In vitro metabolism of KBH-A40, a novel δ-lactam-based histone deacetylase (HDAC) inhibitor, in human liver microsomes and serum

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dc.contributor.authorHwan Mook Kim-
dc.contributor.authorSoo Jin Oh-
dc.contributor.authorSong Kyu Park-
dc.contributor.authorG Han-
dc.contributor.authorK J Kim-
dc.contributor.authorK S Lee-
dc.contributor.authorJong Soon Kang-
dc.contributor.authorM Nam-
dc.contributor.authorKiho Lee-
dc.date.accessioned2017-04-19T09:09:39Z-
dc.date.available2017-04-19T09:09:39Z-
dc.date.issued2008-
dc.identifier.issn0049-8254-
dc.identifier.uri10.1080/00498250701813222ko
dc.identifier.urihttps://oak.kribb.re.kr/handle/201005/8331-
dc.description.abstract1. The metabolism of KBH-A40, a novel δ-lactam-based histone deacetylase (HDAC) inhibitor, was investigated in vitro using human liver microsomes and serum. After 60-min incubation in human liver microsomes with β-nicotinamide adenine dinucleotide phosphate (NADPH) or uridine diphosphate glucuronic acid (UDPGA), the residual KBH-A40 was 90.6% ± 5.1% and 28.9% ± 2.0% (t1/2 = 26 min), respectively, suggesting that KBH-A40 is likely predominantly metabolized by glucuronidation, rather than by cytochrome P450 (CYP)-mediated oxidation. Consistently, KBH-A40 glucuronide was the only metabolite identified following incubations of KBH-A40 with human liver microsomes in the presence of both NADPH and UDPGA. 2. KBH-A40 was not notably degraded when incubated with human serum for 60 min. In contrast, KBH-A40 was rapidly hydrolysed to its carboxylic acid form in rat serum (t1/2 = 13 min). 3. Taken collectively, the results suggest that KBH-A40 is likely metabolized in man predominantly by glucuronidation of its hydroxamic acid moiety, with negligible biotransformation elsewhere in the molecule.-
dc.publisherT&F (Taylor & Francis)-
dc.titleIn vitro metabolism of KBH-A40, a novel δ-lactam-based histone deacetylase (HDAC) inhibitor, in human liver microsomes and serum-
dc.title.alternativeIn vitro metabolism of KBH-A40, a novel δ-lactam-based histone deacetylase (HDAC) inhibitor, in human liver microsomes and serum-
dc.typeArticle-
dc.citation.titleXenobiotica-
dc.citation.number3-
dc.citation.endPage293-
dc.citation.startPage281-
dc.citation.volume38-
dc.contributor.affiliatedAuthorHwan Mook Kim-
dc.contributor.affiliatedAuthorSoo Jin Oh-
dc.contributor.affiliatedAuthorSong Kyu Park-
dc.contributor.affiliatedAuthorK J Kim-
dc.contributor.affiliatedAuthorK S Lee-
dc.contributor.affiliatedAuthorJong Soon Kang-
dc.contributor.affiliatedAuthorKiho Lee-
dc.contributor.alternativeName김환묵-
dc.contributor.alternativeName오수진-
dc.contributor.alternativeName박성규-
dc.contributor.alternativeName한균희-
dc.contributor.alternativeName김강전-
dc.contributor.alternativeName이계숙-
dc.contributor.alternativeName강종순-
dc.contributor.alternativeName-
dc.contributor.alternativeName이기호-
dc.identifier.bibliographicCitationXenobiotica, vol. 38, no. 3, pp. 281-293-
dc.identifier.doi10.1080/00498250701813222-
dc.subject.keywordGlucuronidation-
dc.subject.keywordHistone deacetylase-
dc.subject.keywordHydrolysis-
dc.subject.keywordHydroxamic acid glucuronidation-
dc.subject.keywordKBH-A40-
dc.subject.localGlucuronidation-
dc.subject.localglucuronidation-
dc.subject.localHistone deacetylase-
dc.subject.localhistone deacetylase (HDAC)-
dc.subject.localHistone deacetylases-
dc.subject.localhistone deacetylase-
dc.subject.localHydrolysis-
dc.subject.localhydrolysis-
dc.subject.localHydroxamic acid glucuronidation-
dc.subject.localKBH-A40-
dc.description.journalClassY-
Appears in Collections:
Ochang Branch Institute > Division of National Bio-Infrastructure > Laboratory Animal Resource & Research Center > 1. Journal Articles
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