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6-ketocholestanol
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added at high concentration causes modest increase in enzyme activity
7-ketocholesterol
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added at high concentration causes modest increase in enzyme activity
cholate
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increase of activity in cholate-fed animals
liver fatty acid binding protein/bovine serum albumin
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small increase in activity
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low density lipoprotein
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Mevalonolactone
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intragastric administration, increasing sterol biosynthesis and increasing enzyme activity
phosphatidylethanolamine
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weak stimulatory effect on activity
TNF-alpha
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up-regulating of ACAT1 expression
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25-hydroxycholesterol
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not stimulatory
25-hydroxycholesterol
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25-hydroxycholesterol
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activates
25-hydroxycholesterol
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25-hydroxycholesterol
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activates
25-hydroxycholesterol
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stimulates enzyme activity in liver microsomes in vitro with half-maximal stimulation at 0.0168 mM oxysterol. A major part of the activation of microsomal enzyme is not ascribable to increased substrate availability for the enzyme
albumin
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stimulates
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albumin
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stimulates, effect is dependent on oleoyl-CoA concentration
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albumin
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required in the assay medium to prevent the high concentration of oleoly-CoA from inhibiting the enzyme presumably by disrupting the microsomal membrane
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cholesterol
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day 40 samples, exogenous, added as phosphatidylcholine liposomes, concentration-dependent increase in activity
cholesterol
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day 50 and 60 samples: not stimulatory
cholesterol
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exogenous, not stimulatory
cholesterol
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exogenous cholesterol in the liposomes is absolutely necessary for activity of the reconstituted enzyme
cholesterol
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exogenous, not stimulatory
cholesterol
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addition of cholesterol to frozen microsomes prepared from unfrozen liver tissue increases the enzyme activity
cholesterol
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serves as an enzyme activator in vitro, in addition to its role as an enzyme substrate
cholesterol
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exogenous cholesterol in the liposomes is absolutely necessary for activity of the reconstituted enzyme
cholesterol
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addition of cholesterol to microsomes prepared from frozen liver tissue does not further increase the enzyme activity
cholesterol
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presence of cholesterol stimulates reaction of ACAT1 with sitosterol up to 3fold, reaction of ACAT2 is only moderately activated
cholesterol
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significant activation of reaction with 7-ketocholesterol as substrate, decrease in Hill coefficient from 3.0 without cholesterol to 1.1 with cholesterol
cholesterol
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ACAT2 is transcriptionally regulated by cholesterol
cholesterol
acts as a strong activator and as a substrate
cholesterol
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exogenous, not stimulatory
cholesterol
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exogenous, added as phosphatidylcholine liposome or in acetone solution, stimulates
cholesterol
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exogenous, delivered as a Triton WR-1339 detergent dispersion, increases activity
cholesterol
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exogenous, in liposomes or in organic solvent, stimulates
cholesterol
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exogenous, 25% increase of adrenal microsome activity and 2fold increase of activity in liver
cholesterol
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increase of activity in cholesterol-fed animals
cholesterol
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exogenous, not stimulatory
ent-cholesterol
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epi-cholesterol
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low density lipoprotein
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increase of activity
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low density lipoprotein
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-
sitosterol
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sitosterol
weak activator
additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates
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additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates
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additional information
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enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates
-
additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates. When pregnenolone and cholesterol (or other sterol analogues) are both present, binding of cholesterol at site A causes conformational changes, enabling the enzyme to increase the rate of esterification reaction much more efficiently
-
additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates. When pregnenolone and cholesterol (or other sterol analogues) are both present, binding of cholesterol at site A causes conformational changes, enabling the enzyme to increase the rate of esterification reaction much more efficiently
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additional information
-
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates. When pregnenolone and cholesterol (or other sterol analogues) are both present, binding of cholesterol at site A causes conformational changes, enabling the enzyme to increase the rate of esterification reaction much more efficiently
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates
-
additional information
enzyme ACAT1 can be activated by a variety of sterols. All sterols that possess the iso-octyl side chain including cholesterol, oxysterols, various plant sterols can all be activators of ACAT. Pregnenolone can only be an ACAT substrate because it lacks the iso-octyl side chain required to be an ACAT activator. The unnatural cholesterol analogs epi-cholesterol (with 3-alpha OH in steroid ring B) and ent-cholesterol (the mirror image of cholesterol) contain the iso-octyl side chain but do not have the 3-beta OH at C-3. Thus, they can only serve as activators and cannot serve as substrates
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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additional information
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regulation by sterol
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