Clinical Physiology of Circulation

Chief Editor

Leo A. Bockeria, MD, PhD, DSc, Professor, Academician of Russian Academy of Sciences, President of Bakoulev National Medical Research Center for Cardiovascular Surgery


Subcellular distribution and content of myosin noncanonical light chain kinase in human myocardium

Authors: Chadin A. V., Raevskaya A. A., Bledzhans D. A., Muratov R. M., Stepanova O. V.

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Link: Clinical Physiology of Blood Circulaiton. 2008; (): -

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Abstract

Cardiomyocytes of human myocardium contain sarcomeric myosin and non-muscle myosin type IIB (NMIIB). The phosphorylation plays important role in the development and the contraction of cardiomyocytes. It is known that the myosin light chain kinase is the basic enzyme which phosphorylates myosin in myocardium. However a number of the novel protein kinases were shown recently to phosphorylate myosin. Among these enzymes are ROCK (RhoA- activated kinase), ILK (integrin-linked kinase), ZIPK (zipper interacting protein kinase) and DAPK (death-associated protein kinase). We have determined the localization of these kinases in human cardiomyocytes using immunofluorescence approach. It was found that these protein kinases localize in the Z-lines of sarcomeres. We studied the content of ILK and ZIPK in normal human myocardium and papillary muscles of the patients with hypertrophy of different ethiology. The content of these protein kinases in hypertrophic myocardium is higher compared with normal heart. Our data could reflect an involvement of ROCK, ILK, ZIPK and DAPK in normal functioning of myocardium and hypertrophy of human heart.

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