Tip60 might be a candidate for the acetylation of hepatic carbonic anhydrase I and III in mice

dc.contributor.authorBaltacı, Nurdan Gönül
dc.contributor.authorKoçpınar, Enver Fehim
dc.contributor.authorBudak, Harun
dc.date.accessioned2021-10-19T10:09:52Z
dc.date.available2021-10-19T10:09:52Z
dc.date.issued2021en_US
dc.departmentMeslek Yüksekokulları, Sağlık Hizmetleri Meslek Yüksekokulu, Tıbbi Hizmetler ve Teknikler Bölümüen_US
dc.description.abstractBackground Carbonic anhydrases (CAs) play a significant role in maintaining pH balance by catalyzing the conversion of carbon dioxide to bicarbonate. The regulation of pH is critical for all living organisms. Although there are many studies in the literature on the biochemical, functional, and structural features of CAs, there is not sufficient information about the epigenetic regulation of CAs. Methods and results The lysine acetyltransferase TIP60 (60 kDa Tat-interactive protein) was knocked out specifically in mouse liver using the Cre/loxP system, and knockout rate was shown as 83–88% by Southern blot analysis. The impact of Tip60 on the expression of Ca1, Ca3, and Ca7 was investigated at six Zeitgeber time (ZT) points in the control and liverspecific Tip60 knockout mice (mutant) groups by real-time PCR. In the control group, while Ca1 showed the highest expression at ZT8 and ZT12, the lowest expression profile was observed at ZT0 and ZT20. Hepatic Ca1 displayed robust circadian expression. However, hepatic Ca3 exhibited almost the same level of expression at all ZT points. The highest expression of Ca7 was observed at ZT12, and the lowest expression was determined at ZT4. Furthermore, hepatic Ca7 also showed robust circadian expression. The expression of Ca1 and Ca3 significantly decreased in mutant mice at all time periods, but the expression of Ca7 used as a negative control was not affected. Conclusions It was suggested for the first time that Tip60 might be considered a candidate protein in the regulation of the Ca1 and Ca3 genes, possibly by acetylation.en_US
dc.identifier.issn0301-4851
dc.identifier.scopus2-s2.0-85116999193
dc.identifier.scopusqualityQ2
dc.identifier.urihttps://doi.org/10.1007/s11033-021-06753-8
dc.identifier.urihttps://hdl.handle.net/20.500.12639/2929
dc.identifier.wosWOS:000707301700002
dc.identifier.wosqualityQ4
dc.indekslendigikaynakWeb of Science
dc.indekslendigikaynakScopus
dc.indekslendigikaynakPubMed
dc.institutionauthorKoçpınar, Enver Fehim
dc.language.isoen
dc.publisherSpringeren_US
dc.relation.ispartofMolecular Biology Reportsen_US
dc.relation.publicationcategoryMakale - Uluslararası Hakemli Dergi - Kurum Öğretim Elemanıen_US
dc.rightsinfo:eu-repo/semantics/openAccessen_US
dc.subjectCarbonic anhydrasesen_US
dc.subjectTip60en_US
dc.subjectAcetylationen_US
dc.subjectCircadian rhythmen_US
dc.subjectMiceen_US
dc.titleTip60 might be a candidate for the acetylation of hepatic carbonic anhydrase I and III in miceen_US
dc.typeArticle

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