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Effect of extraction of myosin binding protein C on contractility of rat heart

I. Kulikovskaya,¹ G. McClellan,¹ R. Levine,^2, and S. Winegrad¹

¹Department of Physiology, University of Pennsylvania, School of Medicine, Philadelphia 19104-6085; and ²Department of Neurobiology and Anatomy, MCP-Hahnemann University, Philadelphia, Pennsylvania 19129

Submitted 4 October 2002 ; accepted in final form 28 April 2003

Human hearts with reduced or mutant myosin binding protein C (MyBP-C) undergo hypertrophy and dilation, suggesting that reduction or alteration of MyBP-C interferes with normal contraction. Extraction of 60–70% of MyBP-C over 1 h from a mechanically disrupted cardiac myocyte has been shown to increase Ca sensitivity but does not appear to impair development of maximum Ca-activated force (F_max). To determine whether loss of MyBP-C over a longer period of time will decrease force development in a reversible manner, MyBP-C has been extracted from chemically skinned rat cardiac trabeculae for 1–4 h, and force production, Ca sensitivity, and thick filament structure were measured. Although extraction of MyBP-C for 1 h did not alter F_max, after 4 h, myosin heads became disordered and F_max decreased. At this point, incubation of the trabeculae with rat cardiac MyBP-C in a relaxing solution reversed the decline in F_max and most of the change in order of myosin heads. Extraction of MyBP-C appears to produce a change in the orientation of myosin heads that is associated with a decreased ability of the contractile system to develop force.

thick filament structure; cardiomyopathy; filament stability

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