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Myosin-Binding Protein C (MyBP-C) in Cardiac Muscle and Contractility

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Molecular and Cellular Aspects of Muscle Contraction

Part of the book series: Advances in Experimental Medicine and Biology ((AEMB,volume 538))

Abstract

Myosin binding protein C (MyBP-C) was first discovered in skeletal muscle by Offer et al, (1973), and subsequent work from several laboratories (Koretz 1979, Craig and Offerl976, Davies 1988, Sciler et al 1996, Sebillon et al 2001) has shown that it can play an important role in the formation of normal thick filaments in skeletal muscle. In its absence, isolated myosin does not form thick filaments with uniform thickness, uniform length or helically ordered myosin heads (Koretz 1079, Rhee et al 1994, Lin et al 1994). Surprisingly, cardiac muscle from mice with MyBP-C knocked out form normally appearing sarcomeres and myofibrils (Harris et al 2002), raising the possibility that some form of compensation has occurred or formation of thick filaments differs between cardiac and skeletal muscle.

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Winegrad, S. (2003). Myosin-Binding Protein C (MyBP-C) in Cardiac Muscle and Contractility. In: Sugi, H. (eds) Molecular and Cellular Aspects of Muscle Contraction. Advances in Experimental Medicine and Biology, vol 538. Springer, Boston, MA. https://doi.org/10.1007/978-1-4419-9029-7_3

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  • DOI: https://doi.org/10.1007/978-1-4419-9029-7_3

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-4764-4

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