Skip to main content
SpringerLink
Log in

Postmortem Mechanisms of Meat Tenderization

The Roles of the Structural Proteins and the Calpain System

  • Chapter
Quality Attributes of Muscle Foods

Abstract

The conversion of muscle to meat is a complex process resulting in a set of conditions in postmortem muscle that are vastly different from those in living tissue. Efforts designed to understand the mechanism of postmortem meat tenderization must first define the postmortem biology of muscle tissue. Postmortem meat tenderization is associated with myofibrillar protein degradation. The protease µ-calpain and its endogenous inhibitor calpastatin are implicated as major causative agents/regulators of myofibrillar protein degradation. The interaction between g-calpain, calpastatin and myofibrillar protein substrates is complex, and, on a whole, poorly understood. Postmortem conditions of relatively low temperature, low pH and relatively high ionic strength create conditions which can alter protein conformation and protein interactions. Information regarding post-translational modification and environmentally induced conformational changes of both the calpain system and its substrate proteins can yield important information regarding postmortem meat tenderization

This is a preview of subscription content, log in via an institution to check access.

Access this chapter

Log in via an institution
Chapter
USD 29.95
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
eBook
USD 129.00
Price excludes VAT (USA)
  • Available as PDF
  • Read on any device
  • Instant download
  • Own it forever
Softcover Book
USD 169.99
Price excludes VAT (USA)
  • Compact, lightweight edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info
Hardcover Book
USD 169.99
Price excludes VAT (USA)
  • Durable hardcover edition
  • Dispatched in 3 to 5 business days
  • Free shipping worldwide - see info

Tax calculation will be finalised at checkout

Purchases are for personal use only

Institutional subscriptions

Preview

Unable to display preview. Download preview PDF.

Unable to display preview. Download preview PDF.

References

  • Adachi, Y.; lshida-Takahashi, A.; Takahashi, C.; Takano, E.; Murachi, T.; Hatanaka, M. Phosphorylation and sub-cellular distribution of calpastatin in human hematopoietic system cells. J. Biol. Chem 1991 266,3968–3972

    CAS  Google Scholar 

  • Balcerzak, D.; Poussard, S.; Brustis, J. J.; Elamrani, N.; Soriano, M.; Cottin, P.; Ducastaing, A. An antisense ohgodeoxyribonucleotide to m-calpain mRNA inhibits myoblast fusion. J. Cell Sei 1995 108,2077–2082

    CAS  Google Scholar 

  • Barnoy, S.; Glaser, T.; Kosower, N. S. Calpain and calpastatin in myoblast differentiation and fusion: effects of inhibitors. Biochim. Biophys. Acta 1997 1358,181–188

    CAS  Google Scholar 

  • Barnoy, S.; Glaser, T.; Kosower, N. S. The calpain-calpastatin system and protein degradation in fusing myoblasts. Biochim. Biophys. Acta 1998 1402,52–60

    CAS  Google Scholar 

  • Barnoy, S.; Glasner, T.; Kosower, N. S. The role of calpastatin (the specific calpain inhibitor) in myoblast differentiation and fusion. Biochem. Biophys. Res. Commun 1996 220,933–938

    CAS  Google Scholar 

  • Barrett, M. J.; Goll, D. E.; Thompson, V. F. Effect of substrate on Ca2(+)-concentration required for activity of the Ca2(+)-dependent proteinases, mu-and m-calpain. Life Sci 199148,1659–1669

    CAS  Google Scholar 

  • Belkin, A. M.; Zhidkova, N. L.; Koteliansky, V. E. Localization of talin in skeletal and cardiac muscles. FEBS Lett 1986 200,32–36

    CAS  Google Scholar 

  • Bergen, W. G.; Merkel, R. A. Protein Accretion. In Growth Regulation in Farm Animals; A. M. Pearson and T. R. Dutson, Eds.; Elsever Applied Science: New York, N.Y., 1991

    Google Scholar 

  • Boyer-Berri, C.; Greaser, M. L. Effect of postmortem storage on the Z-line region of titin in bovine muscle. J. Anim. Sci 199876,1034–1044

    CAS  Google Scholar 

  • Byers, T. J.; Kunkel, L. M.; Watkins, S. C. The subcellular distribution of dystrophin in mouse skeletal, cardiac, and smooth muscle. J. Cell Biol 1991 115,411–421

    CAS  Google Scholar 

  • Cockett, N. E.; Jackson, S. P.; Shay, T. L.; Nielsen, D.; Moore, S. S.; Steele, M. R.; Barendse, W.; Green, R. D.; Georges, M. Chromosomal localization of the callipyge gene in sheep (Ovis aries) using bovine DNA markers. Proc. Natl. Acad. Sci. USA 1994 91,3019–3023

