Protein kinase C epsilon translocates to the Receptor for Activated C‐Kinase upon adenosine A1 receptor stimulation of the rat myocardium

TL;DRAbstract

Protein kinase C epsilon (PKCε) in the heart plays an important role in adenosine‐induced anti‐adrenergic effects mediated by the adenosine A 1 receptor (A 1 R). PKCε translocates to the transverse tubules (TT) of myocytes with A 1 R stimulation (AJP 287:H1721, 2004). Since the Receptor for Activated C‐Kinase (RACK2) resides in the TT we investigated whether PKCε translocates to RACK2 with A 1 R stimulation of rat ventricular myocytes and perfused hearts using the A 1 R agonist chlorocyclopentyladenosine (CCPA). Myocytes were exposed to primary rabbit PKCε and mouse RACK2 antibodies with secondaries conjugated to Texas red and Cy5, respectively. A scanning confocal microscope showed that CCPA caused PKCε to co‐localize with RACK2. RACK2 was immunoprecipitated (IP) from extracts of hearts perfused with ZM‐241385 (1 μM, ZM), an adenosine A 2A R antagonist, and stimulated with either CCPA, phenylisoproplyadenosine (PIA) or phorbol 12‐myristate 13‐acetate (Pb) at 1 μM. As assessed by Weste

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