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Titolo:
CYTOCHROME P4502C9 - AN ENZYME OF MAJOR IMPORTANCE IN HUMAN DRUG-METABOLISM
Autore:
MINERS JO; BIRKETT DJ;
Indirizzi:
FLINDERS MED CTR,DEPT CLIN PHARMACOL BEDFORD PK SA 5042 AUSTRALIA FLINDERS UNIV S AUSTRALIA,SCH MED BEDFORD PK SA 5042 AUSTRALIA
Titolo Testata:
British journal of clinical pharmacology
fascicolo: 6, volume: 45, anno: 1998,
pagine: 525 - 538
SICI:
0306-5251(1998)45:6<525:CP-AEO>2.0.ZU;2-#
Fonte:
ISI
Lingua:
ENG
Soggetto:
HUMAN-LIVER-MICROSOMES; POLYMERASE CHAIN-REACTION; TOLBUTAMIDE METABOLISM; TIENILIC ACID; IN-VITRO; STEREOSELECTIVE INTERACTION; WARFARIN-FLUCONAZOLE; CYP2C SUBFAMILY; ALLELIC VARIANT; MEPHENYTOIN 4-HYDROXYLASE;
Keywords:
CYP2C9; CYTOCHROME P450; DRUG INTERACTIONS; DRUG METABOLISM; PHARMACOGENETICS;
Tipo documento:
Review
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
154
Recensione:
Indirizzi per estratti:
Citazione:
J.O. Miners e D.J. Birkett, "CYTOCHROME P4502C9 - AN ENZYME OF MAJOR IMPORTANCE IN HUMAN DRUG-METABOLISM", British journal of clinical pharmacology, 45(6), 1998, pp. 525-538

Abstract

Accumulating evidence indicates that CYP2C9 ranks amongst the most important drug metabolizing enzymes in humans. Substrates for CYP2C9 include fluoxetine, losartan, phenytoin, tolbutamide, torsemide, S-warfarin, and numerous NSAIDs. CYP2C9 activity in vivo is inducible by rifampicin. Evidence suggests that CYP2C9 substrates may also be induced variably by carbamazepine, ethanol and phenobarbitone. Apart h-om the mutual competitive inhibition which may occur between alternate substrates, numerous other drugs have been shown to inhibit CYP2C9 activity invivo and/or in vitro. Clinically significant inhibition may occur with coadministration of amiodarone, fluconazole, phenylbutazone, sulphinpyrazone, sulphaphenazole and certain other sulphonamides. Polymorphisms in the coding region of the CYP2C9 gene produce variants at amino acid residues 144 (Arg144Cys) and 359 (Ile359Leu) of the CYP2C9 protein. Individuals homozygous for Leu359 have markedly diminished metaboliccapacities for most CYP2C9 substrates, although the frequency of thisallele is relatively low. Consistent with the modulation of enzyme activity by genetic and other factors, wide interindividual variability occurs in the elimination and/or dosage requirements of prototypic CYP2C9 substrates. Individualisation of dose is essential for those CYP2C9 substrates with a narrow therapeutic index.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 09/04/20 alle ore 11:02:16