Báo cáo khoa học: Malonyl-CoA decarboxylase (MCD) is differentially regulated in subcellular compartments by 5¢AMP-activated protein kinase (AMPK) Studies using H9c2 cells overexpressing MCD and AMPK by adenoviral gene transfer technique
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Malonyl-CoA, a potent inhibitor of carnitine pamitoyltransferase-I (CPT-I), plays a pivotal role in fuel selection incardiac muscle. Malonyl-CoA decarboxylase (MCD) cata-lyzes the degradation of malonyl-CoA, removes a potentallosteric inhibition on CPT-I and thereby increases fattyacid oxidation in the heart. Although MCDhas several Ser/Thr phosphorylation sites, whether it is regulated by AMP-activated protein kinase (AMPK) has been controversial.We therefore overexpressed MCD(Ad.MCD) and consti-tutively active AMPK (Ad.CA-AMPK) inH9c2 cells, usingan adenoviral gene delivery approach in order to examine ifMCDis regulated by AMPK. ...
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Báo cáo khoa học: Malonyl-CoA decarboxylase (MCD) is differentially regulated in subcellular compartments by 5¢AMP-activated protein kinase (AMPK) Studies using H9c2 cells overexpressing MCD and AMPK by adenoviral gene transfer technique
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Báo cáo khoa học: Malonyl-CoA decarboxylase (MCD) is differentially regulated in subcellular compartments by 5¢AMP-activated protein kinase (AMPK) Studies using H9c2 cells overexpressing MCD and AMPK by adenoviral gene transfer technique
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