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Information on EC 1.5.3.13 - N1-acetylpolyamine oxidase
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1.5.3.13 N1-acetylpolyamine oxidaseIUBMB Comments
The enzyme also catalyses the reaction: N1,N12-diacetylspermine + O2 + H2O = N1-acetylspermidine + 3-acetamamidopropanal + H2O2 . No or very weak activity with spermine, or spermidine in absence of aldehydes. In presence of aldehydes the enzyme catalyses the reactions: 1. spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2. spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 . A flavoprotein (FAD). This enzyme, encoded by the PAOX gene, is found in mammalian peroxisomes and oxidizes N1-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion. Differs in specificity from EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
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Word Map
- 1.5.3.13
- spermine
- putrescine
-
diamine
- ornithine
- oxidases
-
n1-acetyltransferase
- s-adenosylmethionine
- n1-acetylspermine
-
fad-dependent
-
monoamine
- 3-aminopropanal
- 1,3-diaminopropane
- cadaverine
- apoplastic
- aminoaldehydes
- aminoguanidine
- acrolein
-
back-conversion
- alpha-difluoromethylornithine
- samdc
-
n1-acetylated
- thermospermine
- norspermidine
- n8-acetylspermidine
-
tetraamine
-
1.4.3.6
- analysis
- medicine
- pharmacology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Synonyms
polyamine oxidase, paoh1, n1-acetylpolyamine oxidase, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
APAO
EC 1.5.3.11
-
-
formerly, part transferred
-
PAO
PAOX
additional information
-
PAO is a member of the monoamine oxidase family of flavoproteins
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
N1-acetylspermidine + O2 + H2O = putrescine + 3-acetamidopropanal + H2O2
-
-
-
-
N1-acetylspermine + O2 + H2O = spermidine + 3-acetamidopropanal + H2O2
-
-
-
-
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SYSTEMATIC NAME
IUBMB Comments
N1-acetylpolyamine:oxygen oxidoreductase (3-acetamidopropanal-forming)
The enzyme also catalyses the reaction: N1,N12-diacetylspermine + O2 + H2O = N1-acetylspermidine + 3-acetamamidopropanal + H2O2 [1]. No or very weak activity with spermine, or spermidine in absence of aldehydes. In presence of aldehydes the enzyme catalyses the reactions: 1. spermine + O2 + H2O = spermidine + 3-aminopropanal + H2O2, and with weak efficiency 2. spermidine + O2 + H2O = putrescine + 3-aminopropanal + H2O2 [2]. A flavoprotein (FAD). This enzyme, encoded by the PAOX gene, is found in mammalian peroxisomes and oxidizes N1-acetylated polyamines at the exo (three-carbon) side of the secondary amine, forming 3-acetamamidopropanal. Since the products of the reactions are deacetylated polyamines, this process is known as polyamine back-conversion. Differs in specificity from EC 1.5.3.14 [polyamine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.15 [N8-acetylspermidine oxidase (propane-1,3-diamine-forming)], EC 1.5.3.16 (spermine oxidase) and EC 1.5.3.17 (non-specific polyamine oxidase).
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
(R)-alpha-methylspermidine + O2 + H2O
?
-
PAO supplemented with benzaldehyde predominantly catalyzes the cleavage of (R)-isomer of alpha-methylspermidine, whereas in the presence of pyridoxal the (S)-alpha-methylspermidine is preferred
-
-
?
(S)-alpha-methylspermidine + O2 + H2O
?
-
PAO supplemented with benzaldehyde predominantly catalyzes the cleavage of (R)-isomer of alpha-methylspermidine, whereas in the presence of pyridoxal the (S)-alpha-methylspermidine is preferred
-
-
?
(S)-N1-(2-methyl-1-butyl)-N11-ethyl-4,8-diazaundecane-1,11-diamine + O2 + H2O
?
-
-
-
?
alpha-methylspermidine + O2 + H2O
?
-
weak oxidation in presence of benzaldehyde, no oxidation without benzaldehyde
-
-
?
alpha-methylspermine + O2 + H2O
?
