TY - JOUR
T1 - Phenol sulfotransferase in humans
T2 - Properties, regulation, and function
AU - Weinshilboum, R. M.
N1 - Copyright:
Copyright 2004 Elsevier B.V., All rights reserved.
PY - 1986
Y1 - 1986
N2 - Phenol sulfotransferase (PST) catalyzes the sulfate conjugation of phenolic and catechol drugs and neurotransmitters. All human tissues that have been studied in detail contain at least two forms of PST. One form is thermolabile (TL), catalyzes the sulfate conjugation of micromolar concentrations of dopamine and other phenolic monoamines, and is relatively resistant to inhibition by 2,6-dichloro-4-nitrophenol (DCNP). The other form is thermostable (TS), catalyzes the sulfate conjugation of micromolar concentrations of simple phenols such as p-nitrophenol, and is relatively sensitive to DCNP inhibition. These two forms of PST have been physically separated and partially purified from several human tissues, including an easily accessible tissue, the blood platelet. The biochemical properties of platelet PST are very similar to those of PST in human brain, liver, and small intestine. Individual differences in the basal activity of TS PST in the platelet are correlated with individual variations in the activity of this form of the enzyme in human cerebral cortex (r = .94, n = 15, P < 0.001). In addition, both platelet TS and PST activities are correlated significantly with the extent of sulfate conjugation of orally administered drugs such as acetaminophen and methyldopa. These later observations are compatible with the conclusions that PST activity may reflect the activity of the enzyme at sites of drug metabolism, and that variation in PST activity is one factor responsible for individual differences in the sulfate conjugation of orally administered drugs.
AB - Phenol sulfotransferase (PST) catalyzes the sulfate conjugation of phenolic and catechol drugs and neurotransmitters. All human tissues that have been studied in detail contain at least two forms of PST. One form is thermolabile (TL), catalyzes the sulfate conjugation of micromolar concentrations of dopamine and other phenolic monoamines, and is relatively resistant to inhibition by 2,6-dichloro-4-nitrophenol (DCNP). The other form is thermostable (TS), catalyzes the sulfate conjugation of micromolar concentrations of simple phenols such as p-nitrophenol, and is relatively sensitive to DCNP inhibition. These two forms of PST have been physically separated and partially purified from several human tissues, including an easily accessible tissue, the blood platelet. The biochemical properties of platelet PST are very similar to those of PST in human brain, liver, and small intestine. Individual differences in the basal activity of TS PST in the platelet are correlated with individual variations in the activity of this form of the enzyme in human cerebral cortex (r = .94, n = 15, P < 0.001). In addition, both platelet TS and PST activities are correlated significantly with the extent of sulfate conjugation of orally administered drugs such as acetaminophen and methyldopa. These later observations are compatible with the conclusions that PST activity may reflect the activity of the enzyme at sites of drug metabolism, and that variation in PST activity is one factor responsible for individual differences in the sulfate conjugation of orally administered drugs.
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M3 - Article
C2 - 2873064
AN - SCOPUS:0022459257
SN - 0014-9446
VL - 45
SP - 2223
EP - 2228
JO - Federation Proceedings
JF - Federation Proceedings
IS - 8
ER -