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PubMed · 150668

[Age peculiarities of actomyosin enzymic properties in embryogenesis].

N A Lebedeva·A L Solov'ev·L F Efimova
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Abstract

Age changes in the subunits composition were comparatively studied for protein, ATPase activity, sensitivity to Ca2+ in low concentrations and alkaline activation of ATPase of natural actomyosin of skeletal muscles and myocardium in cattle feti. A rise in values in the process of the mentioned parameters development is established for actomyosin of skeletal muscles. The rise is especially considerable by the end of embryonic development. Correspondingly the myocardium actomyosin possesses a lower ATPase activity and higher sensitivity to Ca2+ in low concentrations. The ATPase activity rises moderately with development.

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ActomyosinAdenosine TriphosphatasesAgingAnimalsCalciumCattleEmbryo, MammalianHeartKineticsMuscle DevelopmentMusclesMyocardiumEnglish AbstractJournal Article

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N A Lebedeva, A L Solov'ev, L F Efimova. [Age peculiarities of actomyosin enzymic properties in embryogenesis].. https://pubmed.ncbi.nlm.nih.gov/150668/

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Adenosine 3':5'-monophosphate-mediated inhibition of myosin light chain phosphorylation in bovine aortic actomyosin.

Ca2+-dependent phosphorylation of the myosin light chains in bovine aortic native actomyosin is markedly depressed in the presence of cyclic AMP and its dependent protein kinase. This inhibition occurs with either cardiac, skeletal, or aortic protein kinase plus cyclic AMP, while little or no inhibition occurs with either cyclic AMP or protein kinase alone. The extent of inhibition is related to the concentration of protein kinase and approaches a maximum of approximately 50%. Concomitant with the inhibition of myosin light chain phosphorylation is (a) an increased phosphorylation of a 100,000-dalton moiety which possibly corresponds to the myosin light chain kinase present in the native actomyosin preparation and (b) a decrease in the actomyosin Mg2+-ATPase activity. These findings suggest that modulation of actin-myosin interactions by the cAMP system directly at the level of the contractile proteins may represent a mechanism by which beta adrenergic relaxation occurs in mammalian vascular smooth muscle.

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