Protein kinase Cepsilon interacts with and inhibits the permeability transition pore in cardiac mitochondria

Although functional coupling between protein kinase Cepsilon (PKCepsilon) and mitochondria has been implicated in the genesis of cardioprotection, the signal transduction mechanisms that enable this link and the identities of the mitochondrial proteins modulated by PKCepsilon remain unknown. Based o...

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Veröffentlicht in:	Circulation research 2003-05, Vol.92 (8), p.873-880
Hauptverfasser:	Baines, Christopher P, Song, Chang-Xu, Zheng, Yu-Ting, Wang, Guang-Wu, Zhang, Jun, Wang, Ou-Li, Guo, Yiru, Bolli, Roberto, Cardwell, Ernest M, Ping, Peipei
Format:	Artikel
Sprache:	eng
Schlagworte:	Animals Atractyloside - pharmacology Enzyme Inhibitors - pharmacology Hexokinase - genetics Hexokinase - metabolism Immunoblotting Intracellular Membranes - physiology Mice Mice, Transgenic Mitochondria, Heart - drug effects Mitochondria, Heart - metabolism Mitochondrial ADP, ATP Translocases - antagonists & inhibitors Mitochondrial ADP, ATP Translocases - genetics Mitochondrial ADP, ATP Translocases - metabolism Myocardial Infarction - etiology Myocardial Infarction - metabolism Myocardial Infarction - pathology Myocardial Reperfusion Injury - complications Permeability Phosphorylation Porins - genetics Porins - metabolism Precipitin Tests Protein Binding Protein Kinase C - genetics Protein Kinase C - metabolism Protein Kinase C-epsilon Rats Voltage-Dependent Anion Channel 1 Voltage-Dependent Anion Channels
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