Studies on phosphorylation of canine cardiac sarcoplasmic reticulum by calmodulin-dependent protein kinase

L. M. Bilezikjian, E. G. Kranias, J. D. Potter, A. Schwartz

Research output: Contribution to journalArticlepeer-review

59 Scopus citations

Abstract

Two endogenous protein kinase activities, cAMP-dependent and calmodulin-Ca2+-dependent, are associated with isolated cardiac sarcoplasmic reticulum (SR) vesicles. Both kinases posphorylate an endogenous substrate of ~22,000 daltons (phospholamban). The phosphorylation of phospholamban by either the intrinsic or by exogenous cAMP-dependent protein kinase is found to be Ca2+-independent between 0.05 and 100 μM free Ca2+. Calmodulin-dependent phosphorylation, on the other hand, does not require cAMP and is absolutely dependent on the presence of free Ca2+ over a concentration range that corresponds to physiological levels (10

Original languageEnglish (US)
Pages (from-to)1356-1362
Number of pages7
JournalCirculation research
Volume49
Issue number6
DOIs
StatePublished - 1981

ASJC Scopus subject areas

  • Physiology
  • Cardiology and Cardiovascular Medicine

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