-
oxidation in presence of benzaldehyde, no oxidation without benzaldehyde
-
-
?
alpha-methylspermine + O2 + H2O
spermidine + alpha-methylspermidine + ?
-
-
-
-
?
N,N'-bis-(3-benzylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-benzylaminopropyl)butane-1,4-diamine + H2O2 + ?
-
-
main product
-
?
N,N'-bis-(3-benzylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-benzylaminopropyl)butane-1,4-diamine + N-(3-aminopropyl)-N'-(3-Benzylaminopropyl)butane-1,4-diamine + H2O2
-
-
-
-
?
N,N'-bis-(3-ethylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-ethylaminopropyl)butane-1,4-diamine + H2O2 + ?
-
minor N4-endo cleavage pathways resulting in formation of N1-ethylpropane-1,3-diamine
-
-
?
N-(3-benzylaminopropyl)-N'-(3-ethylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-ethylaminopropyl)butane-1,4-diamine + H2O2 + ?
-
-
-
-
?
N-[(2R)-4-[(4-aminobutyl)amino]butan-2-yl]pyridine-4-carboxamide + O2 + H2O
putrescine + (3R)-3-[(pyridin-4-yl)amino]butanal + H2O2
-
-
-
?
N-[(2S)-4-[(4-aminobutyl)amino]butan-2-yl]pyridine-4-carboxamide + O2 + H2O
putrescine + (3S)-3-[(pyridin-4-yl)amino]butanal + H2O2
-
-
-
?
N1,N11-didansylnorspermine + O2 + H2O
1-dansylnorspermidine + 1-dansylamido-3-propanal + H2O2
N1-(3-benzylaminopropyl)butane-1,4-diamine + O2 + H2O
spermidine + H2O2 + benzylalcohol
-
-
-
-
?
N1-(3-[[(thiophen-2-yl)methyl]amino]propyl)octane-1,8-diamine + O2 + H2O
octane-1,8-diamine + N1-[(thiophen-2-yl)methyl]propanal + H2O2
-
-
-
?
N1-acetyl-2-methylspermidine + O2 + H2O
putrescine + N-(2-methyl-3-oxopropyl)acetamide + H2O2
-
-
-
?
N1-acetyl-8-methylspermidine + O2 + H2O
pentane-1,4-diamine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-benzoyl-(R)-alpha-methylspermidine + O2 + H2O
putrescine + N-[(2R)-4-oxobutan-2-yl]benzamide + H2O2
-
-
-
?
N1-benzoyl-(S)-alpha-methylspermidine + O2 + H2O
putrescine + N-[(2S)-4-oxobutan-2-yl]benzamide + H2O2
-
-
-
?
N1-benzyl-propane-1,3-diamine + O2 + H2O
propane-1,3-diamine + H2O2 + benzylalcohol
-
-
-
-
?
N1-benzyldodecane-1,12-diamine + O2 + H2O
dodecane-1,12-diamine + N1-benzylpropanal + H2O2
-
-
-
?
N1-benzylspermine + O2 + H2O
spermidine + 3-(benzylamino)propanal + H2O2
-
-
-
?
N1-ethyl-N11-(cycloheptyl)methyl-4,8-diazaundecane-1,11-diamine + O2 + H2O
?
-
-
-
?
N1-phenyl-(R)-alpha-methylspermidine + O2 + H2O
putrescine + (3R)-3-anilinobutanal + H2O2
-
-
-
?
N1-phenyl-(S)-alpha-methylspermidine + O2 + H2O
putrescine + (3S)-3-anilinobutanal + H2O2
-
-
-
?
N1-[(naphthalen-2-yl)methyl]spermine + O2 + H2O
spermidine + N1-[(naphthalen-2-yl)methyl]propanal + H2O2
-
-
-
?
N1-[(pyridin-2-yl)methyl]spermine + O2 + H2O
spermidine + N1-[(pyridin-2-yl)methyl]propanal + H2O2
-
-
-
?
N1-[(thiophen-2-yl)methyl]spermine + O2 + H2O
spermidine + N1-[(thiophen-2-yl)methyl]propanal + H2O2
-
-
-
?
N1,N11-didansylnorspermine + O2 + H2O
1-dansylnorspermidine + 1-dansylamido-3-propanal + H2O2
-
-
-
-
?
