Altered calpain levels in longissimus muscle from normal pigs and heterozygotes with the ryanodine receptor mutation

Journal of Animal Science

Volumn 77, Issue 11, 1999, Pages 2956-2964

  Sensky, P L ^a   Parr, T ^a   Lockley, A K ^a   Bardsley, R G ^a   Buttery, P J ^a   Wood, J D ^b   Warkup, C ^c  

^a UNIVERSITY OF NOTTINGHAM   (United Kingdom)

^b UNIVERSITY OF BRISTOL   (United Kingdom)

^c Meat and Livestock Commission   (United Kingdom)

Author keywords

Calpain; Calpastatin; Muscles; Pigs

Indexed keywords

ANIMALIA; SUIDAE; SUS SCROFA;

CALPAIN; RYANODINE RECEPTOR;

ANIMAL; ANIMAL DISEASE; ARTICLE; ENZYMOLOGY; GENETICS; GENOTYPE; HETEROZYGOTE; MEAT; METABOLISM; MOLECULAR WEIGHT; MUSCLE DISEASE; MUTATION; SKELETAL MUSCLE; STANDARD; SWINE;

ANIMALS; CALPAIN; GENOTYPE; HETEROZYGOTE; MEAT; MOLECULAR WEIGHT; MUSCLE, SKELETAL; MUSCULAR DISEASES; MUTATION; RYANODINE RECEPTOR CALCIUM RELEASE CHANNEL; SWINE;

EID: 0033227994     PISSN: 00218812     EISSN: None     Source Type: Journal    
DOI: 10.2527/1999.77112956x     Document Type: Article

References (47)

