Journal
CIRCULATION JOURNAL
Volume 77, Issue 9, Pages 2218-2225Publisher
JAPANESE CIRCULATION SOC
DOI: 10.1253/circj.CJ-13-0627
Keywords
Ca2+/calmodulin; Muscle contraction; Myosin light chain kinase; Regulatory myosin light chain
Categories
Funding
- Japan Society for the Promotion of Science (JSPS) through the Funding Program for Next Generation World Leading Researchers (NEXT Program),
- Ministry of Health, Labor, and Welfare-Japan
- Ministry of Education, Culture, Sports, Science, and Technology-Japan
- Japan Heart Foundation
- Japan Cardiovascular Research Foundation
- Japan Foundation of Applied Enzymology
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Cardiac-specific myosin light chain kinase (cMLCK) is the kinase predominantly responsible for the maintenance of the basal level of phosphorylation of cardiac myosin light chain 2 (MLC2), which it phosphorylates at Ser-15. This phosphorylation repels the myosin heads from the thick myosin filament and moves them toward the thin actin filament. Unlike smooth muscle cells, MLC2 phosphorylation in striated muscle cells appears to be a positive modulator of Ca2+ sensitivity that shifts the Ca2+-force relationship toward the left and increases the maximal force response and thus does not initiate muscle contraction. Recent studies have revealed an increasing number of details of the biochemical, physiological, and pathophysiological characteristics of cMLCK. The combination of recent technological advances and the discovery of a novel class of biologically active nonstandard peptides will hopefully translate into the development of drugs for the treatment of heart diseases.
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