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The C-protein (myosin binding protein C) family: Regulators of contraction and sarcomere formation?

  • P. M. Bennett
  • D. O. Fürst
  • M. Gautel
Chapter
Part of the Reviews of Physiology, Biochemistry and Pharmacology book series (REVIEWS, volume 138)

Keywords

Myosin Heavy Chain Myosin Head Thick Filament Rabbit Psoas Myosin Binding Protein 
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. Alyonycheva, T. N., T. Mikawa, F. C. Reinach, and D. A. Fischman (1997) Isoformspecific interaction of the myosin-binding proteins (MyBPs) with skeletal and cardiac myosin is a property of the C-terminal immunoglobulin domain. J Biol Chem 272:20866–20872PubMedGoogle Scholar
  2. Bähler, M., H. M. Eppenberger, and T. Wallimann (1985a) Novel thick filament protein of chicken pectoralis muscle: the 86K protein. I. Purification and characterization. J Mol Biol 186: 381–391PubMedGoogle Scholar
  3. Bähler, M., H. M. Eppenberger, and T. Wallimann (1985b) Novel thick filament protein of chicken pectoralis muscle: the 86K protein. II. Distribution and localization. J Mol Biol 186:393–401PubMedGoogle Scholar
  4. Bähler, M., H. Moser, H. M. Eppenberger, and T. Wallimann (1985c) Heart C-protein is transiently expressed during skeletal muscle development in the embryo, but persists in cultured myogenic cells. J Muscle Res Cell Mot 112:345–352Google Scholar
  5. Beall, C. J., and E. Fyrberg (1991) Muscle abnormalities in Drosophila melanogaster heldup mutants are caused by missing or aberrant troponin-I isoforms. J Cell Biol 114:941–951PubMedGoogle Scholar
  6. Bennett, P., R. Craig, R. Starr, and G. Offer (1986) The ultrastructural location of C-protein, X-protein and H-protein in rabbit muscle. J Muscle Res Cell Motil 7:550–567PubMedGoogle Scholar
  7. Bennett, P., R. Starr, A. Elliott, and G. Offer (1985) The structure of C-protein and X-protein molecules and a polymer of X-protein. J Mol Biol 184:297–309PubMedGoogle Scholar
  8. Bonne, G., L. Carrier, J. Bercovici, C. Cruaud, P. Richard, B. Hainque, M. Gautel, S. Labeit, M. James, J. Beckmann, J. Weissenbach, H.-P. Vosberg, M. Fiszman, M. Komajada, and K. Schwartz, K. (1995) Cardiac myosin binding protein-C gene splice acceptor site mutation is associated with familial hypertrophic cardiomyopathy. Nat Genet 11:438–440PubMedGoogle Scholar
  9. Bordas, J., G. P. Diakun, J. E. Harries, R. A. Lewis, G. R. Mant, M. L. Martin-Fernandez, and E. Towns-Andrews (1991) Two-dimensional time resolved X-ray diffraction of muscle: recent results. Adv Biophys 27:15–33PubMedGoogle Scholar
  10. Callaway, J. E., and P. J. Bechtel (1981) C-protein from rabbit soleus (red) muscle. Biochem J 195:463–469PubMedGoogle Scholar
  11. Carrier, L., G. Bonne, E. Bahrend, B. Yu, P. Richard, F. Niel, B. Hainque, C. Cruaud, F. Gary, S. Labeit, J. B. Bouhour, O. Dubourg, M. Desnos, A. A. Hagege, R. J. Trent, M. Komajda, M. Fiszman, and K. Schwartz (1997) Organization and sequence of human cardiac myosin binding protein C gene (MYBPC3) and identification of mutations predicted to produce truncated proteins in familial hypertrophic cardiomyopathy. Circ Res 80:427–434PubMedGoogle Scholar
  12. Carrier, L., G. Bonne, and K. Schwartz (1998) Cardiac Myosin-binding protein C and hypertrophic cardiomyopathy. Trends Cardiovasc Med 8:151Google Scholar
  13. Craig, R. (1977) Structure of A-segments from frog and rabbit skeletal muscle. J Mol Biol 109:69–81PubMedGoogle Scholar
