Molecular diversity of myofibrillar proteins: Isoforms analysis at the protein and mRNA level

Methods in Cell Biology

Volumn , Issue 52, 1997, Pages 349-369

  Schiaffino, Stefano ^a   Salviati, Giovanni ^a  

^a UNIVERSITY OF PADOVA   (Italy)

Author keywords

[No Author keywords available]

Indexed keywords

MUSCLE PROTEIN;

ANIMAL; GENETIC VARIABILITY; GENETICS; HUMAN; METABOLISM; MUSCLE; MUSCLE FIBRIL; REVIEW;

ANIMALS; HUMANS; MUSCLE PROTEINS; MUSCLES; MYOFIBRILS; VARIATION (GENETICS);

EID: 0030630832     PISSN: 0091679X     EISSN: None     Source Type: Book Series    
DOI: 10.1016/s0091-679x(08)60387-8     Document Type: Article

References (61)

1. Andersen, J. L., and Schiaffino, S. (1997). Mismatch between myosin heavy chain mRNA and protein in human skeletal muscle fibers. Am. J. Physiol, in press.
2. Andersen, P. A. W., and Oakeley, A. E. (1989). Immunological identification of five troponin T isoforms reveals an elaborate maturational troponin T profile in rabbit myocardium. Circ. Res. 65, 1087-1093.
3. Bandman, E., Matsuda, R., and Strohman, R. C. (1982). Myosin heavy chains from two different adult fast-twitch muscles have different peptide maps but identical mRNAs. Cell 29, 645-650.
4. Bär, A., and Pette, D. (1988). Three fast myosin heavy chain in adult rat skeletal muscle. FEBS Lett. 235, 153-155.
5. Barany, M., Barany, K., Reckard, T., and Volpe, A. (1965). Myosin of fast and slow muscles of the rabbit. Arch. Biochem Biophys. 109, 185-191.
6. Barbato, R. Menabò, R., Dainese, P., Carafoli, E., Schiaffino, S., and Di Lisa, F. (1996). Binding of cytosolic proteins to myofibrils in ischemic rat hearts. Circ. Res. 78, 82-87.
7. Bottinelli, R., Schiaffino, S., and Reggiani, C. (1991). Force-velocity relation and myosin heavy chain isoform composition in skinned fibres of rat skeletal muscle. J. Physiol. (London) 437, 655-672.
8. Bottinelli, R., Betto, R., Schiaffino, S., and Reggiani, C. (1994). Unloaded shortening velocity and myosin heavy chain and alkali light chain isoform composition in rat skeletal muscle fibers. J. Physiol. (London) 478, 341-349.
9. Briggs, M. M., Klevit, R. E., and Schachat, F. H. (1984). Heterogeneity of contractile proteins. Purification and characterization of two species of troponin T from rabbit fast skeletal muscle. J. Biol. Chem. 259, 10369-10375.
10. Carraro, U., and Catani, C. (1983). A sensitive SDS-PAGE method separating myosin heavy chain isoforms of rat skeletal muscles reveals the heterogeneous nature of the embryonic myosin. Biochem. Biophys. Res. Commun. 116, 793-802.
11. d'Albis, A., and Gratzer, W. B. (1973). Electrophoretic examination of native myosin. FEBS Lett. 29, 292-296.
12. d'Albis, A., and Janmot, C. (1993). Separation by gel electrophoresis under nondissociating conditions (PPi PAGE) of the native isoforms of myosin - A technical note. Basic Appl. Myol. 3, 235-238.
13. Danieli-Betto, D., Zerbato, E., and Betto, R. (1986). Type 1, 2A and 2B myosin heavy chain electrophoretic analysis of rat muscle fibers. Biochem Biophys. Res. Commun. 138, 981-987.
14. DeNardi, C., Ausoni, S., Moretti, P., Gorza, L., Velleca, M., Buckingham, M., and Schiaffino, S. (1993). Type 2X myosin heavy chain is coded by a muscle fiber type-specific and developmentally regulated gene. J. Cell Biol. 123, 823-835.
15. Edman, K. A. P., te Kronnie, G., Reggiani, C., and Schiaffino, S. (1988). Maximum velocity of shortening related to myosin isoform composition in frog skeletal muscle fibres. J. Physiol. (London) 395, 679-694.
16. Feldman, A. M., Ray, P. E., Silan, C. M., Mercer, J. A., Minobe, W., and Bristow, M. R. (1991). Selective gene expression in failing human heart. Quantification of steady-state levels of messenger RNA in endomyocardial biopsies using the polymerase chain reaction. Circulation 83, 1866-1872.
17. Gorza, L., Ausoni, S., Merciai, N., Hastings, K. E. M., Shiaffino, S. (1993). Regional differences in troponin I isoform switching during rat heart development. Dev. Biol. 156, 253-264.
