Identification of casein kinase II as a major endogeneous caldesmon kinase in sheep aorta smooth muscle

FEBS Letters

Gusev, Nikolai B.⁴  Collins, John H.²  Vorotniko, Alexander V.¹  Redwood, Charles S.³  Hua, Suming²  Marston, Steven B.³ 

[1] Institute of Experimental Cardiology, Russian National Cardiology Centre, Moscow 121552, Russian Federation;Department of Biological Chemistry, School of Medicine and Medical Biotechnology Center, Maryland Biotechnology Institute, University of Maryland, Baltimore, MD 21201, USA;Department of Cardiac Medicine, National Heart and Lung Institute, Dovehouse St., London, SW3 6LY, UK;Department of Biochemistry, School of Biology, Moscow State University, Moscow 119899, Russian Federation

关键词: Caldesmon;    Smooth muscle;    Phosphorylation;    Casein kinase II;   

DOI  :  10.1016/0014-5793(93)81671-L

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A caldesmon kinase activity was detected in an ATP extract of the myofibril-like pellet from sheep aorta. The enzyme was purified 745-fold and was identified as casein kinase II on the basis of molecular size, substrate specificity, and high sensitivity to heparin inhibition. Casein kinase II phosphorylated isolated caldesmon and caldesmon incorporated into native thin filaments, and transferred about 1 mol of phosphate per mol of caldesmon-h. Ser-73 was the main site phosphorylated by casein kinase II in chicken gizzard caldesmon. Phosphorylation of caldesmon reduced its affinity for smooth muscle myosin but had no effect upon the ability of caldesmon to inhibit the ATPase activity of actomyosin.

【 授权许可】

Unknown