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Delta protein kinase C interacts with the d subunit of the F1F0 ATPase in neonatal cardiac myocytes exposed to hypoxia or phorbol ester. Implications for F1F0 ATPase regulation

Delta protein kinase C interacts with the d subunit of the F1F0 ATPase in neonatal cardiac myocytes exposed to hypoxia or phorbol ester. Implications for F1F0 ATPase regulation

Journal of Biological Chemistry 283(44): 29831-29840

Mitochondrial protein kinase C isozymes have been reported to mediate both cardiac ischemic preconditioning and ischemia/reperfusion injury. In addition, cardiac preconditioning improves the recovery of ATP levels after ischemia/reperfusion injury. We have, therefore, evaluated protein kinase C modulation of the F(1)F(0) ATPase in neonatal cardiac myocytes. Exposure of cells to 3 or 100 nM 4beta-phorbol 12-myristate-13-acetate induced co-immunoprecipitation of delta protein kinase C (but not alpha, epsilon, or zeta protein kinase C) with the d subunit of the F(1)F(0) ATPase. This co-immunoprecipitation correlated with 40+/-3% and 72+/-9% inhibitions of oligomycin-sensitive F(1)F(0) ATPase activity, respectively. We observed prominent expression of delta protein kinase C in cardiac myocyte mitochondria, which was enhanced following a 4-h hypoxia exposure. In contrast, hypoxia decreased mitochondrial zetaPKC levels by 85+/-1%. Following 4 h of hypoxia, F(1)F(0) ATPase activity was inhibited by 75+/-9% and delta protein kinase C co-immunoprecipitated with the d subunit of F(1)F(0) ATPase. In vitro incubation of protein kinase C with F(1)F(0) ATPase enhanced F(1)F(0) activity in the absence of protein kinase C activators and inhibited it in the presence of activators. Recombinant delta protein kinase C also inhibited F(1)F(0) ATPase activity. Protein kinase C overlay assays revealed delta protein kinase C binding to the d subunit of F(1)F(0) ATPase, which was modulated by diacylglycerol, phosphatidylserine, and cardiolipin. Our results suggest a novel regulation of the F(1)F(0) ATPase by the delta protein kinase C isozyme.

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Accession: 052480151

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PMID: 18725417

DOI: 10.1074/jbc.m801642200

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