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

FEBS Letters

Smith, Godfrey L¹  Currie, Susan¹ 

[1]Institute of Biomedical and Life Sciences, West Medical Building, University of Glasgow, Glasgow G12 8QQ, UK

关键词: Sarcoplasmic reticulum;    Heart failure;    Calmodulin-dependent kinase;    Phospholamban;    Ca2+ regulation;    HEPES;    4-[2-hydroxyethyl]-1-piperazine-ethanesulphonic acid;    DTT;    dithiothreitol;    PMSF;    phenylmethylsulphonyl fluoride;    SDS-PAGE;    sodium dodecyl sulphate polyacrylamide gel electrophoresis;    MOPS;    3-[N-morpholino]propanesulphonic acid;   

DOI  :  10.1016/S0014-5793(99)01254-5

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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 δ form of calmodulin dependent protein kinase II and showed it to be up-regulated in hypertrophied hearts.

【 授权许可】

Unknown