Calcium/calmodulin-dependent protein kinase II activity is increased in sarcoplasmic reticulum from coronary artery ligated rabbit hearts

S Currie, G L Smith

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39 Citations (Scopus)

Abstract

A protein kinase activity intrinsic to the sarcoplasmic reticulum was studied in normal and hypertrophied rabbit hearts. The relationship between this kinase activity and phospholamban phosphorylation was examined. Calmodulin-dependent kinase II activity was found to be increased in sarcoplasmic reticulum preparations from hypertrophied hearts compared with normal. This was evident by measuring the phosphotransferase activity of the kinase and also by examining phospholamban phosphorylation by electrophoretic band shift analysis. Increased phospholamban phosphorylation by Calmodulin-dependent protein kinase II was dependent on prior phosphorylation by cAMP-dependent protein kinase, indicating potential crosstalk. Specific immunoblot analysis of the rabbit sarcoplasmic reticulum identified the presence of the delta form of calmodulin dependent protein kinase II and showed it to be up-regulated in hypertrophied hearts.
Original languageEnglish
Pages (from-to)244-248
Number of pages5
JournalFEBS Letters
Volume459
Issue number2
DOIs
Publication statusPublished - 8 Oct 1999

Keywords

  • sarcoplasmic reticulum
  • heart failure
  • calmodulin-dependent kinase
  • phospholamban
  • Ca2+ regulation

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