  14. Craig, R., L. Alamo, and R. Padron (1992) Structure of the myosin filaments of relaxed and rigor vertebrate striated muscle studied by rapid freezing electron microscopy. J Mol Biol 228:474–487PubMedGoogle Scholar
  15. Craig, R., and J. Megerman. (1979) Electron microscope studies of muscle thick filaments. In ‘Motility in Cell Function’. Proc. J. M. Marshall Symp. Cell Biol, F. A. Pepe, J. W. Sanger and V. T. Nachmias, editors. Academic Press, NY, London pp 92–102Google Scholar
  16. Craig, R., and G. Offer (1976) The localization of C-protein in rabbit skeletal muscle. Proc R Soc, London 192:451–461Google Scholar
  17. Davis, J. S. (1988) Interaction of C-protein with pH 8.0 synthetic thick filaments prepared from the myosin of vertebrate skeletal muscle. J Musc Res Cell Motil 9:174–183Google Scholar
  18. Dennis, J. E., T. Shimizu, F. C. Reinach, and D. A. Fischman (1984) Localization of C-protein isoforms in chicken skeletal muscle: ultrastructural detection using monoclonal antibodies. J Cell Biol 98:1514–1522PubMedGoogle Scholar
  19. Dhoot, G. K., M. C. Hales, B. M. Grail, and S. V. Perry (1985) The isoforms of C protein and their distribution in mammalian skeletal muscle. J Musc Res Cell Motil 6:487–505Google Scholar
  20. Einheber, S., and D. A. Fischman (1990) Isolation and characterization of a cDNA clone encoding avian skeletal muscle C-protein: an intracellular member of the immunoglobulin superfamily. Proc Natl Acad Sci USA 87:2157–2161PubMedGoogle Scholar
  21. Fougerousse, F., A. L. Delezoide, M. Y. Fiszman, K. Schwartz, J. S. Beckmann, and L. Carrier (1998) Cardiac myosin binding protein C gene is specifically expressed in heart during murine and human development. Circ Res 82:130–133PubMedGoogle Scholar
  22. Freiburg, A., and M. Gautel (1996) A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur J Biochem 235:317–323PubMedGoogle Scholar
  23. Fürst, D. O., R. Nave, M. Osborn, and K. Weber (1989) Repetitive titin epitopes with a 42 nm spacing coincide in relative position with known A band striations also identified by major myosin-associated proteins; an immunoelectron microscopical study on myofibrils. J Cell Biol 94:119–125Google Scholar
  24. Fürst, D. O., U. Vinkemeier, and K. Weber (1992) Mammalian skeletal muscle C-protein: purification from bovine muscle, binding to titin and the characterization of a full length human cDNA. J Cell Sci 102:769–778PubMedGoogle Scholar
  25. Fyrberg, E., C. C. Fyrberg, C. Beall, and D. L. Saville (1990) Drosophila melanogaster troponin-T mutations engender three distinct syndromes of myofibrillar abnormalities. J Mol Biol 216:657–675PubMedGoogle Scholar
  26. Gautel, M., D. O. Fürst, A. Cocco, and S. Schiaffino (1998) Isoform transitions of the myosin binding protein C family in developing human and mouse muscles: lack of isoform transcomplementation in cardiac muscle. Circ Res 82:124–129PubMedGoogle Scholar
  27. Gautel, M., O. Zuffardi, A. Freiburg, and S. Labeit (1995) Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: a modulator of cardiac contraction? EMBO J 14:1952–1960PubMedGoogle Scholar
  28. Gilbert, R., M. G. Kelly, T. Mikawa, and D. A. Fischman (1996) The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorporation into the A-band of striated muscle. J Cell Sci 101–111Google Scholar
