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The influence of P‐light chain phosphorylation by myosin light chain kinase on the calcium sensitivity of chemically skinned heart fibres
Author(s) -
Morano I.,
Hofmann F.,
Zimmer M.,
Rüegg J.C.
Publication year - 1985
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(85)81027-9
Subject(s) - myosin light chain kinase , immunoglobulin light chain , phosphorylation , contractility , calmodulin , chemistry , calcium , biophysics , myosin , protein kinase a , biochemistry , endocrinology , biology , organic chemistry , antibody , immunology
Phosphorylation of the P‐light chain of myosin might be involved in the regulation of cardiac contractility. Thus an enhanced phosphorylation level of the P‐light chain catalyzed by Ca 2+ ‐calmodulin‐dependent myosin light chain kinase (MLCK) increased significantly the Ca 2+ sensitivity of chemically skinned ventricular fibre bundles of the pig. This effect was reversible. Whereas force development at submaximal Ca 2+ concentration (pCa 5.5) increased by ~ 50% in the presence of MLCK, maximum tension achieved at maximum Ca 2+ ‐concentration (pCa 4.3) was not affected.