18. Granzier, H. L. M., and Wang, K. (1993). Gel electrophoresis of giant proteins. Solubilization and silver-staining of titin and nebulin from single muscle fiber segments. Electrophoresis 14, 56-64.
19. Härtner, K.-T., Kirschbaum, B. J., and Pette, D. (1989). The multiplicity of troponin T isoforms. Distribution in normal rabbit muscles and effects of chronic stimulation. Eur. J. Biochem. 179, 31-38.
20. Henzel, W. J., Billeci, T. M., Stultz, J. T., Wong, S. C., Grimley, C., and Watanabe, C. (1993). Identifying proteins from two-dimensional gels by molecular mass searching of peptide fragments in protein sequence databases. Proc. Natl. Acad. Sci. USA 90, 5011-5015.
21. Hoffman, E. P., Watkins, S. C., Slayter, H. S., and Kunkel, L. M. (1989). Detection of a specific isoform of alpha-actinin with antisera directed against dystrophin. J. Cell Biol. 108, 503-510.
22. Hoh, J. F. Y. (1975). Neural regulation of mammalian fast and slow muscle myosins: An electrophoretic analysis. Biochemistry 14, 742-747.
23. James, P., Quadroni, M., Carafoli, E., and Gonnet, G. (1993). Protein identification by mass profile fingerprinting. Biochem. Biophys. Res. Commun. 195, 58-64.
24. Kucera, J., and Walro, J. M. (1989). Nonuniform expression of myosin heavy chain isoforms along the length of cat intrafusal muscle fibers. Histochemistry 92, 291-299.
25. 4. Nature (London) 227, 680-685.
26. LaFramboise, W. A., Daood, M. J., Guthrie, R. D., Moretti, P., Schiaffino, S., and Ontell, M. (1990). Electrophoretic separation and immunological identification of type 2X myosin heavy chain in rat skeletal muscle. Biochem. Biophys. Acta 1035, 109-112.
27. Larsson, L., and Salviati, G. (1992). A technique for studies of the contractile apparatus in single human muscle fibre segments obtained by percutaneous biopsy. Acta Physiol. Scand. 146, 485-495.
28. Lompré, A. M., Nadal-Ginard, B., and Mahdavi, V. (1984). Expression of the cardiac ventricular α-and β-myosin heavy chain genes is developmentally and hormonally regulated. J. Biol. Chem. 259, 6437-6446.
29. Lowey, S., Waller, G. S., and Trybus, K. M. (1993). Function of skeletal muscle myosin heavy and light chains isoforms by an in vitro motility assay. J. Biol. Chem. 268, 20414-20418.
30. Merrill, C. R., Goldman, D., Sedman, S. A., and Ebert, M. H. (1981). Ultrasensitive stain for proteins in polyacrylamide gels shows regional variation in cerebrospinal fluid proteins. Science 211, 1437-1438.
31. Metzger, J. M., Parmacek, M. S., Barr, E., Pasyk, K., Lin, W. I., Cochrane, K. L., Field, L. J., and Leiden, J. M. (1993). Skeletal troponin C reduces contractile sensitivity to acidosis in cardiac myocytes from transgenic mice. Proc. Natl. Acad. Sci. USA 90, 9036-9040.
32. Moore, G. E., Briggs, M. M., and Schachat, F. H. (1987). Patterns of troponin expression in mammalian fast, slow and promiscuous fibres. J. Muscle Res. Cell Motil. 8, 13-22.
33. 2+ regulation of mechanical properties of striated muscle. Mechanistic studies using extraction and replacement of regulatory proteins. Circ. Res. 70, 865-884.
34. O'Farrell, P. H. (1975). High resolution two-dimensional electrophoresis of proteins. J. Biol. Chem. 250, 4007-4021.
35. O'Farrell, P. Z., Goodman, H. H., and O'Farrell, P. H. (1977). High resolution two-dimensional electrophoresis of basic as well as acidic proteins. Cell 12, 1133-1142.
36. Ordahl, C. P. (1986). The skeletal and cardiac α-actin genes are coexpressed in early embryonic striated muscle. Dev. Biol. 117, 488-492.
37. Otto, J. J. (1993). Immunoblotting. Meth. Cell Biol. 37, 105-117.
38. Pette, D., and Staron, R. S. (1990). Cellular and molecular diversities of mammalian skeletal muscle fibers. Rev. Physiol. Biochem. Pharmacol. 116, 1-76.
39. Pette, D., and Staron, R. S. (1987). Mammalian skeletal muscle fiber type transitions. Int. Rev. Cytol. 170, 143.
40. Rossini, K., Rizzi, C., Sandri, M., Bruson, A., and Carraro, U. (1995). High-resolution SDS-PAGE and immunochemical identification of the 2X and embryonic myosin heavy chains in complex mixtures of isomyosins. Electrophoresis, 16, 101-104.
