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Am J Physiol Cell Physiol 281: C1059-C1063, 2001;
0363-6143/01 $5.00
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Vol. 281, Issue 3, C1059-C1063, September 2001

Protein kinase Cepsilon contributes to regulation of the sarcolemmal Na+-K+ pump

Kerrie A. Buhagiar1,2, Peter S. Hansen1,2, Nerida L. Bewick1, and Helge H. Rasmussen1,2

1 Department of Cardiology, Royal North Shore Hospital, and 2 University of Sydney, Sydney, New South Wales, Australia 2065

A reduction in angiotensin II (ANG II) in vivo by treatment of rabbits with the angiotensin-converting enzyme inhibitor, captopril, increases Na+-K+ pump current (Ip) of cardiac myocytes. This increase is abolished by exposure of myocytes to ANG II in vitro. Because ANG II induces translocation of the varepsilon -isoform of protein kinase C (PKCvarepsilon ), we examined whether this isozyme regulates the pump. We treated rabbits with captopril, isolated myocytes, and measured Ip of myocytes voltage clamped with wide-tipped patch pipettes. Ip of myocytes from captopril-treated rabbits was larger than Ip of myocytes from controls. ANG II superfusion of myocytes from captopril-treated rabbits decreased Ip to levels similar to controls. Inclusion of PKCvarepsilon -specific blocking peptide in pipette solutions used to perfuse the intracellular compartment abolished the effect of ANG II. Inclusion of psi varepsilon RACK, a PKCvarepsilon -specific activating peptide, in pipette solutions had an effect on Ip that was similar to that of ANG II. There was no additive effect of ANG II and psi varepsilon RACK. We conclude that PKCvarepsilon regulates the sarcolemmal Na+-K+ pump.

intracellular sodium; protein kinase C isozymes; cardiac myocytes; angiotensin; cardiac hypertrophy


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