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• W2039147530 abstract "Protein kinase C (PKC) appears to be a common intracellular effector and signal collector during cardiac preconditioning; however, it remains unknown whether agonists that activate different PKC isoforms are also linked to select aspects of myocardial protection. Using agonists that are known to activate unique combinations of PKC isoforms, we interogated the relationship between isoform activation and the different aspects (pH, function, and viability) of endogenous myocardial protection. To study this, isolated rat hearts were subjected to ischemia–;reperfusion (I/R) (20 min/40 min), without (control = Ctrl) or with receptor-dependent [phenylephrine (PE), 50 μM;adenosine (ADO), 125 μM] or -independent [phorbol myristate acetate (PMA), 100 nM] activation of PKC. Function, pH, and viability were assessed by rate pressure product (%RPP) and coronary flow (CF; ml/min), by31P NMR, and by CF creatine kinase (CK; U/liter) leak, respectively. PMA, which activates PKCδ but not η, resulted in intracellular pH (pHi) and viability protection, but did not protect against postischemic myocardial stunning. ADO, which activates PKCη but not δ, protects against stunning, but not acidosis or necrosis. PE, which activates PKCδ and η, provided global myocardial protection against necrosis, acidosis, and stunning. Different PKC isoforms may be linked to distinct aspects of myocardial protection. Targeted activation of PKC isoforms may allow precise mechanistic application of preconditioning-like myocardial protection." @default.
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• W2039147530 date "1997-04-01" @default.
• W2039147530 modified "2023-10-16" @default.
• W2039147530 title "Protein Kinase C Isoform Diversity in Preconditioning" @default.
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• W2039147530 doi "https://doi.org/10.1006/jsre.1997.5072" @default.
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