N1,N11-didansylnorspermine + O2 + H2O
1-dansylnorspermidine + 1-dansylamido-3-propanal + H2O2
-
-
-
-
?
N1,N12-diacetylspermine + O2 + H2O
N1-acetylspermidine + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1,N12-diacetylspermine + O2 + H2O
N1-acetylspermidine + 3-acetamidopropanal + H2O2
N1-acetylspermine is first liberated as a product and then oxidized further to putrescine
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
the enzyme is involved in polyamine catabolism. The enzyme is a constitutively expressed enzyme that catalyzes the oxidative cleavage of N1-acetylpolyamines to yield a less basic polyamine, 3-acetylamidopropanal, and hydrogen peroxide
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
oxidized at the carbon on the exo-side of the N4-nitrogen
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
at pH 6.5, substrate preference is in the following decreasing order: thermospermine, N1-acetylspermine, norspermine, spermine, spermidine. Spermidine is catabolized at a very low rate. At pH 7.5, substrate preference is in the following decreasing order: spermine, norspermine, N1-acetylspermine, thermospermine, spermidine. Spermidine is catalyzed at a very low rate
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
PAO preferentially oxidizes acetylspermine or acetylspermidine over spermine
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
oxidized at the carbon on the exo-side of the N4-nitrogen
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
at pH 8.0, the substrate preference in decreasing order is as follows: spermine/thermospermine, N1-acetylspermine, norspermine, spermidine. At pH 7.0, the substrate preference in decreasing order is as follows: thermospermine, norspermine, spermine, N1-acetylspermine, spermidine
-
-
?
spermidine + O2 + H2O
?
-
no activity in absence of aldehydes, weak activity in presence of aldehydes
-
-
?
spermidine + O2 + H2O
?
-
weak oxidation in presence of benzaldehyde, no oxidation without benzaldehyde
-
-
?
spermine + O2 + H2O
?
-
oxidation in presence of benzaldehyde, no oxidation without benzaldehyde
-
-
?
spermine + O2 + H2O
?
-
rather poor substrate for hPAO, aldehyde supplementation greatly increased its degradation
-
-
?
spermine + O2 + H2O
spermidine + 3-aminopropanal + H2O2
least favoured substrate
-
-
?
additional information
?
-
Bjpao2 shows no activity with spermine
-
-
?
additional information
?
-
PAO expression is inducible by polyamine analogues and thus may contribute to the inhibition of cell growth
-
-
?
additional information
?
-
-
PAO expression is inducible by polyamine analogues and thus may contribute to the inhibition of cell growth
-
-
?
additional information
?
-
no efficient hydrolysis of: spermine, spermidine and N8-acetylspermidine, SL-11144, SL-11150, SL-11158 and SL-11156
-
-
?
additional information
?
-
-
no efficient hydrolysis of: spermine, spermidine and N8-acetylspermidine, SL-11144, SL-11150, SL-11158 and SL-11156
-
-
?
additional information
?
-
-
no production of spermidine from bis-alpha-methylspermine, hPAO
-
-
?
additional information
?
-
-
APAO is capable of metabolizing several N-alkylated polyamine derivatives, substrate specificity, overview. N1-(3-Ethylaminopropyl)butane-1,4-diamine trihydrochloride is a poor substrate
-
-
?
additional information
?
-
-
assay method development and validation, evaluation of quantitative determination of reaction products, overview
-
-
?
additional information
?
-
no substrate: N1-acetyl-3-methylspermidine
-
-
-
additional information
?
-
PAOX naturally metabolizes achiral N1-acetylated polyamines, displays aldehyde-controllable stereospecificity with chiral 1-methylated polyamines, like (R)- and (S)-1-methylspermidine
-
-
-
additional information
?
-
-
PAOX naturally metabolizes achiral N1-acetylated polyamines, displays aldehyde-controllable stereospecificity with chiral 1-methylated polyamines, like (R)- and (S)-1-methylspermidine
-
-
-
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
N,N'-bis-(3-benzylaminopropyl)butane-1,4-diamine + O2 + H2O
N1-(3-benzylaminopropyl)butane-1,4-diamine + N-(3-aminopropyl)-N'-(3-Benzylaminopropyl)butane-1,4-diamine + H2O2
-
-
-
-
?
