Intermuscular variation in tenderness: Association with the ubiquitous and muscle-specific calpains

Journal of Animal Science

Volumn 79, Issue 1, 2001, Pages 122-132

  Ilian, M A ^a,c   Morton, J D ^a   Kent, M P ^a   Le Couteur, C E ^a   Hickford, J ^a   Cowley, R ^b   Bickerstaffe, R ^a  

^a LINCOLN UNIVERSITY   (New Zealand)

^b Canterbury Frozen Meat Company   (New Zealand)

^c NONE   (New Zealand)

Author keywords

Bovidae; Calpain; Calpastatin; Muscles; Sheep; Tenderness

Indexed keywords

CALCIUM BINDING PROTEIN; CALPAIN; CALPASTATIN; CYSTEINE PROTEINASE INHIBITOR; MESSENGER RNA; NUCLEASE S1;

ANIMAL; ARTICLE; CATTLE; ENZYMOLOGY; GENETICS; MALE; MEAT; METABOLISM; PH; SHEEP; SKELETAL MUSCLE; STANDARD;

ANIMALS; ASPERGILLUS NUCLEASE S1; CALCIUM-BINDING PROTEINS; CALPAIN; CATTLE; CYSTEINE PROTEINASE INHIBITORS; HYDROGEN-ION CONCENTRATION; MALE; MEAT; MUSCLE, SKELETAL; RNA, MESSENGER; SHEEP;

EID: 0035218640     PISSN: 00218812     EISSN: None     Source Type: Journal    
DOI: 10.2527/2001.791122x     Document Type: Article

References (46)