  29. Hanson, J., E. J. O’Brien, and P. M. Bennett (1971) Structure of the myosincontaining filament assembly (A-segment) separated from frog skeletal muscle. J Mol Biol 58:865–871PubMedGoogle Scholar
  30. Harford, J. J., M. W. Chew, J. M. Squire, and E. Towns-Andrews (1991) Crossbridge states in isometrically contracting fish muscle: evidence for swinging of myosin heads on actin. Adv Biophys 27:45–61PubMedGoogle Scholar
  31. Hartzell, H. C., and D. B. Glass (1984) Phosphorylation of purified cardiac muscle C-protein by purified cAMP-dependent and endogenous Ca2+-calmodulindependent protein kinases. J Biol Chem 259:15587–15596PubMedGoogle Scholar
  32. Hartzell, H. C., and W. S. Sale (1985) Structure of C-protein purified from cardiac muscle. J Cell Biol 100:208–215PubMedGoogle Scholar
  33. Hartzell, H. C., and L. Titus (1982) Effects of cholinergic and adrenergic agonists on phosphorylation of 165,000-dalton myofibrillar protein in intact cardiac muscle. J Biol Chem 257:2111–2120PubMedGoogle Scholar
  34. Hofmann, P. A., H. C. Hartzell, and R. L. Moss (1991a) Alterations in Ca2+ sensitive tension due to partial extraction of C-protein from rat skinned cardiac myocytes and rabbit skeletal muscle fibres. J Gen Physiol 97:1141–1163PubMedGoogle Scholar
  35. Hofmann, P. A., M. L. Greaser, and R. L. Moss (1991b) C-protein limits shortening velocity of rabbit skeletal muscle fibres at low levels of Ca2+ activation. J Physiol 439:701–715PubMedGoogle Scholar
  36. Houmeida, A., J. Holt, L. Tskhovrebova, and J. Trinick (1995) Studies of the interaction between titin and myosin. J Cell Biol 131:1471–1481PubMedGoogle Scholar
  37. Huxley, H. E. (1967) Recent X-ray diffraction and electron microscope studies of striated muscle. J Gen Physiol 50:71–81PubMedGoogle Scholar
  38. Huxley, H. E., and W. Brown (1967) The low-angle X-ray diagram of vertebrate striated muscle and its behaviour during contraction and rigor. J Mol Biol 30:383–434PubMedGoogle Scholar
  39. Jeacocke, S. A., and P. J. England (1980) Phosphorylation of a myofibrillar protein of Mr 150 000 in perfused rat heart, and the tentative identifcation of this with C-protein. FEBS Lett 122:129–132PubMedGoogle Scholar
  40. Kasahara, H., M. Itoh, T. Sugiyama, N. Kido, H. Hayashi, H. Saito, S. Tsukita, and N. Kato (1994) Autoimmune myocarditis induced in mice by cardiac C-protein. Cloning of complementary DNA encoding murine cardiac C-protein and partial characterization of the antigenic peptides. J Clin Invest 94:1026–1036PubMedGoogle Scholar
  41. Kawashima, M., S. Kitani, T. Tanaka, and T. Obinata (1986) The earliest form of C-protein expressed during striated muscle development is immunologically the same as cardiac-type C-protein. J Biochem 99:1037–1047PubMedGoogle Scholar
  42. Kimura, A., H. Harada, J. E. Park, H. Nishi, M. Satoh, M. Takahashi, S. Hiroi, T. Sasaoka, N. Ohbuchi, T. Nakamura, T. Koyanagi, T. H. Hwang, J. A. Choo, K. S. Chung, A. Hasegawa, R. Nagai, O. Okazaki, H. Nakamura, M. Matsuzaki, T. Sakamoto, H. Toshima, Y. Koga, T. Imaizumi, and T. Sasazuki (1997) Mutations in the cardiac troponin I gene associated with hypertrophic cardiomyopathy. Nat Genet 16:379–382PubMedGoogle Scholar
  43. Kolmerer, B., N. Olivieri, C. C. Witt, B. G. Herrmann, and S. Labeit (1996) Genomic organization of M line titin and its tissue-specific expression in two distinct isoforms. J Mol Biol 256:556–563PubMedGoogle Scholar
