Currie, S and Smith, G L (1999) Calcium/calmodulin-dependent protein kinase II activity is increased in sarcoplasmic reticulum from coronary artery ligated rabbit hearts. FEBS Letters, 459 (2). pp. 244-248. ISSN 0014-5793Full text not available in this repository. (Request a copy from the Strathclyde author)
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.
|Keywords:||sarcoplasmic reticulum, heart failure, calmodulin-dependent kinase, phospholamban, Ca2+ regulation, Pharmacy and materia medica, Biochemistry, Structural Biology, Cell Biology, Genetics, Molecular Biology, Biophysics|
|Subjects:||Medicine > Pharmacy and materia medica|
|Department:||Faculty of Science > Strathclyde Institute of Pharmacy and Biomedical Sciences|
|Depositing user:||Pure Administrator|
|Date Deposited:||02 Aug 2012 09:45|
|Last modified:||07 Jan 2017 01:20|