1. Aoki, K., S. Imajoh, S. Ohno, M. Emori, M. Koike, G. Kosaki, and K. Suzuki. 1986. Complete amino acid sequence of human calcium-activated neutral proteinase (μ CANP) deduced from its cDNA sequence. FEBS Lett. 205:313-317.
2. Arnold, M. K., T. Parr, P. L. Sensky, R. G. Bardsley, and P. J. Buttery. 1995. Differential calpastatin expression in cardiac and skeletal muscle. Biochem. Soc. Trans. 23:454S.
3. Bardsley, R. G., S.M.J. Allcock, J. M. Dawson, N. W. Dumelow, J. A. Higgins, Y. V. Lasslett, A. K. Lockley, T. Parr, and P. J. Buttery. 1992. Effect of β-agonists on expression of calpain and calpastatin activity in skeletal muscle. Biochimie 74:267-273.
4. Brandt, N. R., A. H. Caswell, T. Brandt, K. Brew, and R. L. Mellgren. 1992. Mapping of the calpain proteolysis products of the junctional foot protein of the skeletal muscle triad junctions. J. Membr. Biol. 127:35-47.
5. Brown, S. N., P. D. Warriss, G. R. Nute, J. E. Edwards, and T. G. Knowles. 1998. Meat quality in pigs subjected to minimal preslaughter stress. Meat Sci. 49:257-266.
6. Catterall, W. A. 1995. Structure and function of voltage-gated ion channels. Annu. Rev. Biochem. 64:493-531.
7. Chomczynski, P., and N. Sacchi. 1989. Single step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162:156-159.
8. Cong, M., V. F. Thompson, D. E. Goll, and P. B. Antin. 1998. The bovine calpastatin gene promoter and a new N-terminal region of the protein are targets for cAMP-dependent protein kinase. J. Biol. Chem. 273:660-666.
9. de Vries, A. G., P. G. van der Wal, T. Long, G. Eikelenboom, and J.W.M. Merks. 1994. Genetic-parameters of pork quality and production traits in Yorkshire populations. Livest. Prod. Sci. 40:277-289.
10. Doumit, M. E., S. M. Lonergan, J. R. Arbona, J. Killefer, and M. Koohmaraie. 1996. Development of an enzyme-linked immunosorbent assay (ELISA) for quantification of skeletal muscle calpastatin. J. Anim. Sci. 74:2679-2686.
11. Frangioni, J. V., and B. G. Neel. 1993. Solubilization and purification of active glutathione-S-transferase (pGEX) fusion proteins. Anal. Biochem. 210:179-187.
12. Fujii, J., K. Otsu, F. Zorzato, S. De Leon, V. K. Khanna, J. Weiler, P. J. O'Brien, and D. H. MacLennan. 1991. Identification of a mutation in porcine ryanodine receptor associated with malignant hyperthermia. Science (Wash DC) 253:448-451.
13. Geesink, G. H., D. Nonneman, and M. Koohmaraie. 1998. An improved purification protocol for heart and skeletal muscle calpastatin reveals two isoforms resulting from alternative splicing. Arch. Biochem. Biophys. 356:19-24.
14. Genstat. 1996. Genstat® for Windows (Version 5, Release 3.2, 2nd Ed.). Lawes Agricultural Trust, IACR-Rothamsted, U.K.
15. Goll, D. E., V. F. Thompson, R. G. Taylor, and T. Zalewska. 1992. Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? BioEssays 14:549-556.
16. Houde, A., and S. Pommier. 1993. Use of polymerase chain reaction technology to detect a mutation associated with malignant hyperthermia in different pig tissues. Meat Sci. 33:349-358.
17. Imajoh, S., K. Aoki, S. Ohno, Y. Emori, H. Kawasaki, H. Sugihara, and K. Suzuki. 1988. Molecular cloning of the cDNA for the large subunit of the high calcium-requiring form of the human calcium-activated neutral proteinase. Biochemistry 27:8122-8128.
18. Kawasaki, H., and S. Kawashima. 1996. Regulation of the calpain-calpastatin system by membranes (Review). Mol. Membr. Biol. 13:217-224.
19. Koohmaraie, M. 1994. Muscle proteinases and meat aging. Meat Sci. 36:93-104.
20. Koohmaraie, M. 1996. Biochemical factors regulating the toughening and tenderization processes of meat. Meat Sci. 43:S193-S201.
21. Koohmaraie, M., G. Whipple, D. H. Kretchmar, J. D. Crouse, and H. J. Mersmann. 1991. Postmortem proteolysis in longissimus muscle from beef, lamb and pork carcasses. J. Anim. Sci. 69:617-624.
22. Kretchmar, D. H., M. R. Hathaway, R. J. Epley, and W. R. Dayton. 1990. Alterations in postmortem degradation of myofibrillar proteins in muscle of lambs fed a β-adrenergic agonist. J. Anim. Sci. 68:1760-1772.
23. Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of the bacteriophage T4. Nature (Lond.) 227:680-685.
24. Lockley, A. K., J. S. Bruce, S. J. Franklin, and R. G. Bardsley. 1996. Use of mutagenically-separated PCR for the detection of the mutation associated with porcine stress syndrome. Meat Sci. 43:93-97.
