Wednesday, May 24, 2017

Carbonylation of atrial myosin prolongs its interaction with actin

G. Kopylova, S. Nabiev, D. Shchepkin, S. Bershitsky

Carbonylation induced by hyperthyroidism suppresses force generation of skeletal myosin and sliding velocity of actin filaments in an in vitro motility assay. However, its effects on cardiac myosin at the molecular level have not been studied. Hyperthyroidism induces a change in expression of myosin heavy chains in ventricles, which may mask the effect of oxidation. In contrast to ventricular myosin, expression of myosin heavy chains in the atrium does not change upon hyperthyroidism and enables investigation of the effect of oxidation on cardiac myosin. We studied the influence of carbonylation, a type of protein oxidation, on the motor function of atrial myosin and Ca2+ regulation of actin-myosin interaction at the level of isolated proteins and single molecules using an in vitro motility assay and an optical trap. Carbonylation of atrial myosin prolonged its attached state on actin and decreased maximal sliding velocity of thin filaments over this myosin but did not affect the calcium sensitivity of the velocity. The results indicate that carbonylation of atrial myosin induced by hyperthyroidism can be a rate-limiting factor of atrium contractility and so participates in the genesis of heart failure in hyperthyroidism.

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