  44. Koretz, J. F. (1979) Effect of C-protein on synthetic myosin filament structure. Biophys J 27:433–446PubMedGoogle Scholar
  45. Koretz, J. F., L. M. Coluccio, and A. M. Bertasso (1982) The aggregation characteristics of column-purified rabbit skeletal myosin in the presence and absence of C-protein at pH 7.0. Biophys J 37:433–440PubMedGoogle Scholar
  46. Labeit, S., and B. Kolmerer (1995) Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270:293–296PubMedGoogle Scholar
  47. Labeit, S., M. Gautel, A. Lakey and J. Trinick (1992) Towards a molecular understanding of titin. EMBO J 11:1711–1716PubMedGoogle Scholar
  48. Luther, P. K. (1998) Three dimensional structure of the A-band and localization of MyBP-C. Biophys J 74:A352Google Scholar
  49. Magid, A., H. P. Ting-Beall, M. Carvell, T. Kontis, and C. Lucaveche (1984) Connecting filaments, core filaments, and side-struts: a proposal to add three new loadbearing structures to the sliding filament model. Adv Exp Med Biol 170:307–328PubMedGoogle Scholar
  50. McCormick, K. M., K. M. Baldwin, and F. Schachat (1994) Coordinate changes in C protein and myosin expression during skeletal muscle hypertrophy. Am J Physiol C443–449Google Scholar
  51. Miyahara, M. and H. Noda (1980) Interaction of C-protein with myosin. J Biochem 87:1413–1420PubMedGoogle Scholar
  52. Moolman-Smook, J. C., B. Mayosi, P. Brink, and V. A. Corfield (1998) Identification of a new missense mutation in MyBP-C associated with hypertrophic cardiomyopathy. J Med Genet 35:253–254PubMedGoogle Scholar
  53. Moos, C., C. M. Mason, J. M. Besterman, I. M. Feng, and J. H. Dubin (1978) The binding of skeletal muscle C-protein to F-actin and its relation to the interaction of actin with myosin sub fragment-1. J Mol Biol 124:571–586PubMedGoogle Scholar
  54. Moos, C., G. Offer, R. Starr, and P. Bennett (1975) Interaction of C-protein with myosin, myosin rod and light meromyosin. J Mol Biol 97:1–9PubMedGoogle Scholar
  55. Morimoto, K., and W. F. Harrington (1973) Isolation and composition of thick filaments from rabbit skeletal muscle. J Mol Biol 77:165–175PubMedGoogle Scholar
  56. Morimoto, K., and W. F. Harrington (1974) Substructure of the thick filament of vertebrate striated muscle. J Mol Biol 82:83–97Google Scholar
  57. Murakami, U., K. Uchida, and T. Hiratsuka (1976) Cardiac myosin from pig heart ventricle. Purification and enzymatic properties. J Biochem 80: 611–619PubMedGoogle Scholar
  58. Niimura, H., L. L. Bachinski, S. Sangwatanaroj, H. Watkins, A. E. Chudley, W. McKenna, A. Kristinsson, R. Roberts, M. Sole, B. J. Maron, J. G. Seidman, and C. E. Seidman (1998) Mutations in the gene for cardiac myosin-binding protein C and lateonset familial hypertrophic cardiomyopathy. N Engl J Med 338:1248–1257PubMedGoogle Scholar
  59. Obermann, W. M., M. Gautel, F. Steiner, P. F. M. van der Ven, K. Weber, and D. O. Fürst (1996) The structure of the sarcomeric M band: localization of defined domains of myomesin, M-protein, and the 250-kD carboxy-terminal region of titin by immunoelectron microscopy. J Cell Biol 134:1441–1453PubMedGoogle Scholar
  60. Obermann, W. M., U. Plessmann, K. Weber, and D. O. Fürst (1995) Purification and biochemical characterization of myomesin, a myosinbinding and titin-binding protein, from bovine skeletal muscle. Eur J Biochem 233:110–115PubMedGoogle Scholar
