Picture of virus under microscope

Research under the microscope...

The Strathprints institutional repository is a digital archive of University of Strathclyde research outputs.

Strathprints serves world leading Open Access research by the University of Strathclyde, including research by the Strathclyde Institute of Pharmacy and Biomedical Sciences (SIPBS), where research centres such as the Industrial Biotechnology Innovation Centre (IBioIC), the Cancer Research UK Formulation Unit, SeaBioTech and the Centre for Biophotonics are based.

Explore SIPBS research

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

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 0014-5793

Full text not available in this repository. (Request a copy from the Strathclyde author)

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.