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http://purl.uniprot.org/citations/18619574http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/18619574http://www.w3.org/2000/01/rdf-schema#comment"The aim of the present study was to estimate the relative contribution of cytochrome P450 isoforms (P450s), including P450s of the CYP2C subfamily, to the metabolism of caffeine in human liver. The experiments were carried out in vitro using cDNA-expressed P450s, liver microsomes and specific P450 inhibitors. The obtained results show that (1) apart from the 3-N-demethylation of caffeine - a CYP1A2 marker reaction and the main oxidation pathway of caffeine in man - 1-N-demethylation is also specifically catalyzed by CYP1A2 (not reported previously); (2) 7-N-demethylation is catalyzed non-specifically, mainly by CYP1A2 and, to a smaller extent, by CYP2C8/9 and CYP3A4 (and not by CYP2E1, as suggested previously); (3) C-8-hydroxylation preferentially involves CYP1A2 and CYP3A4 and, to a smaller degree, CYP2C8/9 and CYP2E1 (and not only CYP3A, as suggested previously) at a concentration of 100 microM corresponding to the maximum therapeutic concentration in humans. At a higher caffeine concentration, the contribution of CYP1A2 to this reaction decreases in favour of CYP2C8/9. The obtained data show for the first time the contribution of CYP2C isoforms to the metabolism of caffeine in human liver and suggest that apart from 3-N-demethylation, 1-N-demethylation may also be used for testing CYP1A2 activity. Moreover, they indicate that the C-8-hydroxylation is not exclusively catalyzed by CYP3A4."xsd:string
http://purl.uniprot.org/citations/18619574http://purl.org/dc/terms/identifier"doi:10.1016/j.bcp.2008.05.025"xsd:string
http://purl.uniprot.org/citations/18619574http://purl.uniprot.org/core/author"Daniel W.A."xsd:string
http://purl.uniprot.org/citations/18619574http://purl.uniprot.org/core/author"Kot M."xsd:string
http://purl.uniprot.org/citations/18619574http://purl.uniprot.org/core/date"2008"xsd:gYear
http://purl.uniprot.org/citations/18619574http://purl.uniprot.org/core/name"Biochem Pharmacol"xsd:string
http://purl.uniprot.org/citations/18619574http://purl.uniprot.org/core/pages"543-551"xsd:string
http://purl.uniprot.org/citations/18619574http://purl.uniprot.org/core/title"The relative contribution of human cytochrome P450 isoforms to the four caffeine oxidation pathways: an in vitro comparative study with cDNA-expressed P450s including CYP2C isoforms."xsd:string
http://purl.uniprot.org/citations/18619574http://purl.uniprot.org/core/volume"76"xsd:string
http://purl.uniprot.org/citations/18619574http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/18619574
http://purl.uniprot.org/citations/18619574http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/18619574
http://purl.uniprot.org/uniprot/P08684#attribution-411441DA125C53FD36776D3185E9752Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18619574
http://purl.uniprot.org/uniprot/P10632#attribution-411441DA125C53FD36776D3185E9752Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18619574
http://purl.uniprot.org/uniprot/P11712#attribution-411441DA125C53FD36776D3185E9752Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18619574
http://purl.uniprot.org/uniprot/P05177#attribution-411441DA125C53FD36776D3185E9752Fhttp://purl.uniprot.org/core/sourcehttp://purl.uniprot.org/citations/18619574
http://purl.uniprot.org/uniprot/#_P05177-mappedCitation-18619574http://www.w3.org/1999/02/22-rdf-syntax-ns#objecthttp://purl.uniprot.org/citations/18619574
http://purl.uniprot.org/uniprot/P05177http://purl.uniprot.org/core/mappedCitationhttp://purl.uniprot.org/citations/18619574