Asian-Australasian Journal of Animal Sciences

  • 제22권2호
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  • Pages.282-288
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  • 2009
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  • 1011-2367(pISSN)
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  • 1976-5517(eISSN)
아세아태평양축산학회 (Asian Australasian Association of Animal Production Societies)
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Stability of Proteasomes Extracted from Pressurized, Aged Skeletal Muscles

  • Yamamoto, Shuhei (Food Science Center, Niigata University) ;
  • Suzuki, Atsushi (Department of Health and Nutrition, Faculty of Medical Science for Health, Teikyo Heisei University) ;
  • Nishiumi, Tadayuki (Department of Applied Biological Chemistry, Faculty of Agriculture, Niigata University)
  • 투고 : 2007.03.24
  • 심사 : 2008.09.08
  • 발행 : 2009.02.01
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초록

The present paper describes the effects of pressure and post-mortem aging treatments on in situ proteasome activity in rabbit and bovine skeletal muscles. Synthetic peptide hydrolyzing activity of rabbit proteasomes remained in the muscle after exposure to pressures up to 100 MPa. However, when a pressure of 400 MPa or more was applied, proteasomes were markedly inactivated. The extraction of proteasomes from excessively pressurized muscle appeared to be difficult. Proteasomes in aged muscle remained relatively stable throughout the aging process, with activity after 168 h (7 days) being 35%, 48%, 53% and 31% of the 0 h post-mortem LLVY, LSTR, AAF and LLE total hydrolyzing activities, respectively. The synthetic peptide hydrolyzing activities of bovine muscle proteasomes were similar to those of rabbit skeletal muscle proteasomes. The results suggest that synthetic peptide hydrolyzing activity remains in muscle exposed to relatively low pressures. Furthermore, it is known that high-pressure treatment induces fragmentation of myofibrils, modification of actin-myosin interaction and activation of intramuscular proteinases, cathepsins and calpains. Thus, proteasomes are probably involved in the tenderization process in combination with other intramuscular proteinases under high-pressure conditions. Our findings confirmed that proteasomes play a role in meat tenderization induced by high-pressure treatment or aging.

