EffEct of cytochromE P450 2D6 anD 3a EnzymE InhIbItIon on thE mEtabolIsm of oxycoDonE
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P-192: Association of Cytochrome P450 2D6 (CYP2D6) Gene Polymorphism with Clomiphene Citrate Treatment in Iranian Infertile Women with Polycystic Ovary Syndrome
Background: Clomiphene Citrate (CC) is the most frequently administered drug for the treatment of female infertility [e.g. polycystic ovary syndrome (PCOS)]; which aims at restoring ovulation. Clomiphene is metabolized by CYP2D6, an important enzyme responsible for the metabolism of approximately 25% of clinically used drugs. CYP2D6 is very polymorphic and thought to result in inter- individual...
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In vitro metabolism of methadone was investigated in cytochrome P450 (CYP) supersomes and phenotyped human liver microsomes (HLMs) to reconcile past findings on CYP involvement in stereo-selective metabolism of methadone. Racaemic methadone was used for incubations; (R)- and (S)-methadone turnover and (R)- and (S)-EDDP formation were determined using chiral liquid chromatography-tandem mass spe...
متن کاملQuantitative contribution of CYP2D6 and CYP3A to oxycodone metabolism in human liver and intestinal microsomes.
Oxycodone undergoes N-demethylation to noroxycodone and O-demethylation to oxymorphone. The cytochrome P450 (P450) isoforms capable of mediating the oxidation of oxycodone to oxymorphone and noroxycodone were identified using a panel of recombinant human P450s. CYP3A4 and CYP3A5 displayed the highest activity for oxycodone N-demethylation; intrinsic clearance for CYP3A5 was slightly higher than...
متن کاملLKY-047: First Selective Inhibitor of Cytochrome P450 2J2.
Highly selective cytochrome P450 CYP2J2 (CYP2J2) inhibitors suitable for reaction phenotyping are currently not available. (7S)-(+)-(4-Nitro-phenyl)-acrylic acid, 8,8-dimethyl-2-oxo-6,7-dihydro-2H,8H-pyrano[3,2-g]chromen-7-yl-ester (LKY-047), a decursin derivative, was synthesized, and its inhibitor potencies toward CYP2J2 as well as other cytochrome P450 (P450) enzymes in human liver microsome...
متن کاملMetabolism of sesamin by cytochrome P450 in human liver microsomes.
Metabolism of sesamin by cytochrome P450 (P450) was examined using yeast expression system and human liver microsomes. Saccharomyces cerevisiae cells expressing each of human P450 isoforms (CYP1A1, 1A2, 2A6, 2B6, 2C8, 2C9, 2C18, 2C19, 2D6, 2E1, and 3A4) were cultivated with sesamin, and monocatechol metabolite was observed in most of P450s. Kinetic analysis using the microsomal fractions of the...
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