TAILIEUCHUNG - 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

Malonyl-CoA, a potent inhibitor of carnitine pamitoyl transferase-I (CPT-I), plays a pivotal role in fuel selection in cardiac muscle. Malonyl-CoA decarboxylase (MCD) cata-lyzes the degradation of malonyl-CoA, removes a potent allosteric inhibition on CPT-I and thereby increases fatty acid 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() and consti-tutively active AMPK () inH9c2 cells, using an adenoviral gene delivery approach in order to examine if MCDis regulated by AMPK. . | Eur. J. Biochem. 271 2831-2840 2004 FEBS 2004 doi 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 Nandakumar Sambandam Michael Steinmetz Angel Chu Judith Y. Altarejos Jason R. B. Dyck and Gary D. Lopaschuk Department of Pediatrics Faculty of Medicine Dentistry University of Alberta Edmonton Canada Malonyl-CoA a potent inhibitor of carnitine pamitoyl transferase-I CPT-I plays a pivotal role in fuel selection in cardiac muscle. Malonyl-CoA decarboxylase MCD catalyzes the degradation of malonyl-CoA removes a potent allosteric inhibition on CPT-I and thereby increases fatty acid oxidation in the heart. Although MCD las Severn 1 SSc Thr phosphorylation sites whether it is regulated by AMP-activated protein kinase AMPK has been controversial. We therefore overexpressed MCD Ad-MCDa and conili-tutively active AMPK in H9c2 cells using an adenoviral gene delivery approach in order to examine if MCDis regulated by AMPK. Cells infected with demonstrated a fourfold increase in AMPK activity as compared with control cells expressing green fluorescent protein . MCD activity increased 40- to 50-fold in cells whnn Compared wíth control. Co-expressing AMPK with MCD fw-ther augmented MCDexpression and activity in eeHs compared wíth the contl ol. subeelhflar fractionation further revealed that kDa isofocm of MCD expression was significantly higher in cytosolic fractions of eeUs than of the control. However the MCDactivities in cytosolic fractions were not different between the two groups. Interestingly in the mitochondrial fractions MCDactivity significantly increased in cells when compared with eeHs. Using phosphoserine and .

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