Protein kinase C{varepsilon} contributes to regulation of the sarcolemmal Na+-K+ pump |
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Authors: | Buhagiar, Kerrie A. Hansen, Peter S. Bewick, Nerida L. Rasmussen, Helge H. |
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Abstract: | A reduction in angiotensinII (ANG II) in vivo by treatment of rabbits with theangiotensin-converting enzyme inhibitor, captopril, increasesNa+-K+ pump current (Ip)of cardiac myocytes. This increase is abolished by exposure of myocytesto ANG II in vitro. Because ANG II induces translocation of the-isoform of protein kinase C (PKC), we examined whether thisisozyme regulates the pump. We treated rabbits with captopril, isolatedmyocytes, and measured Ip of myocytes voltageclamped with wide-tipped patch pipettes. Ip ofmyocytes from captopril-treated rabbits was larger thanIp of myocytes from controls. ANG II superfusionof myocytes from captopril-treated rabbits decreasedIp to levels similar to controls. Inclusion ofPKC-specific blocking peptide in pipette solutions used to perfusethe intracellular compartment abolished the effect of ANG II. Inclusionof RACK, a PKC-specific activating peptide, in pipettesolutions had an effect on Ip that was similarto that of ANG II. There was no additive effect of ANG II andRACK. We conclude that PKC regulates the sarcolemmalNa+-K+ pump. |
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