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참고문헌

  1. Bradford, M. M. 1976, A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding, Anal. Biochem. 72:248-254 https://doi.org/10.1016/0003-2697(76)90527-3
  2. Bouton, P. E., A. L. Ford, P. V. Harris, J. J. Macfarlane and J. M. O'Shea, 1977, Pressure-heat treatment of postrigor muscle,Effect on tenderness, J. Food Sci. 42:132-135 https://doi.org/10.1111/j.1365-2621.1977.tb01235.x
  3. Dahlmann, B., M. Rutschmann, L. Kuehn and H. Reinauer. 1985, Activation of the multicatalytic proteinase from rat skeletal muscle by fatty acid or sodium dodecyl sulphate, Biochem. J.228:171-177
  4. Farout, L., M. Lamare, C. Cardozo, M. Harrisson, M. Briand and Y. Briand. 2000, Distribution of proteasomes and of the five proteolytic activities in rat tissues, Arch. Biochem. Biophys.374:207-212 https://doi.org/10.1006/abbi.1999.1585
  5. Gardrat, F., B. Fraigneau, V. Montel, J. Raymond and J. L. Azanza. 1999, Effect of high hydrostatic pressure on 20S proteasome activity, Eur. J. Biochem 262:900-906 https://doi.org/10.1046/j.1432-1327.1999.00470.x
  6. Gerelt, B., S. Yamamoto, T. Sugiyama, T. Nishiumi and A. Suzuki. 2006, Changes in the immunogold electron-microscopic localization of calpain in bovine skeletal muscle induced by conditioning and high-pressure treatment, Biosci. Biotechnol. Biochem. 70:1249-1254 https://doi.org/10.1271/bbb.70.1249
  7. Homma, N., Y. Ikeuchi and A. Suzuki. 1994, Effect of high pressure treatment on the proteolytic enzymes in meat, Meat Sci. 38:219-228 https://doi.org/10.1016/0309-1740(94)90111-2
  8. Homma, N., Y. Ikeuchi and A. Suzuki. 1995, Levels of calpain and calpastatin in meat subjected to high pressure, Meat Sci.41:251-260 https://doi.org/10.1016/0309-1740(95)00005-6
  9. Kim, K., Y. Ikeuchi and A. Suzuki. 1992, Pressure-induced conversion of α-connectin to $\beta$-connectin, Meat Sci. 32:237-243 https://doi.org/10.1016/0309-1740(92)90110-P
  10. Koohmaraie, M. 1992, Ovine skeletal muscle multicatalytic proteinase complex (proteasome): purification, characterization and comparision of its effects on myofibrils with $\mu$-calpains, J. Anim. Sci. 70: 3697-3708
  11. Koomaraie, M., W. H. Kennick, E. A. Elgasim and A. F. Anglemier. 1984, Effect of prerigor pressurization on the activity of calcium-activated factor, J. Food Sci. 49:680-684 https://doi.org/10.1111/j.1365-2621.1984.tb13187.x
  12. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4, Nature 227:680-685 https://doi.org/10.1038/227680a0
  13. Lamare, M., R. G. Taylor, L. Farout, Y. Briand and M. Briand. 2002, Changes in proteasome activity during postmortem aging of bovine muscle. Meat Sci. 61:199-204 https://doi.org/10.1016/S0309-1740(01)00187-5
  14. Macfarlane, J. J. 1973, Pressure-induced solubilization of meat proteins in saline solution, J. Food Sci. 38:294-298 https://doi.org/10.1111/j.1365-2621.1973.tb01409.x
  15. Macfarlane, J. J. 1985, High pressure technology and meat quality. In: Development in Meat Science-3 (Ed. R. A. Lawrie), Elsevier Applied Science Publishers, London. pp. 155-184
  16. Matsuishi, M. and A. Okitani. 1997, Proteasome from rabbit skeletal muscle: Some properties and effect on muscle proteins, Meat Sci. 45:451-462 https://doi.org/10.1016/S0309-1740(96)00126-X
  17. Mellgren, R. L. 1990, Interaction of human erythrocyte multicatalytic proteinase with polycations, Biochem. Biophys. Acta. 995:181-186
  18. Mykles, D. L. 1989a, High-molecular-weight serine proteinase from lobster muscle that degrades myofibrillar proteins, J. Exp.Zool. 250:244-252 https://doi.org/10.1002/jez.1402500303
  19. Mykles, D. L. 1989b, Purification and characterization of multicatalytic proteinase from crustacean muscle: comparison of latent and heat-activated forms, Arch. Biochem, Biophys.274:216-228 https://doi.org/10.1016/0003-9861(89)90433-5
  20. Mykles, D. L. and M. F. Haire. 1995, Branch-chain-amino-acidpreferring peptidase activity of the lobster multicatalytic proteinase (proteasome) and the degradation of myofibrillar proteins, Biochem. J. 306:285-291