    CAS  Google Scholar 

  • Cockett, N. E.; Jackson, S. P.; Snowder, G. D.; Carpenter, C. E. Characterization of the callipyge trait in sheep. Proc. Recip. Meat Conf 1996. 49 102–105

    Google Scholar 

  • Cong, J.; Goll, D. E.; Peterson, A. M.; Kapprell, H. P. The role of autolysis in activity of the Ca’-dependent proteinases (mu-calpain and m-calpain). J. Biol. Chem.1989 264, 10096–10103

    CAS  Google Scholar 

  • Cong, J.; Thompson, V. F.; Goll, D. E. Effect of monoclonal antibodies specific for the 28-kDa subunit on catalytic properties of the calpains. J. Biol. Chem 1993 268,25740–25747

    CAS  Google Scholar 

  • Cong, M.; Thompson, V. F.; Goll, D. E.; Antin, P. B. The bovine calpastatin gene promoter and a new N-terminal region of the protein are targets for cAMP-dependent protein kinase activity. J. Biol. Chem 1998 273, 660–666

    CAS  Google Scholar 

  • Cottin, P.; Brustis, J. J.; Poussard, S.; Elamrani, N.; Broncard, S.; Ducastaing, A. Ca(2+)-dependent proteinases (calpains) and muscle cell differentiation. Biochim. Biophys. Acta 1994 1223,170–178

    CAS  Google Scholar 

  • Cottin, P.; Vidalenc, P. L.; Ducastaing, A. Ca’+-dependent association between a Ca`’-activated neutral protease (CaANP) and its specific inhibitor. FEBSLett 1981 136,221–228

    CAS  Google Scholar 

  • Culler, R. D.; Parrish, F. C., Jr.; Smith, G. C.; Cross, H. R. Relationship of myofibril fragmentation index to certain chemical, physical and sensory characteristics of bovine longissimus dorsi muscle. J. Food Sci 1978, 43, 1177–1180

    CAS  Google Scholar 

  • Danowski, B. A.; Imanaka-Yoshida, K.; Sanger, J. M.; Sanger, J. W. Costameres are sites of force transmission to the substratum in adult rat cardiomyocytes. J. Cell Biol 1992 118,1411–1420

    CAS  Google Scholar 

  • Davey, C. L.; Gilbert, K. V. Studies in meat tenderness. 7. Changes in the fine structure of meat during aging. J. Food Sci 1969 34,69–74

    Google Scholar 

  • Davies, P. J. A.; Wallach, D.; Willingham, M. C.; Pastan, I.; Ymaguchi, M., Robson, R.M. Filamin-actin interaction. Dissociation of binding from gelation by Ca“-activated proteolysis. J. Biol. Chem 1978 253,4036–4042

    CAS  Google Scholar 

  • Dayton, W. R.; Goll, D. E.; Stromer, M. H.; Robson, R. M.; Reville, W. J. Some properties of a Cat -activated protease that may be involved in myofibrillar protein turnover. In Proteases and Biological Control; E. Reich; D. B. Rifkin and E. Shaw, Eds.; Cold Spring Harbor Laboratory: Cold Spring Harbor, N.Y., 1975; p 551

    Google Scholar 

  • DeMartino, G. N.; Wachendorfer, R.; McGuire, M. J.; Croall, D. E. Proteolysis of the protein inhibitor of calcium-dependent proteases produces lower molecular weight fragments that retain inhibitory activity. Arch. Biochem. Biophys 1988 262,189–198

    CAS  Google Scholar 

  • Di Lisa, F.; De Tullio, R.; Salamino, F.; Barbato, R.; Melloni, E.; Siliprandi, N.; Schiaffino, S.; Pontremoli, S. Specific degradation of troponin T and I by mu-calpain and its modulation by substrate phosphorylation. Biochem. J 1995 308,57–61

    Google Scholar 

  • Edmunds, T.; Nagainis, P. A.; Sathe, S. K.; Thompson, V. F.; Goll, D. E. Comparison of the autolyzed and unautolyzed forms of mu-and m-calpain from bovine skeletal muscle. Biochim. Biophys. Acta 1991 1077,197–208

    CAS  Google Scholar 

  • Emori, Y.; Kawasaki, H.; Imajoh, S.; Imahori, K.; Suzuki, K. Endogenous inhibitor for calcium-dependent cysteine protease contains four internal repeats that could be responsible for its multiple reactive sites. Proc. Natl. Acad. Sci. USA 1987 84,3590–3594