  61. Obinata, T., M. Kawashima, S. Kitani, O. Saitoh, T. Masaki, D. M. Bader, and D. A. Fishman (1985) Expression of C-protein isoforms during chicken striated muscle development and its dependence on innervation. In ‘Molecular Biology of Muscle Development’. B. Nadal-Ginard and M. A. Q. Siddiqui, editors. Alan. R. Liss, New YorkGoogle Scholar
  62. Obinata, T., F. C. Reinach, D. M. Bader, T. Masaki, S. Kitani, and D. A. Fischman (1984) Immunochemical analysis of C-protein isoform transitions during the development of chicken skeletal muscle. Dev Biol 101:116–124PubMedGoogle Scholar
  63. Odermatt, E., J. W. Tamkun, and R. O. Hynes (1985) Repeating modular structure of the fibronectin gene: relationship to protein structure and subunit variation. Proc Natl Acad Sci USA 82:6571–6575PubMedGoogle Scholar
  64. Offer, G. (1972) C-protein and the periodicity in the thick filaments of vertebrate skeletal muscle. CSH Symp. Quant Biol 37:87–95Google Scholar
  65. Offer, G., C. Moos, and R. Starr (1973) A new protein of the thick filaments of vertebrate skeletal myofibrils. Extractions, purification and characterization. J Mol Biol 74:653–676PubMedGoogle Scholar
  66. Okagaki, T., F. E. Weber, D. A. Fischman, K. T. Vaughan, T. Mikawa, and F. C. Reinach (1993) The major myosin-binding domain of skeletal muscle MyBP-C (C protein) resides in the COOH-terminal, immunoglobulin C2 motif. J Cell Biol 123:619–626PubMedGoogle Scholar
  67. Pepe, F. A., P. K. Chowrashi, and P. R. Wachsberger (1975) Myosin filaments of skeletal and uterine muscle. In ‘Comparative Physiology — Functional Aspects of Structural Materials’. L. Bolis, H. P. Maddrell and K. Schmidt-Nielsen, editors. North-Holland, Amsterdam, pp 105–120Google Scholar
  68. Pepe, F. A. and B. Drucker (1975) The myosin filament. III. C-protein. J Mol Biol 99:609–617PubMedGoogle Scholar
  69. Reinach, F. C., T. Masaki, and D. A. Fischman (1983) Characterization of the C-protein from posterior latissimus dorsi muscle of the adult chicken: heterogeneity within a single sarcomere. J Cell Biol 96:297–300PubMedGoogle Scholar
  70. Reinach, F. C., T. Masaki, S. Shafiq, T. Obinata, and D. A. Fischman (1982) Isoforms of C-protein in adult chicken skeletal muscle: detection with monoclonal antibodies. J Cell Biol 95:78–84PubMedGoogle Scholar
  71. Rome, E., G. Offer, and F. A. Pepe (1973) X-ray diffraction of muscle labelled with antibody to C-protein. Nature New Biol 244:152–154PubMedGoogle Scholar
  72. Rottbauer, W., M. Gautel, J. Zehelein, S. Labeit, W. M. Franz, C. Fischer, B. Vollrath, G. Mall, R. Dietz, W. Kübler, and H. A. Katus (1997) Novel splice donor site mutation in the cardiac myosin-binding proteinC gene in familial hypertrophic cardiomyopathy. Characterization of cardiac transcript and protein. J Clin Invest 100:475–482PubMedGoogle Scholar
  73. Schlender, K. K., and L. J. Bean (1991) Phosphorylation of chicken cardiac C-protein by calcium/calmodulin-dependent protein kinase II. J Biol Chem 266:2811–2817PubMedGoogle Scholar
  74. Schultheiss, T., Z. X. Lin, M. H. Lu, J. Murray, D. A. Fischman, K. Weber, T. Masaki, M. Imamura, and H. Holtzer (1990) Differential distribution of subsets of myofibrillar proteins in cardiac nonstriated and striated myofibrils. J Cell Biol 110:1159–1172PubMedGoogle Scholar
  75. Schwartz, K., L. Carrier, P. Guicheney, and M. Komajda (1995) Molecular basis of familial cardiomyopathies. Circulation 91:532–540PubMedGoogle Scholar