  21. Nishiwaki, T., Y. Ikeuchi and A. Suzuki. 1996, Effect of high pressure treatment on Mg-enhanced ATPase activity of rabbit myofibrils, Meat Sci. 43:145-155 https://doi.org/10.1016/0309-1740(96)84586-4
  22. Ohmori, T., T. Shigehisa, S. Taji and R. Hayashi. 1991, Effect of high pressure on the protease activities in meat, Agric. Biol. Chem. 55:357-361 https://doi.org/10.1271/bbb1961.55.357
  23. Orlowski, M. 1990, The multicatalytic proteinase complex, a major extralysosomal proteolytic system, Biochem. 29:10289-10297 https://doi.org/10.1021/bi00497a001
  24. Orlowski, M and S. Wilk. 1981, A multicatalytic proteinase complex from pituitary that forms enkephalin and enkephalin containing peptides, Biochem. Biophys. Res. Commun. 101:814-822 https://doi.org/10.1016/0006-291X(81)91823-4
  25. Otsuka, Y., N. Homma, K. Shiga, J. Ushiki, Y. Ikeuchi and A. Suzuki. 1998, Purification and properties of rabbit muscle proteasome, and its effect on myofibrillar structure, Meat Sci.49:365-378 https://doi.org/10.1016/S0309-1740(97)00141-1
  26. Rivett, A. J. 1989a, The multicatalytic proteinase of mammalian cells, Arch. Biochem. Biophys. 268:1-8 https://doi.org/10.1016/0003-9861(89)90558-4
  27. Rivett, A. J. 1989b, The multicatalytic proteinase, J. Biol. Chem. 264:12215-12219
  28. Rivett, A. J. 1993, Proteasome: multicatalytic proteinase complexes, Biochem. J. 291:1-10
  29. Rusman, H., B. Gerelt, S. Yamamoto, T. Nishiumi and A. Suzuki. 2007, Combined effects of high pressure and heat on shear value and histological characteristics of bovine skeletal muscle, Asian-Aust. J. Anim. Sci. 20:994-1001
  30. Suzuki, A., K. Kim, N. Homma, Y. Ileuchi and M. Saito. 1992, Accelaration of meat conditioning by high-pressure. In: High pressure and biotechnology (Ed. C. Balny, R. Hayashi, K. Heremens and P. Masson), Colloques INSERM/John Libbey Eurotext, Montrouge. pp. 219-227
  31. Suzuki, A., A. Okamoto, Y. Ikeuchi and M. Saito. 1993, Pressureinduced Ca2+ release from rabbit sarcoplasmic reticulum, Biosci. Biotechnol. Biochem. 57:862-863 https://doi.org/10.1271/bbb.57.862
  32. Suzuki, A., M. Watanabe, K. Iwamura, Y. Ikeuchi and M. Saito. 1990, Effect of high pressure treatment on the ultrastructure and myofibrillar protein of beef skeletal muscle, Agric. Biol. Chem. 54:3085-3091 https://doi.org/10.1016/S0308-8146(01)00395-8
  33. Tanaka, K., K. Ii, A. Ichihara, L. Waxman and A. L. Goldberg. 1986, A high molecular weight proteinase in the cytosol of ratliver, J. Biol. Chem. 261:15197-15203
  34. Towbin, H., T. Staehelin and J. Gordon. 1979, Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheet: Procedure and some applications, Proc. Natl. Acad. Sci. USA. 76:4350-4354 https://doi.org/10.1073/pnas.76.9.4350
  35. Thomas, A. R., H. Gondoza, L. C. Hoffman, V. Oosthuizen and R. J. Naud$\acute{e}$. 2004, The roles of the proteasome, and cathepsins B, L, H and D, in ostrich meat tenderization, Meat Sci. 67:113-120 https://doi.org/10.1016/j.meatsci.2003.10.001
  36. Trinick, J., P. Knight and A. Whiting. 1984, Purification and properties of native titin, J. Mol. Biol. 180:331-356 https://doi.org/10.1016/S0022-2836(84)80007-8
  37. Wilk, S. and M. Orlowski. 1983, Evidence that pituitary cationsensitive neutral endopeptidase is a multicatalytic proteinase complex,Journal of Neurochem. 40:842-849 https://doi.org/10.1111/j.1471-4159.1983.tb08056.x
  38. Yamamoto, S., B. Gerelt, T. Nishiumi and A. Suzuki, 2005a Purification and properties of bovine skeletal muscle proteasome, Asian-Aust. J. Anim. Sci. 18:884-891
  39. Yamamoto, S., Y. Otsuka, B. Gerelt, K. Masuda, Y. Ikeuchi, T. Nishiumi and A. Suzuki. 2005b, Effects of a high-pressure treatment on the activity and structure of rabbit muscle protesome, Biosci. Biotechnol. Biochem. 69:1239-1245 https://doi.org/10.1271/bbb.69.1239

피인용 문헌

  1. Effect of High Pressure on Physicochemical Properties of Meat vol.53, pp.7, 2013, https://doi.org/10.1080/10408398.2011.560296