NDLI: Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle.

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Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle.

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Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Winegrad, S. Weisberg, A.
Description	Author Affiliation: Weisberg A ( Department of Physiology, School of Medicine, University of Pennsylvania, Philadelphia 19104-6085, USA.);
Abstract	In addition to the contractile proteins actin and myosin, contractile filaments of striated muscle contain other proteins that are important for regulating the structure and the interaction of the two force-generating proteins. In the thin filaments, troponin and tropomyosin form a Ca-sensitive trigger that activates normal contraction when intracellular Ca is elevated. In the thick filament, there are several myosin-binding proteins whose functions are unclear. Among these is the myosin-binding protein C (MBP-C). The cardiac isoform contains four phosphorylation sites under the control of cAMP and calmodulin-regulated kinases, whereas the skeletal isoform contains only one such site, suggesting that phosphorylation in cardiac muscle has a specific regulatory function. We isolated natural thick filaments from cardiac muscle and, using electron microscopy and optical diffraction, determined the effect of phosphorylation of MBP-C on cross bridges. The thickness of the filaments that had been treated with protein kinase A was increased where cross bridges were present. No change occurred in the central bare zone that is devoid of cross bridges. The intensity of the reflections along the 43-nm layer line, which is primarily due to the helical array of cross bridges, was increased, and the distance of the first peak reflection from the meridian along the 43-nm layer line was decreased. The results indicate that phosphorylation of MBP-C (i) extends the cross bridges from the backbone of the filament and (ii) increases their degree of order and/or alters their orientation. These changes could alter rate constants for attachment to and detachment from the thin filament and thereby modify force production in activated cardiac muscle.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	17
Volume Number	93
Language	English
Publisher	National Academy of Sciences
Publisher Date	1996-10-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Carrier Proteins Metabolism Myocardium Ultrastructure Myofibrils Myosins Animals Crystallography Cyclic AMP Cyclic AMP-Dependent Protein Kinases Negative Staining Periodicity Phosphorylation Subcellular Fractions Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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