N1,N12-diacetylspermine + O2 + H2O
N1-acetylspermidine + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1-acetylspermine + O2 + H2O
spermidine + 3-acetaminopropanal + H2O2
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
-
-
-
?
N1-acetylspermidine + O2 + H2O
putrescine + 3-acetamidopropanal + H2O2
-
the enzyme is involved in polyamine catabolism. The enzyme is a constitutively expressed enzyme that catalyzes the oxidative cleavage of N1-acetylpolyamines to yield a less basic polyamine, 3-acetylamidopropanal, and hydrogen peroxide
-
-
?
additional information
?
-
PAO expression is inducible by polyamine analogues and thus may contribute to the inhibition of cell growth
-
-
?
additional information
?
-
-
PAO expression is inducible by polyamine analogues and thus may contribute to the inhibition of cell growth
-
-
?
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COFACTOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
1,12-diaminododecane
1,12-diaminododecane derivatives could represent good candidates for the development of novel highly specific mPAO inhibitors
6,6'-[ethane-1,2-diyldi(piperidine-4,1-diyl)]bis[N-[(2-methoxyphenyl)methyl]hexan-1-amine]
17fold selectivity for spermine oxidase over polyamine oxidase
-
methoctramine
120fold selectivity for spermine oxidase over polyamine oxidase
-
N,N'-butanedienyl butanediamine
-
i.e. MDL 72527 or CPC-200, a small molecule specific inhibitor of polyamine oxidase, effectively blocks androgen-induced reactive oxygen species production in human prostate cancer cells, as well as significantly delays prostate cancer progression and death in animals developing spontaneous prostate cancer
N1,N1'-(pentane-1,5-diyl)bis[N6-[(2-methoxyphenyl)methyl]hexane-1,6-diamine]
9fold selectivity for spermine oxidase over polyamine oxidase
-
N1,N7-bis(6-[[(2-methoxyphenyl)methyl]amino]hexyl)heptane-1,7-diamine
40fold selectivity for spermine oxidase over polyamine oxidase
-
MDL72527
irreversible. In addition to the covalent adduct, a second MDL72527 molecule is bound in the active site. Binding of MDL72527 is accompanied by altered conformations in the APAO backbone
N1,N4-bis(2,3-butadienyl)-1,4-butanediamine
2.5 mM, 70% inhibition of N1-acetylspermine oxidation
additional information
-
no inhibitory activity: N-(3-aminopropyl)-N -2-propynyl-1,4-butanediamine and N-[3-(2-propynylamino)propyl]-1,4-butanediamine
-
additional information
no inhibition at pH 7.5: 1,8-diaminooctane. Comparative study on murine PAO (mPAO) and SMO (mSMO) inhibition. The different behaviour displayed by 1,12-diaminododecane towards mPAO and mSMO reveals the occurrence of basic differences in the ligand binding mode of the two enzymes, the first enzyme interacting mainly with substrate secondary amino groups and the second one with substrate primary amino groups. The data provide the basis for the development of novel and selective inhibitors able to discriminate between mammalian SMO and PAO activities
-
additional information
-
no inhibition at pH 7.5: 1,8-diaminooctane. Comparative study on murine PAO (mPAO) and SMO (mSMO) inhibition. The different behaviour displayed by 1,12-diaminododecane towards mPAO and mSMO reveals the occurrence of basic differences in the ligand binding mode of the two enzymes, the first enzyme interacting mainly with substrate secondary amino groups and the second one with substrate primary amino groups. The data provide the basis for the development of novel and selective inhibitors able to discriminate between mammalian SMO and PAO activities
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Adenocarcinoma
A small molecule polyamine oxidase inhibitor blocks androgen-induced oxidative stress and delays prostate cancer progression in the transgenic adenocarcinoma of the mouse prostate model.
Adenocarcinoma
Effect of polyamine oxidase inhibition on the colonic malignant transformation process induced by 1,2-dimethylhydrazine.
