelial cells, indicating their potential utility for future therapeutic applications in thromboembolic diseases
medicine
tissue plasminogen activator converts plasminogen into plasmin and is used clinically to treat thrombosis
medicine
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putative interaction and cleavage of NR1 subunit of N-methyl-D-aspartate receptors by a tPA-dependent mechanism can be a relevant therapeutic target for stroke treatment in humans
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