Pressure-induced changes in the connectin/titin localization in the myofibrils revealed by immunoelectron microscopy

Meat Science

Volumn 59, Issue 2, 2001, Pages 193-197

  Suzuki, A ^a   Homma, Y ^a   Kim, K ^a   Ikeuchi, Y ^a   Sugiyama, T ^a   Saito, M ^a  

^a NIIGATA UNIVERSITY   (Japan)

Author keywords

Connectin; High pressure treatment; Monoclonal antibody; Post mortem muscle; Titin

Indexed keywords

GALLUS GALLUS;

EID: 0035590393     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0309-1740(01)00070-5     Document Type: Article

References (29)

1. Fritz, J. D. & Greaser, M. L. (1991). Changes in titin and nebulin in postmortem bovine muscle revealed by gel electrophoresis, western blotting and immunofluorescence microscopy. Journal of Food Science, 56, 607-610, 615.
2. Fritz J.D., Mitchell M.C., Marsh B.B., Greaser M.L. Titin content of beef in relation to tenderness. Meat Science. 33:1993;41-50.
3. Fürst D.O., Osborn M., Nave R., Weber K. The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten repetitive epitopes starting at the Z line extends close to the M line. Journal of Cell Biology. 106:1988;1563-1572.
4. Higuchi H. Viscoelasticity and function of connectin/titin filaments in skinned muscle fibers. Advances in Biophysics. 33:1996;159-171.
5. Horowits R., Maruyama K., Podolsky R.J. Elastic behavior of connectin filaments during thick filament movement in activated skeletal muscle. Journal of Cell Biology. 109:1989;2169-2176.
6. Homma Y., Ikeuchi Y., Suzuki A. The difference between connectin and titin revealed by monoclonal antibody. Bulletin of Faculty of Agriculture, Niigata University. 44:1992;99-106. (in Japanese).
7. Kim K., Homma Y., Ikeuchi Y., Suzuki A. Effect of high hydrostatic pressure on the conversion of α-connectin to β-connectin. Journal of Biochemistry. 114:1993;463-467.
8. Kim K., Ikeuchi Y., Suzuki A. Pressure-induced conversion of α-connectin to β-connectin. Meat Science. 32:1992;237-243.
9. King N.L. Breakdown of connectin during cooking of meat. Meat Science. 11:1984;27-43.
10. King N.L., Kurth L., Shorthose W.R. Proteolytic degradation of connectin, a high molecular weight myofibrillar protein, during heating of meat. Meat Science. 5:1981;389-396.
11. Kitazawa T. Glycerinated muscle. Ebashi S., Maruyama K. Kinniku, Seikagaku Jikken Kouza. 1975;281-294 Tokyo Kagaku Dojin, Tokyo. (in Japanese).
12. Locker R.H. The role of gap filaments in muscle and meat. Food Microstructure. 3:1984;17-32.
13. Locker R.H., Leet N.G. Histology of highly stretched beef muscle. II Further evidence on the location and nature of gap filaments. Journal of Ultrastructure Research. 55:1976;157-172.
14. Lusby, M. L., Ridpath, J. F., Parrish, F. C. Jr., & Robson, R.M. (1983). Effect of postmortem storage on degradation of the myofibrillar protein titin in bovine longissimus muscle. Journal of Food Science, 48, 1787-1790, 1795.
15. Maruyama K. Connectin, an elastic filamentous protein of striated muscle. International Review of Cytology. 104:1986;81-114.
16. Maruyama K., Kimura S., Yoshidomi H., Sawada H., Kikuchi M. Molecular size and shape of β-connectin, an elastic protein of striated muscle. Journal of Biochemistry. 95:1984;1423-1433.
17. Maruyama K., Matsubara S., Natori R., Nonomura Y., Kimura S., Ohashi K., Murakami F., Handa S., Eguchi G. Connectin, an elastic protein of muscle, characterization and function. Journal of Biochemistry. 82:1977;317-337.
18. Maruyama K., Natori R., Nonomura Y. New elastic protein from muscle. Nature. 262:1976;58-60.
19. Maruyama K., Yoshida T., Higuchi H., Ohashi K., Kimura S., Natori R. Connectin filaments link thick filaments and Z-lines in frog skeletal muscle as revealed by immunoelectron microscopy. Journal of Cell Biology. 101:1985;2167-2172.
20. Ohtsuka S., Kimura S., Kawamura Y., Hirono Y., Maruyama K. Chicken leg muscle α-connectin as stained by a monoclonal antibody to the 1200 kDa fragment. Comparative Biochemistry and Physiology. 103B:1992;543-546.
21. Paterson B.C., Parish F.C. Jr. SDS-PAGE condition for detection of titin and nebulin in tender and tough bovine muscle. Journal of Food Science. 52:1987;509-510.
22. Ringkob T.P., Marsh B.B., Greaser M.L. Change in titin position in postmortem bovine muscle. Journal of Food Science. 53:1988;276-277.
23. Seki N., Watanabe T. Connectin content and its post-mortem changes in fish muscle. Journal of Biochemistry. 95:1984;1161-1167.
24. Suzuki A., Hoshino K., Sasaki E., Sano N., Nakane M., Ikeuchi Y., Saito M. Post-mortem changes of native connectin in rabbit skeletal muscle. Agricultural & Biological Chemistry. 52:1987;1439-1444.
25. Suzuki A., Kim K., Tanji H., Ikeuchi Y. Effects of high hydrostatic pressure on postmortem muscle. Recent Research Development in Agricultural & Biological Chemistry. 2:1998;30. 7-331.
26. Suzuki A., Sawaki T., Hosaka M., Ikarashi Y., Nonami Y. Post-mortem changes of connectin in chicken skeletal muscle. Meat Science. 15:1985;77-83.
27. Takahashi K., Saito H. Post-mortem changes in skeletal muscle connectin. Journal of Biochemistry. 85:1979;1539-1542.
28. Wang K. Sarcomere-associated cytoskeletal lattices in striated muscle, review and hypothesis. Shay J.W. Cell and Muscle Motility. 1985;305-369 Plenum Press, New York.
29. Wang K., McClure J., Tu A. Titin. a major myofibrillar component Proceedings of National Academy of Science USA. 76:1979;3698-3702.