Adenocarcinoma
The growth of MAT-LyLu rat prostatic adenocarcinoma can be prevented in vivo by polyamine deprivation.
Brain Edema
Effects of MDL 72527, a specific inhibitor of polyamine oxidase, on brain edema, ischemic injury volume, and tissue polyamine levels in rats after temporary middle cerebral artery occlusion.
Brain Injuries, Traumatic
Elevated N1-acetylspermidine levels in gerbil and rat brains after CNS injury.
Brain Ischemia
Elevated N1-acetylspermidine levels in gerbil and rat brains after CNS injury.
Brain Ischemia
[Changes and significance of PAO activities and polyamine levels at different time of reperfusion after transient focal cerebral ischemia in rats]
Breast Neoplasms
Estrogens and polyamines in breast cancer: their profiles and values in disease staging.
Breast Neoplasms
Inducible expression of maize polyamine oxidase in the nucleus of MCF-7 human breast cancer cells confers sensitivity to etoposide.
Breast Neoplasms
Spermine oxidase SMO(PAOh1), Not N1-acetylpolyamine oxidase PAO, is the primary source of cytotoxic H2O2 in polyamine analogue-treated human breast cancer cell lines.
Carcinoma
Cytotoxic effects of the polyamine oxidase inactivator MDL 72527 to two human colon carcinoma cell lines SW480 and SW620.
Carcinoma
Induction of the PAOh1/SMO polyamine oxidase by polyamine analogues in human lung carcinoma cells.
Carcinoma
Inhibition of polyamine oxidase improves the antitumoral effect of ornithine decarboxylase inhibitors.
Carcinoma
Inhibition of polyamine oxidase prevented cyclin-dependent kinase inhibitor-induced apoptosis in HCT 116 colon carcinoma cells.
Carcinoma, Hepatocellular
Expression of spermidine/spermine N1-acetyltransferase in growing Yoshida AH-130 hepatoma cells.
Carcinoma, Lewis Lung
Inhibition of polyamine oxidase improves the antitumoral effect of ornithine decarboxylase inhibitors.
Cataract
Polyamine Oxidase Is Involved in Spermidine Reduction of Transglutaminase Type 2-Catalyzed ?H-Crystallins Polymerization in Calcium-Induced Experimental Cataract.
Cervical Intraepithelial Neoplasia
Cervical intraepithelial neoplasia is associated with increased polyamine oxidase and diamine oxidase concentrations in cervical mucus.
Colonic Neoplasms
Inhibition of polyamine oxidase enhances the cytotoxicity of polyamine oxidase substrates. A model study with N(1)-(n-octanesulfonyl)spermine and human colon cancer cells.
Colorectal Neoplasms
Polyamine oxidase activity and polyamine levels in human colorectal cancer and in normal surrounding mucosa.
Diabetes Mellitus, Type 1
Does polyamine oxidase activity influence the oxidative metabolism of children who suffer of diabetes mellitus?
Epilepsy
A barley polyamine oxidase isoform with distinct structural features and subcellular localization.
Glioblastoma
Inhibition of the growth of U-251 human glioblastoma in nude mice by polyamine deprivation.
Hyperbilirubinemia, Neonatal
Polyamine oxidase activity in peripheral blood of newborn infants with neonatal hyperbilirubinemia: is bilirubin an antioxidant?
Infarction, Middle Cerebral Artery
Effects of MDL 72527, a specific inhibitor of polyamine oxidase, on brain edema, ischemic injury volume, and tissue polyamine levels in rats after temporary middle cerebral artery occlusion.
Infections
Free polyamine and polyamine regulation during pre?penetration and penetration resistance events in oat against crown rust (Puccinia coronata f. sp. avenae)
Infections
Polyamines as a common source of hydrogen peroxide in host- and nonhost hypersensitive response during pathogen infection.
Kidney Failure, Chronic
[Physiological functions of polyamines and regulation of polyamine content in cells]
Leukemia
Participation of T-lymphocytes in the curative effect of a novel synthetic polyamine analogue, N,N'-bis[3-(ethylamino)propyl]-1,7-heptanediamine, against L1210 leukemia in vivo.