  76. Schwarzbauer, J. E., R. S. Patel, D. Fonda, and R. 0. Hynes (1987) Multiple sites of alternative splicing of the rat fibronectin gene transcript. EMBO J 6:2573–2580PubMedGoogle Scholar
  77. Sjöström, M., and J. M. Squire (1977) Fine structure of the A-band in cryo-sections: the structure of the A-band of human skeletal muscle fibers from ultra-thin cryosections, negatively-stained. J Mol Biol 109:49–68PubMedGoogle Scholar
  78. Soteriou, A., M. Gamage, and J. Trinick (1993) A survey of interactions made by the giant protein titin. J Cell Sci 104:119–123PubMedGoogle Scholar
  79. Squire, J. M., M. Sjöström, and P. Luther (1976) Fine structure of the A-band in cryosections. II. Evidence for a length-determining protein in the thick filaments of vertebrate skeletal muscle. 6th Eur. Conf. Electron Microscopy, Jerusalem, pp 91–95Google Scholar
  80. Squire, J., A. C. Edman, A. Freundlich, J. Harford, and M. Sjöström (1982) Muscle structure, cryo-methods and image analysis. J Microsc 125:215–225PubMedGoogle Scholar
  81. Starr, R., R. Almond, and G. Offer (1985) Location of C-protein, H-protein and Xrotein in rabbit skeletal muscle fibre types. J Muscle Res Cell Motil 6:227–256PubMedGoogle Scholar
  82. Starr, R., and G. Offer (1971) Polypeptide chains of intermediate molecular weight in myosin preparations. FEBS Lett 15:40–44PubMedGoogle Scholar
  83. Starr, R., and G. Offer (1978) The interaction of C-protein with heavy meromyosin and subfragment-2. Biochem J 171:813–816PubMedGoogle Scholar
  84. Starr, R., and G. Offer (1982) Preparation of C-protein, H-protein, X-protein, and phosphofructokinase. Meth Enzymol 130–138Google Scholar
  85. Starr, R., and G. Offer (1983) H-protein and X-protein. Two new components of the thick filaments of vertebrate skeletal muscle. J Mol Biol 170:675–698PubMedGoogle Scholar
  86. Steiner, F., K. Weber, and D. O. Fürst (1998) Structure and expression of the gene encoding murine M-protein, a sarcomere-specific member of the immunoglobulin superfamily. Genomics 49:83–95PubMedGoogle Scholar
  87. Swan, R. C., and D. A. Fischman (1986) Electron microscopy of C-protein molecules from chicken skeletal muscle. J Muscle Res Cell Motil 7:160–166PubMedGoogle Scholar
  88. Sweeney, L. J., W. A. J. Clark, P. K. Umeda, R. Zak, and F. J. Manasek (1984) Immunofluorescence analysis of the primordial myosin detectable in embryonic striated muscle. Proc Natl Acad Sci USA 81:797–800PubMedGoogle Scholar
  89. Takano-Ohmuro, H., S. M. Goldfine, T. Kojima, T. Obinata, and D. A. Fischman (1989) Size and charge heterogeneity of C-protein isoforms in avian skeletal muscle. Expression of six different isoforms in chicken muscle. J Muscle Res Cell Motil 10:369–378PubMedGoogle Scholar
  90. Theiler, K. 1972. The house mouse. Springer Verlag Berlin Heidelberg New YorkGoogle Scholar
  91. Towbin, J. A. (1998) The role of cytoskeletal proteins in cardiomyopathies. Curr Opin Cell Biol 10:131–139PubMedGoogle Scholar
  92. Vaughan, K. T., F. E. Weber, S. Einheber, and D. A. Fischman (1993a) Molecular cloning of chicken myosin-binding protein (MyBP) H (86-kDa protein) reveals extensive homology with MyBP-C (C-protein) with conserved immunoglobulin C2 and fibronectin type III motifs. J Biol Chem 268:3670–3676PubMedGoogle Scholar
  93. Vaughan, K. T., F. E. Weber, T. Ried, D. C. Ward, F. C. Reinach, and D. A. Fischman (1993b) Human myosin-binding protein H (MyBP-H): complete primary sequence, genomic organization, and chromosomal localization. Genomics 16:34–40PubMedGoogle Scholar