1. Ashmore, C. R. 1974. Phenotypic expression of muscle fiber types and some implications to meat quality. J. Anim. Sci. 38:1158-1164.
2. Ausubel, F. M., R. Brent, R. E. Kingston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl. 1987. Current Protocols in Molecular Biology. Wiley Interscience, New York.
3. Bickerstaffe, R. 1996. Proteases and meat quality. Proc. N. Z. Soc. Anim. Prod. 56:153-156.
4. Boehm, M. L., T. L. Kendall, V. F. Thompson, and D. E. Goll. 1998. Changes in the calpains and calpastatin during postmortem storage of bovine muscle. J. Anim. Sci. 76:2415-2434.
5. Briand, M., A. Talmant, Y. Briand, G. Monin, and R. Durand. 1981. Metabolic types of muscle in the sheep: I. Myosin ATPase, glycolytic, and mitochondrial enzyme activities. Eur. J. Appl. Physiol. 46:347-358.
6. 2+-dependent protease in rat skeletal muscle. J. Nutr. 113:145-158.
7. Chomczynski, P., and N. Sacchi. 1987. Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
8. Chrystall, B. B., and C. E. Devine. 1991. Quality assurance for tenderness. Publ. No. 872, Meat Industries Research Institute of New Zealand, Hamilton.
9. Cridge, A. G., R. Bickerstaffe, R. Cowley, and G. Savage. 1994. Postmortem factors influencing the quality of beef. Proc. Nutr. Soc. N. Z. 19:93-100.
10. 2+-activated protease possibly involved in myofibrillar protein turnover: Partial characterisation of the purified enzyme. Biochemistry 15:2159-2167.
11. Dayton, W. R., J. V. Schollmeyer, R. A. Lepley, and L. R. Cortes. 1981. A calcium-activated protease possibly involved in myofibrillar protein turnover: Isolation of a low-calcium-requiring form of the protease. Biochim. Biophys. Acta 659:48-61.
12. Doumit, M. E., and M. Koohmararie. 1999. Immunoblot analysis of calpastatin degradation: Evidence for cleavage by calpain in postmortem muscle. J. Anim. Sci. 77:1467-1473.
13. Forsberg, N. E., M. A. Ilian, A. Ali-Bar, P. R. Cheeke, and N. B. Wehr. 1989. Effects of cimaterol on rabbit growth and myofibrillar protein degradation and on calcium-dependent proteinase and calpastatin activities in skeletal muscle. J. Anim. Sci. 67:3313-3321.
14. Geesink, G. 1993. Postmortem muscle proteolysis and bovine tenderness with special reference to the action of the calpain/calpastatin system. dissertation. Utrecht Univ., The Netherlands.
15. Goll, D., M. Boehm, G. H. Geesink, and V. Thompson. 1997. What causes postmortem tenderisation. In: Proc. 50th Recip. Meat Conf., Ames, IA. pp 60-67.
16. Goll, D. E., R. G. Taylor, J. A. Christainsen, and V. F. Thompson. 1992. Role of proteinases and protein turnover in muscle growth and meat quality. In: Proc. 44th Recip. Meat Conf., Manhattan, KS. pp 25-36.
17. Hediger, R., H. A. Ansari, and G. F. Stranzinger. 1991. Chromosome banding and gene localization support extensive conservation of chromosome structure between cattle and sheep. Cytogenet. Cell Genet. 57:127-134.
18. Huff-Lonergan, E., T. Mitsuhashi, D. D. Beekman, F. C. Parrish, Jr., D. G. Olson, and R. M. Robson. 1996. Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. J. Anim. Sci. 74:993-1008.
19. Hunt, M. C., and H. B. Hedrick. 1977. Profile of fiber types and related properties of five bovine muscles. J. Food Sci. 42:513-517.
20. Ilian, M. A., and N. E. Forsberg. 1992. Gene expression of calpains and their specific endogenous inhibitor, calpastatin, in skeletal muscle of fed and fasted rabbits. Biochem. J. 287:163-171.
21. Ilian, M. A., R. S. Gilmour, and R. Bickerstaffe. 1999. Quantification of ovine and bovine calpain I, calpain II, and calpastatin mRNA levels by ribonuclease protection assay. J. Anim. Sci. 77:853-864.
22. Jones, S. W., T. Parr, P. L. Sensky, G. P. Scothern, R. G. Bardsley, and P. J. Buttery. 1999. Fibre type-specific expression of p94, a skeletal muscle-specific calpain. J. Muscle. Res. Cell Motil. 20:417-427.
23. Kenrick, M. K., L. Jiang, C. L. Potts, P. J. Owen, D. J. Shuey, J. G. Econome, J. G. Anson, and E. M. Quinet. 1997. A homogeneous method to quantify mRNA levels: A hybridisation of RNase protection and scintillation proximity assay technologies. Nucleic Acids Res. 25:2947-2948.
24. Klont, R. E., L. Brocks, and G. Eikelenboom. 1998. Muscle fibre type and meat quality. Meat Sci. 49:8219-8229.