    CAS  Google Scholar 

  • Emori, Y.; Kawasaki, H.; Imajoh, S.; Minami, Y.; Suzuki, K. All four repeating domains of the endogenous inhibitor for calcium-dependent protease independently retain inhibitory activity. Expression of the cDNA fragments in Escherichia coli. J. Biol. Chem 1988 263,2364–2370

    CAS  Google Scholar 

  • Fritz, J. D.; Greaser, M. L. Changes in thin and nebulin in postmortem bovine muscle revealed by gel electrophoresis, western blotting, and immunofluorescence microscopy. J. Food Sci 199156,607–610

    CAS  Google Scholar 

  • Furst, 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 nonrepetitive epitopes starting at the Z line extends close to the M line. J.Cell Biol 1988 106,1563–1572

    CAS  Google Scholar 

  • Goll, D. E.; Kleese, W. C.; Szpacenko, A. Skeletal muscle proteases and protein turnover. In Animal Growth Regulation; D. R. Campion; G. J. Hausman and R. J. Martin, Eds.; Plenum Publishing Corp.: New York, N.Y., 1989

    Google Scholar 

  • Goll, D. E.; Thompson, V. F.; Taylor, R. G.; Christiansen, J. A. Role of the calpain system in muscle growth. Biochimie 1992a 74,225–237

    CAS  Google Scholar 

  • Goll, D. E.; Thompson, V. F.; Taylor, R. G.; Zalewska, T. Is calpain activity regulated by membranes and autolysis or by calcium and calpastatin? Bioessays 1992b 14,549–556

    CAS  Google Scholar 

  • Gorlin, J. B.; Yamin, R.; Egan, S.; Stewart, M.; Stossel, T. P.; Kwiatkowski, D. J.; Hartwig, J. H. Human endothelial actin-binding protein (ABP-280, nonmuscle filamin): a molecular leaf spring. J. Cell Biol 1990 111,1089–1105

    CAS  Google Scholar 

  • Granzier, H. L.; Wang, K. Passive tension and stiffness of vertebrate skeletal and insect flight muscles: the contribution of weak cross-bridges and elastic filaments. Biophys. J 199365,2141–2159

    CAS  Google Scholar 

  • Guttmann, R. R; Elce, J. S.; Bell, R. D.; Isbell, J. C.; Johnson, G. V. Oxidation inhibits substrate proteolysis by cal-pain I but not autolysis. J Biol. Chem.1997 272,2005–2012

    CAS  Google Scholar 

  • Ho, C. Y.; Stromer, M. H.; Robson, R. M. Effect of electrical stimulation on postmortem titin, nebulin, desmin, and troponin-T degradation and ultrastructural changes in bovine longissimus muscle. J. Anim. Sci 1996 74,1563–1575

    CAS  Google Scholar 

  • Ho, C. Y.; Stromer, M. H.; Robson, R. M. Identification of the 30 kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T. Biochimie 1994 76,369–375

    CAS  Google Scholar 

  • Ho, C. Y.; Stromer, M. H.; Rouse, G.; Robson, R. M. Effects of electrical stimulation and postmortem storage on changes in titin, nebulin, desmin, troponin-T, and muscle ultrastructure in Bos indicus crossbred cattle. J. Anim. Sci 1997 75,366–376

    CAS  Google Scholar 

  • Huff-Lonergan, E.; Lonergan, S. M.; Kriese, L. A.; Wiegand, B. R. Postmortem degradation and calpastatin activity in top loin steaks from Brangus cattle. J. Anim. Sci 1997, (Suppl. 1)75–76

    Google Scholar 

  • Huff-Lonergan, E.; Mitsuhashi, T.; Beekman, D. D.; Parrish, F. C., Jr.; Olson, D. G.; Robson, R. M. Proteolysis of specific muscle structural proteins by mu-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. J. Anim. Sci 1996, 74, 993–1008

    CAS  Google Scholar 

  • Huff-Lonergan, E.; Parrish, F. C., Jr.; Robson, R. M. Effects of postmortem aging time, animal age, and sex on degradation of titin and nebulin in bovine longissimus muscle. J. Anim. Sci 1995 73,1064–1073

    CAS  Google Scholar 

  • Hwan, S. F.; Sandman, E. Studies of desmin and a-actinin degradation in bovine semitendinosis muscle. J. Food Sci 1989 54,1426–1430

