PKC alpha-Specific Phosphorylation of the Troponin Complex in Human Myocardium: A Functional and Proteomics Analysis

V. Kooij, P.B. Zhang, S.R. Piersma, V. Sequeira Oliveira, N. Boontje, P.J.M. Wijnker, C.R. Jimenez, K.E. Jaquet, C. dos Remedios, A.M. Murphy, J.E. van Eyk, J. van der Velden, G.J.M. Stienen

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Aims:Protein kinase Cα (PKCα) is one of the predominant PKC isoforms that phosphorylate cardiac troponin. PKCα is implicated in heart failure and serves as a potential therapeutic target, however, the exact consequences for contractile function in human myocardium are unclear. This study aimed to investigate the effects of PKCα phosphorylation of cardiac troponin (cTn) on myofilament function in human failing cardiomyocytes and to resolve the potential targets involved.Methods and Results:Endogenous cTn from permeabilized cardiomyocytes from patients with end-stage idiopathic dilated cardiomyopathy was exchanged (∼69%) with PKCα-treated recombinant human cTn (cTn (DD+PKCα)). This complex has Ser23/24 on cTnI mutated into aspartic acids (D) to rule out in vitro cross-phosphorylation of the PKA sites by PKCα. Isometric force was measured at various [Ca
Original languageEnglish
Article numbere74847
Number of pages10
Issue number10
Publication statusPublished - 2013

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