Lung Neoplasms
Highly expressed N1-acetylpolyamine oxidase detoxifies polyamine analogue N1-cyclopropylmethyl-N11-ethylnorspermine in human lung cancer cell line A549.
Malaria
Polyamine oxidase in human retroplacental serum inhibits the growth of Plasmodium falciparum.
Melanoma
Polyamine oxidase activity and concentration of polyamines in tissues and serum of hamsters with transplantational pigmented melanoma IC-Sofia.
Melanoma, Experimental
Polyamine transporter recognization and antitumor effects of anthracenymethyl homospermidine.
Neoplasms
Cervical intraepithelial neoplasia is associated with increased polyamine oxidase and diamine oxidase concentrations in cervical mucus.
Neoplasms
Cytotoxicity of the polyamine oxidase inactivator MDL 72527 to cancer cells: comparison with a saturated structural analogue.
Neoplasms
Effect of polyamine analogues and inhibition of polyamine oxidase on spermidine/spermine N1-acetyltransferase activity and cell proliferation.
Neoplasms
Effect of polyamine deprivation on the survival of intracranial glioblastoma bearing rats.
Neoplasms
Effect of polyamine oxidase inhibition on the colonic malignant transformation process induced by 1,2-dimethylhydrazine.
Neoplasms
Inhibition of polyamine oxidase activity affects tumor development during the maize-Ustilago maydis interaction.
Neoplasms
Inhibition of polyamine oxidase enhances the cytotoxicity of polyamine oxidase substrates. A model study with N(1)-(n-octanesulfonyl)spermine and human colon cancer cells.
Neoplasms
Inhibition of the growth of U-251 human glioblastoma in nude mice by polyamine deprivation.
Neoplasms
Microarray analysis uncovers retinoid targets in human bronchial epithelial cells.
Neoplasms
Purvalanol A is a strong apoptotic inducer via activating polyamine catabolic pathway in MCF-7 estrogen receptor positive breast cancer cells.
Neoplasms
Stimulation of clonal tumor cell growth in vitro by inhibiting the serum polyamine oxidase activity.
Neoplasms
Studies of the mechanism by which increased spermidine/spermine N1-acetyltransferase activity increases susceptibility to skin carcinogenesis.
Neurodegenerative Diseases
Targeting Polyamine Oxidase to Prevent Excitotoxicity-Induced Retinal Neurodegeneration.
Ovarian Neoplasms
Polyamine catabolism in platinum drug action: Interactions between oxaliplatin and the polyamine analogue N1,N11-diethylnorspermine at the level of spermidine/spermine N1-acetyltransferase.
Pancreatitis
Gossypol activates pancreatic polyamine catabolism in normal rats and induces acute pancreatitis in transgenic rats over-expressing spermidine/spermine N1-acetyltransferase.
Pancreatitis
[Methylated analogues of spermine and spermidine as tools to investigate cellular functions of polyamines and the enzymes of their metabolism]
Parasitemia
Trypanosoma brucei: polyamine oxidase mediated trypanolytic activity in the serum of naturally resistant cattle.
Prostatic Neoplasms
A small molecule polyamine oxidase inhibitor blocks androgen-induced oxidative stress and delays prostate cancer progression in the transgenic adenocarcinoma of the mouse prostate model.
Prostatic Neoplasms
Ornithine Decarboxylase Is Sufficient for Prostate Tumorigenesis via Androgen Receptor Signaling.
Stroke
Polyamine oxidase and acrolein as novel biochemical markers for diagnosis of cerebral stroke.
Stroke
[Physiological functions of polyamines and regulation of polyamine content in cells]
Ureteral Obstruction
Polyamine oxidase and diamine oxidase activities in acute ureteral obstruction.
Uterine Cervical Neoplasms
Altered urinary profiles of polyamines and endogenous steroids in patients with benign cervical disease and cervical cancer.
Uterine Cervical Neoplasms
Cervical intraepithelial neoplasia is associated with increased polyamine oxidase and diamine oxidase concentrations in cervical mucus.
Vascular System Injuries
Treatment with polyamine oxidase inhibitor reduces microglial activation and limits vascular injury in ischemic retinopathy.
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