25. Lundstrom, K., A. Karlsson, J. Hakansson, I. Hansson, M. Johansson, L. Andersson, and K. Andersson. 1995. Production, carcass and meat quality traits of F2-crosses between European Wild Pigs and domestic pigs including halothane gene carriers. Anim. Sci. 61:325-331.
26. MacDougall, D. B. 1986. The chemistry of colour and appearance. Food Chem. 21:273-299.
27. McPhee, C. P., and G. R. Trout. 1995. The effects of selection for lean growth and the halothane allele on carcass and meat quality of pigs transported long and short distances to slaughter. Livest. Prod. Sci. 42:55-62.
28. Mellgren, R. L., R. D. Lane, and M. T. Mericle. 1989. The binding of large calpastatin to biologic membranes is mediated in part by interaction of an amino terminal region with acidic phospholipids. Biochim. Biophys. Acta 999:71-77.
29. Mersmann, H. J. 1998. Overview of the effects of β-adrenergic receptor agonists on animal growth including mechanisms of action. J. Anim. Sci. 76:160-172.
30. Mickelson, J. R., J. M. Ervasti, L. A. Litterer, K. P. Campbell, and C. F. Lewis. 1994. Skeletal muscle junctional membrane protein content in pigs with different ryanodine receptor genotypes. Am. J. Physiol. 267:C282-C292.
31. Molinari, M., and E. Carafoli. 1997. Calpain: A cytosolic proteinase active at the membranes. J. Membr. Biol. 156:1-8.
32. Murray, A. C., S.D.M. Jones, and A. P. Sather. 1989. The effect of preslaughter feed restriction and genotype for stress susceptibility on pork lean quality and composition. Can. J. Anim. Sci. 69:83-91.
33. O'Brien, P. J. 1987. Etiopathogenetic defect of malignant hyperthermia: Hypersensitive calcium-release channel of skeletal muscle sarcoplasmic reticulum. Vet. Res. Commun. 11:527-559.
34. O'Brien, P. J., H. Shen, C. R. Cory, and X. Zhang. 1993. Use of a DNA-based test for the mutation associated with porcine stress syndrome (malignant hyperthermia) in 10,000 breeding swine. JAVMA 203:842-851.
35. Parr, T., R. G. Bardsley, R. S. Gilmour, and P. J. Buttery. 1992. Changes in calpain and calpastatin mRNA induced by β-adrenergic stimulation of bovine skeletal muscle. Eur. J. Biochem. 208:333-339.
36. Sambrook, J., E. F. Fritsch, and T. Maniatis. 1989. Molecular Cloning. A Laboratory Manual. (2nd Ed.). Cold Spring Harbor Laboratory Press, Cold Spring Harbor, NY.
37. Sensky, P. L., T. Parr, R. G. Bardsley, and P. J. Buttery. 1996a. The relationship between plasma epinephrine concentration and the activity of the calpain enzyme system in porcine longissimus muscle. J. Anim. Sci. 74:380-387.
38. Sensky, P. L., T. Parr, R. G. Bardsley, P. J. Buttery, S. N. Brown, and J. D. Wood. 1996b. Relationship between pigmeat toughness and the calpain proteolytic system. Anim. Sci. 62:663-664.
39. Shackelford, S. D., M. Koohmaraie, L. V. Cundiff, K. E. Gregory, G. A. Rohrer, and J. W. Savell. 1994. Heritabilities and phenotypic and genetic correlations for bovine postrigor calpastatin activity, intramuscular fat content, Warner-Bratzler shear force, retail product yield, and growth rate. J. Anim. Sci. 72:857-863.
40. Shevchenko, S., W. Feng, M. Varsanyi, and V. Shoshan-Barmatz. 1998. Identification, characterization and partial purification of a thiol protease which cleaves specifically the skeletal muscle ryanodine receptor/Ca2+ release channel. J. Membr. Biol. 161:33-43.
41. Sun, W., S. Q. Ji, P. J. Ebert, C. A. Bidwell, and D. L. Hancock. 1993. Cloning the partial cDNAs of μ-calpain and m-calpain from porcine skeletal muscle. Biochimie 75:931-936.
42. Takano, E., M. Maki, H. Mori, M. Hatanaka, T. Marti, K. Titani, R. Kannagi, T. Ooi, and T. Murachi. 1988. Pig heart calpastatin: Identification of repetititve domain structure and anomalous behaviour in polyacrylamide gel electrophoresis. Biochemistry 27:1964-1972.
43. Towbin, H., T. Steadhin, and J. Gordon. 1979. Electrophoretic transfer of protein from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc. Natl. Acad. Sci. USA 76:4350-4354.
44. Wang, S.-Y., and D. H. Beermann. 1988. Reduced calcium-dependent proteinase activity in cimaterol-induced muscle hypertrophy in lambs. J. Anim. Sci. 66:2545-2550.
45. Warner, R. D., R. G. Kauffman, and M. L. Greaser. 1997. Muscle protein changes post mortem in relation to pork quality traits. Meat Sci. 45:339-352.
46. 644,969 on muscle protein turnover, endogneous proteinase activities, and meat tenderness in steers. J. Anim. Sci. 70:3035-3043.
47. 2+ release channel. J. Biol. Chem. 272:25051-25061.