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pubmed-article:1332493pubmed:abstractTextActivation of protein kinase C (PKC) modulates the mobilization of intracellular Ca2+ induced by extracellular ATP in rat ventricular myocytes. Pretreatment of myocytes with PKC activators attenuated both the ATP-induced Ca2+ transient and the noradrenergic potentiation of the Ca2+ response. Various PKC activators decreased both the basal cAMP level and the cAMP levels that had been elevated by norepinephrine, forskolin, or 3-isobutyl-1-methylxanthine. The inhibitory effects of PKC activators were reversed by the PKC inhibitor staurosporine. The ATP-induced Ca2+ response is an integrated response resulting from ATP eliciting an inward cation current (IATP), cellular depolarization, Ca2+ influx through Ca2+ channels, and Ca2+ release from the sarcoplasmic reticulum. We used the whole cell voltage-clamp technique to investigate which steps of this integrated response are affected by PKC. PKC activators did not significantly affect the IATP. In contrast, PKC activators decreased the basal Ca2+ current (ICa) or Ba2+ current and the beta-adrenergic-stimulated ICa. These results suggest that PKC-induced suppression of the ATP-induced Ca2+ response and the beta-adrenergic-potentiated Ca2+ response is achieved at least partially by decreasing the intracellular cAMP level and ICa.lld:pubmed
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pubmed-article:1332493pubmed:authorpubmed-author:LevyM NMNlld:pubmed
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pubmed-article:1332493pubmed:authorpubmed-author:ZhengJ SJSlld:pubmed
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pubmed-article:1332493pubmed:dateRevised2009-11-19lld:pubmed
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pubmed-article:1332493pubmed:articleTitleCa2+ mobilization by extracellular ATP in rat cardiac myocytes: regulation by protein kinase C and A.lld:pubmed
pubmed-article:1332493pubmed:affiliationDepartment of Physiology and Biophysics, School of Medicine, Case Western Reserve University, Cleveland, Ohio 44106.lld:pubmed
pubmed-article:1332493pubmed:publicationTypeJournal Articlelld:pubmed
pubmed-article:1332493pubmed:publicationTypeResearch Support, U.S. Gov't, P.H.S.lld:pubmed
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