Basal myosin light chain phosphorylation is a determinant of Ca2+ sensitivity of force and activation dependence of the kinetics of myocardial force development

American Journal of Physiology. Heart and Circulatory Physiology
M Charlotte OlssonR L Moss

Abstract

It is generally recognized that ventricular myosin regulatory light chains (RLC) are approximately 40% phosphorylated under basal conditions, and there is little change in RLC phosphorylation with agonist stimulation of myocardium or altered stimulation frequency. To establish the functional consequences of basal RLC phosphorylation in the heart, we measured mechanical properties of rat skinned trabeculae in which approximately 7% or approximately 58% of total RLC was phosphorylated. The protocol for achieving approximately 7% phosphorylation of RLC involved isolating trabeculae in the presence of 2,3-butanedione monoxime (BDM) to dephosphorylate RLC from its baseline level. Subsequent phosphorylation to approximately 58% of total was achieved by incubating BDM-treated trabeculae in solution containing smooth muscle myosin light chain kinase, calmodulin, and Ca2+ (i.e., MLCK treatment). After MLCK treatment, Ca2+ sensitivity of force increased by 0.06 pCa units and maximum force increased by 5%. The rate constant of force development (ktr) increased as a function of Ca2+ concentration in the range between pCa 5.8 and pCa 4.5. When expressed versus pCa, the activation dependence of ktr appeared to be unaffected by MLCK treatment...Continue Reading

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Citations

Dec 30, 2009·The Journal of Biological Chemistry·Audrey N ChangJames T Stull
Jun 23, 2010·The Journal of Biological Chemistry·Michelle S ParvatiyarJames D Potter
May 14, 2008·The Journal of Biological Chemistry·Jian HuangJames T Stull
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Aug 16, 2006·The Journal of General Physiology·Julian E StelzerRichard L Moss
Jun 17, 2008·American Journal of Physiology. Heart and Circulatory Physiology·Chao YuanR John Solaro
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