title: Ca-independent regulation of cardiac myosin.
abstract: Calcium-independent regulation of the contractile proteins of cardiac muscle has been studied using hyperpermeable cells from rat ventricles and sections of quickly frozen rat hearts. These preparations have been used to study maximum Ca-activated force, myosin ATPase activity and the maximum velocity of unloaded shortening. Beta adrenergic activity increases the amount of force and the ATPase activity in accordance with the concentration of the V1 isozyme of myosin. V3 activity is decreased at the same time. In tissues containing only V1, there is no change in maximum velocity in response to beta adrenergic stimulation. These results indicate that beta adrenergic stimulation recruits V1 force generators and probably regulates a transition between a Ca unresponsive and a Ca responsive force generator. A 21,000 dalton protein that reproduces the effect of beta adrenergic stimulation on myosin has been isolated.
authors.affiliation: Department of Physiology, School of Medicine, University of Pennsylvania, Philadelphia 19104-6085.
authors.forename: S
authors.initials: S
authors.lastname: Winegrad
authors.forename: G
authors.initials: G
authors.lastname: McClellan
authors.forename: A
authors.initials: A
authors.lastname: Weisberg
authors.forename: L E
authors.initials: LE
authors.lastname: Lin
authors.forename: S
authors.initials: S
authors.lastname: Weindling
authors.forename: R
authors.initials: R
authors.lastname: Horowits
mesh_terms: D000251:Adenosine Triphosphatases / Q000378:metabolism*; D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D006352:Heart Ventricles / Q000201:enzymology; D008954:Models, Biological; D009200:Myocardial Contraction / Q000187:drug effects; D009206:Myocardium / Q000201:enzymology*; D009218:Myosins / Q000378:metabolism*; D051381:Rats
chemical_list: D000251:Adenosine Triphosphatases; D009218:Myosins; D002118:Calcium