41. Salviati, G., Betto, R., and Danieli-Betto, D. (1982). Polymorphism of myofibrillar proteins of rabbit skeletal-muscle fibres. An electrophoretic study of single fibres. Biochem. J. 207, 261-272.
42. Sambrook, J., Fritsch, E. F., and Maniatis, T. (1989). "Molecular Cloning: A Laboratory Manual," 2nd ed. Cold Spring Harbor, New York: Cold Spring Harbor Laboratory.
43. Sanders, C., Stewart, D. I. H., and Smillie, L. B. (1987). Troponin-T and glyceraldehyde-3-phosphate dehydrogenase share a common antigenic determinant. J. Muscle Res. Cell Motil. 8, 118-124.
44. Sassoon, D., and Rosenthal, N. (1993). Detection of messenger RNA by in situ hybridization. Meth. Enzymol. 225, 384-404.
45. Sassoon, D., Garner, I., and Buckingham, M. (1988). Transcripts of α-cardiac and α-skeletal actins are early markers for myogenesis in the mouse embryo. Development 104, 155-164.
46. Schachat, F. H., Diamond, M. S., and Brandt, P. W. (1987). Effect of different troponin T-tropomyosin combinations on thin filament activation. J. Mol. Biol. 198, 551-554.
47. Schiaffino, S., and Reggiani, C. (1996). Molecular diversity of myofibrillar proteins: Gene regulation and functional significance. Physiol. Rev. 76, 371-423.
48. Schiaffino, S., Saggin, L., Viel, A., Ausoni, S., Sartore, S., and Gorza, L. (1986). Muscle fiber types identified by monoclonal antibodies to myosin heavy chains. In "Biochemical Aspects of Physical Exercise" (G. Benzi, L. Packer, and N. Siliprandi, eds.), pp. 27-34. Amsterdam: Elsevier.
49. Schiaffino, S., Ausoni, S., Gorza, L., Saggin, L., Gundersen, K., and Lømo, T. (1988a). Myosin heavy chain isoforms and velocity of shortening of type 2 skeletal muscle fibres. Acta Physiol. Scand. 134, 565-566.
50. Schiaffino, S., Gorza, L., Pitton, G., Saggin, L., Ausoni, S., Sartore, S., and Lømo, T. (1988b). Embryonic and neonatal myosin heavy chain in denervated and paralyzed rat skeletal muscle. Dev. Biol. 127, 1-11.
51. Schiaffino, S., Gorza, L., Sartore, S., Saggin, L., Vianello, M., Gundersen, K., and Lømo, T. (1989). Three myosin heavy chain isoforms in type 2 skeletal muscle fibres. J. Muscle Res. Cell Motil. 10, 197-205.
52. Smerdu, V., Karsch-Mizrachi, I., Campione, M., Leinwand, L., Schiaffino, S. (1994). Type 2X myosin heavy chain transcripts are expressed in type 2B fibers of human skeletal muscle. Am. J. Physiol. 267, 1723-1728.
53. Staron, R. S., and Pette, D. (1987). Nonuniform myosin expression along single fibers of chronically stimulated and contralateral rabbit tibialis anterior muscles. Pflugers Arch. 409, 67-73.
54. Sigiura, T., and Murakami, N. (1990). Separation of myosin heavy chain isoforms in rat skeletal muscles by gradient sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Biomed. Res. 11, 87-91.
55. Takagi, M., Takano-Ohmuro, H., Nakamura, T., Kawahara, H., Shimizu, T., Obinata, T., and Kohama, K. (1989). Cross-reactivity of an antineurofilament antibody with a troponin-T isoform. Muscle Nerve 12, 827-832.
56. Talmadge, R. J., and Roy, R. R. (1993). Electrophoretic separation of rat skeletal muscle myosin heavy-chain isoforms. J. Appl. Physiol. 75, 2337-2340.
57. Termin, A., Staron, R. S. and Pette, D. (1989). Myosin heavy chain isoforms in histochemically defined fiber types of rat muscle. Histochemistry 92, 453-457.
58. Towbin, H., Staehelin, T., and Gordon, J. (1979). Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76, 4350-4354.
59. Wada, M., and Pette, D. (1993). Relationship between alkali light-chain complement and myosin heavy-chain isoforms in single fast-twitch fibers of rat and rabbit. Eur. J. Biochem. 214, 157-161.
60. Westfall, M. V., and Solaro, R. J. (1992). Alterations in myofibrillar function and protein profiles after complete global ischemia in rat hearts. Circ. Res. 70, 302-313.
61. Winegrad, S., Wisnewsky, C., and Schwartz, K. (1990). Effect of thyroid hormone on the accumulation of mRNA for skeletal and cardiac α-actin in hearts from normal and hypophysectomized rats. Proc. Natl. Acad. Sci. USA 87, 2456-2460.