25. 2+-dependent proteinase (calpains) in post-mortem proteolysis and meat tenderness. Biochimie (Paris) 74:239-245.
26. Koohmaraie, M. 1996. Biochemical factors regulating the toughening and tenderisation processes of meat. Meat Sci. 43:193-201.
27. Koohmaraie, M., S. C. Scideman, J. E. Schollmeyer, T. R. Dutson, and A. S. Babiker. 1988. Factors associated with the tenderness of three bovine muscles. J. Food Sci. 53:407-410.
28. Locker, R. H., and C. J. Hagyard. 1963. A cold shortening effect in beef muscles. J. Sci. Food Agric. 14:787-792.
29. Morton, J. D., R. Bickerstaffe, M. Kent, E. Dransfield, and G. R. Keely. 1999. Calpain-calpastatin and toughness in M. longissimus from electrically stimulated ovine and bovine carcasses. Meat Sci. 52:71-79.
30. Ouali, A. 1991. Sensory quality of meat as affected by muscle biochemistry and modern technologies. In: L. O. Fiems, B. G. Cottin, and D. I. Demeyer (ed.) Animal Biotechnology and the Quality of Meat Production. pp 85-103. Elsevier Science, Amsterdam.
31. Ouali, A., and A. Talmant. 1990. Calpains and calpastatin distribution in bovine, porcine and ovine skeletal muscles. Meat Sci. 28:331-348.
32. Parr, T., P. L. Sensky, G. P. Scothern, R. G. Bardsley, P. J. Buttery, J. D. Wood, and C. Warkup. 1999. Relationship between skeletal muscle-specific calpain and tenderness of conditioned porcine Longissimus muscle. J. Anim. Sci. 77:661-668.
33. Poussard, S., M. Duvert, D. Balcerzak, S. Ramassamy, J. Brustis, P. Cottin, and A. Ducastaing. 1996. Evidence for implication of muscle-specific calpain (calpain 3) in myofibrillar integrity. Cell Growth Differ. 7:1461-1469.
34. Puissant, C., and L. M. Houdebine. 1990. An improvement of the single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. BioTechniques 8:148-149.
35. Shackelford, S. D., T. L. Wheeler, and M. Koohmaraie. 1995. Relationship between shear force and trained sensory panel tenderness ratings of 10 major muscles from Bos indicus and Bos taurus cattle. J. Anim. Sci. 73:3333-3340.
36. Scideman, S. C., H. R. Cross, and J. D. Crouse. 1989. Variations in the sensory properties of beef as affected by sex condition, muscle and postmortem aging. J. Food Qual. 12:39-58.
37. Sorimachi, H., S. Imajoh-Ohmi, Y. Emori, H. Kawasaki, S. Ohno, Y. Minami, and K. Suzuki. 1989. Molecular cloning of a novel mammalian calcium-dependent protease distinct from both m- and μ-types. J. Biol. Chem. 264:20106-20111.
38. Sorimachi, H., S. Ishiura, and K. Suzuki. 1997. Structure and physiological function of calpains. Biochem. J. 328:721-732.
39. Sorimachi, H., K. Kinbara, S. Kimura, M. Takahashi, S. Ishiura, N. Sasagawa, N. Sorimachi, H. Shimada, K. Tagawa, K. Maruyama, and K. Suzuki. 1995. Muscle-specific calpain, p94, responsible for limb-girdle muscular dystrophy Type 2A, associates with connectin through IS2, a p94-specific sequence. J. Biol. Chem. 270:31158-31162.
40. Ueyama, H., T. Kumamoto, S. Fujimoto, T. Murakami, and T. Tsuda 1998. Expression of three calpain isoform genes in human skeletal muscle. J. Neurol. Sci. 155:163-169.
41. Van den Hemel-Grooten, H. N. A., M. F. W. te Pas, T. J. van den Bosch, G. J. Garssen, V. V. A. M. Schreurs, and M. W. A. Verstegen. 1997. mRNA levels of the calpain system in longissimus muscle of young pigs during prolonged feeding of a protein-free diet. J. Anim. Sci. 75:968-974.
42. 2+-dependent neural proteinases and their specific inhibitor during postmortem storage of rabbit skeletal muscle. J. Sci. Food Agric. 34:1241-1250.
43. Vorndam, A. V., and J. Kerschner. 1986. Purification of small oligonucleotides by polyacrylamide gel electrophoresis and transfer to diethylaminoethyl paper. Anal. Biochem. 152:221-225.
44. Wheeler, T. L., and M. Koohmaraie. 1999. The extent of proteolysis is independent of sarcomere length in lamb longissimus and psoas major. J. Anim. Sci. 77:2444-2451.
45. Wipple, G., and M. Khoohmaraie. 1991. Degradation of myofibrillar proteins by extractable lysosomal enzymes and m-calpain, and the effects of zinc chloride. J. Anim. Sci. 69:4449-4460.
46. Wipple, G., and M. Khoohmaraie. 1992. Effects of lamb age, muscle type, and 24-hour activity of endogenous proteinases on postmortem proteolysis. J. Anim. Sci. 70:798-804.