DC Field | Value | Language |
---|---|---|
dc.contributor.author | Hwan Mook Kim | - |
dc.contributor.author | Soo Jin Oh | - |
dc.contributor.author | Song Kyu Park | - |
dc.contributor.author | G Han | - |
dc.contributor.author | K J Kim | - |
dc.contributor.author | K S Lee | - |
dc.contributor.author | Jong Soon Kang | - |
dc.contributor.author | M Nam | - |
dc.contributor.author | Kiho Lee | - |
dc.date.accessioned | 2017-04-19T09:09:39Z | - |
dc.date.available | 2017-04-19T09:09:39Z | - |
dc.date.issued | 2008 | - |
dc.identifier.issn | 0049-8254 | - |
dc.identifier.uri | 10.1080/00498250701813222 | ko |
dc.identifier.uri | https://oak.kribb.re.kr/handle/201005/8331 | - |
dc.description.abstract | 1. 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.publisher | T&F (Taylor & Francis) | - |
dc.title | In vitro metabolism of KBH-A40, a novel δ-lactam-based histone deacetylase (HDAC) inhibitor, in human liver microsomes and serum | - |
dc.title.alternative | In vitro metabolism of KBH-A40, a novel δ-lactam-based histone deacetylase (HDAC) inhibitor, in human liver microsomes and serum | - |
dc.type | Article | - |
dc.citation.title | Xenobiotica | - |
dc.citation.number | 3 | - |
dc.citation.endPage | 293 | - |
dc.citation.startPage | 281 | - |
dc.citation.volume | 38 | - |
dc.contributor.affiliatedAuthor | Hwan Mook Kim | - |
dc.contributor.affiliatedAuthor | Soo Jin Oh | - |
dc.contributor.affiliatedAuthor | Song Kyu Park | - |
dc.contributor.affiliatedAuthor | K J Kim | - |
dc.contributor.affiliatedAuthor | K S Lee | - |
dc.contributor.affiliatedAuthor | Jong Soon Kang | - |
dc.contributor.affiliatedAuthor | Kiho Lee | - |
dc.contributor.alternativeName | 김환묵 | - |
dc.contributor.alternativeName | 오수진 | - |
dc.contributor.alternativeName | 박성규 | - |
dc.contributor.alternativeName | 한균희 | - |
dc.contributor.alternativeName | 김강전 | - |
dc.contributor.alternativeName | 이계숙 | - |
dc.contributor.alternativeName | 강종순 | - |
dc.contributor.alternativeName | 남 | - |
dc.contributor.alternativeName | 이기호 | - |
dc.identifier.bibliographicCitation | Xenobiotica, vol. 38, no. 3, pp. 281-293 | - |
dc.identifier.doi | 10.1080/00498250701813222 | - |
dc.subject.keyword | Glucuronidation | - |
dc.subject.keyword | Histone deacetylase | - |
dc.subject.keyword | Hydrolysis | - |
dc.subject.keyword | Hydroxamic acid glucuronidation | - |
dc.subject.keyword | KBH-A40 | - |
dc.subject.local | Glucuronidation | - |
dc.subject.local | glucuronidation | - |
dc.subject.local | Histone deacetylase | - |
dc.subject.local | histone deacetylase (HDAC) | - |
dc.subject.local | Histone deacetylases | - |
dc.subject.local | histone deacetylase | - |
dc.subject.local | Hydrolysis | - |
dc.subject.local | hydrolysis | - |
dc.subject.local | Hydroxamic acid glucuronidation | - |
dc.subject.local | KBH-A40 | - |
dc.description.journalClass | Y | - |
There are no files associated with this item.
Items in OpenAccess@KRIBB are protected by copyright, with all rights reserved, unless otherwise indicated.