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

Conference paper
Part of the Advances in Experimental Medicine and Biology book series (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.

Keywords

Cardiac Muscle Thin Filament Myosin Head Layer Line Thick Filament 
These keywords were added by machine and not by the authors. This process is experimental and the keywords may be updated as the learning algorithm improves.

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References

  1. Bonne, G., Carrier, L, Bercovici, J., Cruard, C., Richard, P., Hainque, B., Gautel, M., Labiet, S., James, M., Beckman, J., Weissenbach, J., Vosberg, HP., Fiszman, M., Komajda, M., Schwartz, K. 1995 Cardiac myosin binding protein C gene splice acceptor site mutation is associated with familial hypertrophie cardiomyopathy. Nature Genet. 11:438–440.PubMedCrossRefGoogle Scholar
  2. Carrier, L., Bonne, G., Bahrend, E., Yu, B., Richard, P., Niel, F., Hainque, B., Cruard, C, Gary, F., Labiet, S., Bouhour, J-B., Dubourg, O., Desnos, M., Hagege, A., Trent, Komajda, M, Fiszman, M., Schwartz, K. Organization and sequence of human cardiac myosin binding protein C gene (MyBP-C3) and identification of the mutations predicted to produce truncated proteins in familial hypertrophie cardiomyopathy. Circ. Res. 80: 427–434, 1997.PubMedGoogle Scholar
  3. Craig, R., and Offer, G. 1976.The location of C-protein in rabbit skeletal muscle. Proc. R. Soc. (Lond) 192:451–461CrossRefGoogle Scholar
  4. Davies, J. 1988 Interaction of C-protein with pH 8.0 synthetic thick filaments prepared from the myosin of vertebrate skeletal muscle. J. Muse. Res. Cell Motil. 9:174–183CrossRefGoogle Scholar
  5. Flavigny, J, Souchet. M, Sebillon P, Berrebi-Bertrand I, Hainque B, Mallet A, Bril A, Schwartz K, And Carrier L. 1999. COOH-terminal truncated cardiac myosin binding protein C mutants resulting from familial hypertrophie cardiomyopathy mutations exhibit altered expression and/or incorporation into fetal rat cardiomyocytes. J. Mol. Biol. 294: 443–456.PubMedCrossRefGoogle Scholar
  6. Gautel, M., Zuffardi, O., Freiberg, A., and Labeit, S. 1995. Phosphorylation switches specific for the cardiac isoforms of myosin binding protein C: a modulator of cardiac contraction. EMBO J. 14: 1952–1960.PubMedGoogle Scholar
  7. Gilbert, R., Kelly, M.G., Mikawa, T., and Fischman, D. A 1996. The carboxyl terminus of myosin binding protein-C (MyBP-C), C-protein) specifies incorporation into the A-band of striated muscle. J. Cell Sc. 109: 101–111.Google Scholar
  8. Gruen, M., and Gautel, M.. 1999 Mutations in beta-myosin S2 that cause familial hypertrophie cardiomyopathy (FHC) abolish the interaction with the regulatory domain of myosin binding protein-C., J.Mol. Biol. 286, 933–949.PubMedCrossRefGoogle Scholar
  9. Gruen, M, Prinz, H, and Gautel, M. 1999 cAPK-phosphorylation controls the interaction of the regulatory domain of cardiac myosin binding protein C with myosin-S2 in an on-off fashion. FEBS Letters. 453(3):254–259.PubMedCrossRefGoogle Scholar
  10. Harris, SP., Bartley, CR., Hacker, TA,. McDonald, KS., Douglas, PS,. Greaser, ML,. Powers, PA., Moss, RL. 2002; Hypertrophie cardiomyopathy in cardiac myosin binding protein-C knockout mice. Circulation Research. 90:594–601.PubMedCrossRefGoogle Scholar
  11. Hartzell, C., and Glass, D. 1984. Phosphorylation of purified cardiac muscle protein by purified cAMP-dependent and endogenous Ca-calmodulin-dependent protein kinases. J. Biol. Chem 259: 15587–15596.PubMedGoogle Scholar
  12. Hofmann, PA, Hartzell, HC and Moss, RL. 1991 Alterations in Ca sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibers. J. Gen. Physiol. 97: 1141–1163.PubMedCrossRefGoogle Scholar
  13. Koretz, J. F. 1979. Effects of C-protein on synthetic myosin filament structure. Biophys. J. 27: 433–446.PubMedCrossRefGoogle Scholar
  14. Kunst, G., Kress, K.R., Gruen, M, Uttenweiler, D., Gautel, M., and Fink, R.H.A.. 2000. MyBP-C (C-Protein)-a phosphorylation dependent force regulator in muscle that controls the attachment of myosin heads by its interaction with myosin — S2. Circ. Res 86: 51–58.PubMedCrossRefGoogle Scholar