  94. Vikström, K. L., and L. A. Leinwand (1996) Contractile protein mutations and heart disease. Curr Opin Cell Biol 8:97–105PubMedGoogle Scholar
  95. Ward, S. M., D. K. Dube, M. E. Fransen, and L. F. Lemanski (1996) Differential expression of C-protein isoforms in the developing heart of normal and cardiac lethal mutant axolotls (Ambystoma mexicanum). Dev Dyn 205:93–103PubMedGoogle Scholar
  96. Ward, S. M., L. F. Lemanski, U. N. Erginel, D. K. Dube, and N. Eiginel-Unaltuna (1995) Cloning, sequencing and expression of an isoform of cardiac C-protein from the Mexican axolotl (Ambystoma mexicanum) Biochem Biophys Res Commun 213:225–231PubMedGoogle Scholar
  97. Watkins, H., D. Conner, L. Thierfelder, J. A. Jarcho, C. MacRae, W. J. McKenna, B. J. Maron, J. G. Seidman, and C. E. Seidman (1995) Mutations in the cardiac myosin-binding protein-C on chromosome 11 cause familial hypertrophic cardiomyopathy. Nature Genet 11:434–437PubMedGoogle Scholar
  98. Weber, F. E., K. T. Vaughan, F. C. Reinach, and D. A. Fischman (1993) Complete sequence of human fast-type and slow-type muscle myosinbinding-protein C (MyBP-C) Differential expression, conserved domain structure and chromosome assignment. Eur J Biochem 216:661–669PubMedGoogle Scholar
  99. Weisberg, A., and S. Winegrad (1996) Alteration of myosin cross bridges by phosphorylation of myosin-binding protein C in cardiac muscle. Proc Natl Acad Sci USA 93:8999–9003PubMedGoogle Scholar
  100. Weisberg, A., and S. Winegrad (1998) Relation between crossbridge structure and actomyosin ATPase activity in rat heart. Circ Res 83:60–72PubMedGoogle Scholar
  101. Williams, A. F., and A. N. Barclay (1988) The immunoglobulin superfamily — domains for cell surface recognition. Ann Rev Immunol 6:381–405Google Scholar
  102. Wilson, F. J., and M. J. Irish (1980) The structure of segments of the anisotropic band of muscle. II. Preparation and properties of A segments from vertebrate skeletal muscle. Cell Tissue Res 212:213–223PubMedGoogle Scholar
  103. Yamamoto, K. (1984) Characterisation of H-protein, a component of skeletal muscle myofibrils. J Biol Chem 259:7163–7168PubMedGoogle Scholar
  104. Yamamoto, K., and C. Moos (1983) The C-proteins of rabbit red, white and cardiac muscles. J Biol Chem 258:8395–8401PubMedGoogle Scholar
  105. Yasuda, M., S. Koshida, N. Sato, and T. Obinata (1995) Complete primary structure of chicken cardiac C-protein (MyBP-C) and its expression in developing striated muscles. J Mol Cell Cardiol 27:2275–2286PubMedGoogle Scholar
  106. Young, O. A., and C. L. Davey (1981) Electrophoretic analysis of proteins from single bovine muscle fibres. Biochem J 195:315–327Google Scholar
  107. Yu, B., J. A. French, L. Carrier, R. W. Jeremy, D. R. McTaggart, M. R. Nicholson, B. Hambly, C. Semsarian, D. R. Richmond, K. Schwartz, and R. J. Trent (1998) Molecular pathology of familial hypertrophic cardiomyopathy caused by mutations in the cardiac myosin binding protein C gene. J Med Genet 35:205–210PubMedGoogle Scholar

Copyright information

© Springer-Verlag 1999

Authors and Affiliations

  • P. M. Bennett
    • 1
  • D. O. Fürst
    • 2
  • M. Gautel
    • 3
  1. 1.The Randall InstituteKing’s College LondonLondonUK
  2. 2.Department of Cell BiologyUniversity of PotsdamPotsdamGermany
  3. 3.European Molecular Biology LaboratoryHeidelbergGermany

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