Literature DB >> 2552475

A calcium independent on-off switch for cardiac force generators.

S Winegrad1, A Weisberg, L E Lin, G McClellan.   

Abstract

Developed force and ATPase activity of actomyosin in cardiac muscle are regulated not only by the concentration of cytosolic calcium, but also by the state of the contractile proteins. In this study, it has been shown that cardiac actomyosin ATPase, even in the presence of adequate Ca, can exist in an inactive state. Micromolar cyclic AMP activates the ATPase, inducing substantial enzymatic activity. Both active and inactive forms of myosin can co-exist in the same cells. Mammalian hearts appear to contain a physiological mechanism for altering the response of actomyosin to optimal concentrations of Ca.

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Year:  1989        PMID: 2552475

Source DB:  PubMed          Journal:  Prog Clin Biol Res        ISSN: 0361-7742


  3 in total

1.  In situ compartmentation of creatine kinase in intact sarcomeric muscle: the acto-myosin overlap zone as a molecular sieve.

Authors:  G Wegmann; E Zanolla; H M Eppenberger; T Wallimann
Journal:  J Muscle Res Cell Motil       Date:  1992-08       Impact factor: 2.698

Review 2.  Intracellular compartmentation, structure and function of creatine kinase isoenzymes in tissues with high and fluctuating energy demands: the 'phosphocreatine circuit' for cellular energy homeostasis.

Authors:  T Wallimann; M Wyss; D Brdiczka; K Nicolay; H M Eppenberger
Journal:  Biochem J       Date:  1992-01-01       Impact factor: 3.857

3.  For myosin light chain phosphatase, a very small subunit can make very big differences in the heart.

Authors:  William J Pearce
Journal:  Am J Physiol Heart Circ Physiol       Date:  2018-03-23       Impact factor: 4.733

  3 in total

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