  15. Levine, R.J.C., Weisberg A., Kulikovskaya, I., McClellan, G. and Winegrad, S. 2001. Multiple structures of thick filaments in resting cardiac muscle and their influence on cross bridge interactions. Biophys. J. 81: 1070–1082.PubMedCrossRefGoogle Scholar
  16. Lin, Z., Lu, M.H Schultheiss, T., Choi, J., Holtzer, S., DiLuulo, C, Fischman, D.A., and Holtzer, H. 1994. Sequential appearance of muscle-specific proteins in myoblasts as a function of time after cell division: evidence for a conserved myoblast differentiation program in skeletal muscle. Cell Motil. Cytoskel. 29: 1–19.CrossRefGoogle Scholar
  17. Matsubara, I., Yagi, N., Endoh, M. 1979 Movement of myosin heads during a heart beat. Nature 278: 474–476.PubMedCrossRefGoogle Scholar
  18. McClellan, G, Weisberg, A., and Winegrad, S. 1994. CAMP can raise or lower cardiac actomyosin ATPase activity depending on alpha adrenergic activity. Amer. J. Physiol. 267: H431–442PubMedGoogle Scholar
  19. McClellan, G, Kulikovskaya, I. and Winegrad, S.2001 Structural and functional responses of the contractile proteins to changes in calcium concentration in the heart. Biophys. J. 81: 1083–1092PubMedCrossRefGoogle Scholar
  20. Moolman-Smook J., Flashman, E., de Lange, W., Li, Z., Corfield, V., Redwood, C, Wathins, H. 2002. Idnentification of novel interactions between domains of myosin binding protein C that are modulated by hypertrophic cardiomyopathy missense mutations Circ. Res. 91: 704–711.Google Scholar
  21. Offer, G., Moos, C., and Starr, R. 1973. A new protein of the thick filaments of vertebrate skeletal myofibrils. Extraction, purification and characterization. J. Mol. Biol.; 74: 653–676.PubMedCrossRefGoogle Scholar
  22. Okagaki, T., Weber, F.E., Fischman, D.A, Vaughan, K.T., Mikawa, T., and Reinach, F.C. 1993. The major myosin binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 repeat. J. Cell Biol. 123: 619–626.PubMedCrossRefGoogle Scholar
  23. Rhee, D. Sänger, J.M., and Sanger, J.W. 1994. The premyofibril: evidence for its role in myofibrillogenesis. Cell Motil. Cytoskel. 28: 1–24.CrossRefGoogle Scholar
  24. Rottbauer, W., Gautel, M., Zehelein, J., Labeit, S., Franz, W.M., Fischer, C, Vollrath, B., Mall, G., Dietz, R., Kubier, W., Katus, H.A. Novel splice donor site mutation in the cardiac myosin-binding protein C gene in familail hypertrophic cardiomyopathy. Charaterization of cardiac transcript and protein. J. Clin. Invest. 100:475–482. 1997PubMedCrossRefGoogle Scholar
  25. Sebillon, P, Bonne, G, Flavigny, J, Venin, S, Rouche, A, Fiszman, M, Vikstrom, K, Leinwand, L, Carrier, L, Schwartz, K. 2001 COOH-terminal truncated human cardiac MyBP-C alters myosin filament organization. Comp. Rendus Acad. Sc. 324: 251–260.CrossRefGoogle Scholar
  26. Schlender K. and Bean L. 1991. Phosphorylation of chicken cardiac C protein by calcium calmodulin-dependent protein kinase II. J. Biol. Chem. 266: 2811–281PubMedGoogle Scholar
  27. Schwartz, K., Carrier, L., Guicheney, P., Komajda, M. 1995 The molecular basis of cardiomyopathies. Circulation 1: 1336–1347.Google Scholar
  28. Sciler, S.H., Fischman, D.A, Leinwand, L.A 1996 Modulation of myosin filament organization by C protein family members. Molec. Biol. Cell 7: 113–127.Google Scholar
  29. Starr, R. and Offer, G. 1978 The interaction of C-protein with heavy meromyosin and subfragment-2. Biochem. J. 171: 813–816.PubMedGoogle Scholar
  30. Watkins, H, Conner, D, Thierfelder, L, Jarcho, JA, MacCrea, C, McKenna, WJ, Maron, BJ, Scidman, JG, Scidman CE. 1995; Mutations in the cardiac myosin binding protein C on chromosome 11 cause familial hypertrophie cardiomyopathy. Nat. Genetics 1: 433–438.CrossRefGoogle Scholar
  31. Weisberg, A., and Winegrad, S. 1996. Alteration in myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle. Proc. Nat. Acad. Sc (USA) 93: 8999–9003.CrossRefGoogle Scholar
  32. Weisberg, A., and Winegrad, S. 1998. Relation between cross bridge structure and actomyosin ATPase activity in rat heart. Circ. Res. 1998; 83: 60–72PubMedCrossRefGoogle Scholar
  33. Winegrad, S. 1999. Cardiac myosin binding protein C. Circ. Res. 84: 1117–1126.PubMedCrossRefGoogle Scholar

Copyright information

© Springer Science+Business Media New York 2003

Authors and Affiliations

  1. 1.Saul Winegrad, Department of PhysiologySchool of Medicine, University of PennsylvaniaPhiladelphiaUSA

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