    CAS  Google Scholar 

  • Imajoh, S.; Kawasaki, H.; Suzuki, K. The amino-terminal hydrophobic region of the small subunit of calcium-activated neutral protease (CANP) is essential for its activation by phosphatidylinositol. J. Biochem. (Tokyo) 1986 99,1281–1284

    CAS  Google Scholar 

  • Inomata, M.; Saito, Y.; Kon, K.; Kawashima, S. Binding sites for calcium-activated neutral protease on erythrocyte membranes are not membrane phospholipids. Biochem. Biophys. Res. Commun 1990 171,625–632

    CAS  Google Scholar 

  • Ip, W.; Heuser, J. E.; Pang, Y. Y.; Hartzer, M. K.; Robson, R. M. Subunit structure of desmin and vimentin protofilaments and how they assemble into intermediate filaments. Ann. N. Y. Acad. Sci 1985 455,185–199

    CAS  Google Scholar 

  • lshima, R.; Tamura, A.; Akasaka, K.; Hamaguchi, K.; Makino, K.; Murachi, T.; Hatanaka, M.; Maki, M. Structure of the active 27-residue fragment of human calpastatin. FEBS Lettt 1991 294,64–66

    Google Scholar 

  • Itoh, Y.; Suzuki, T.; Kimura, S.; Ohashi, K.; Higuchi, H.; Sawada, H.; Shimizu, T.; Shibata, M.; Maruyama, K. Extensible and less-extensible domains of connectin filaments in stretched vertebrate skeletal muscle sarcomeres as detected by immunofluorescence and immunoelectron microscopy using monoclonal antibodies. J. Biochem. (Tokyo) 1988 104, 504–508

    CAS  Google Scholar 

  • Jin, J. R; Wang, K. Cloning, expression, and protein interaction of human nebulin fragments composed of varying numbers of sequence modules. J. Biol. Chem 1991 266,21215–21223

    CAS  Google Scholar 

  • Kapprell, H. R; Goll, D. E. Effect of Ca2+ on binding of the calpains to calpastatin. J. Biol. Chem 1989 264, 17888–17896

    CAS  Google Scholar 

  • Kawasaki, H.; Emori, Y.; lmajoh-Ohmi, S.; Minami, Y.; Suzuki, K. Identification and characterization of inhibitory sequences in four repeating domains of the endogenous inhibitor for calcium-dependent protease. J. Biochem. (Tokyo) 1989 106, 274–281

    CAS  Google Scholar 

  • Kawasaki, H.; Emori, Y.; Suzuki, K. Calpastatin has two distinct sites for interaction with calpain--effect of calpastatin fragments on the binding of calpain to membranes. Arch. Biochem. Biophys 1993 305,467–472

    CAS  Google Scholar 

  • Killefer, J.; Koohmaraie, M. Bovine skeletal muscle calpastatin: cloning, sequence analysis, and steady-state mRNA expression. J. Anim. Sci 1994 72, 606–614

    CAS  Google Scholar 

  • Kimura, S.; Matsuura, T.; Ohtsuka, S.; Nakauchi, Y.; Matsuno, A.; Maruyama, K. Characterization and localization of alpha-connectin (titin 1): an elastic protein isolated from rabbit skeletal muscle. J. Muscle Res. Cell Motil 1992 13, 39–47

    CAS  Google Scholar 

  • Koohmaraie, M. Muscle proteinases and meat aging. Meat Sci 1994 36, 93–103

    CAS  Google Scholar 

  • Koohmaraie, M. Role of neutral proteinases in postmortem muscle degradation and meat tenderness. Proc. Recip. Meat Conf 1992 45, 63–74

    Google Scholar 

  • Koohmaraie, M. The role of endogenous proteases and meat tenderness. Proc. Recip. Meat Conf 1988 41,89–100

    Google Scholar 

  • Koohmaraie, M.; Kennick, W. H.; Anglemier, A. F.; Elgasim, E. A.; Jones, T. K. Effect of postmortem stroage on cold-shortened bovine muscle: Analysis by SDS-polyacrylamide gel electrophoresis. J. Food Sci 1984a 49, 290–291

    CAS  Google Scholar 

  • Koohmaraie, M.; Kennick, W. H.; Elgasim, E. A.; Anglemier, A. F. Effect of postmortem storage on muscle protein degradation: Analysis by SDS-polyacrylamide gel electrophoresis. J. Food Sci 1984b 49,292–293

    CAS  Google Scholar 

  • Koohmaraie, M.; Killefer, J.; Bishop, B. D.;hackelford, S. D.; Wheeler, T. L.; Arbona, J. R. Calpastatin-based methods for predicting meat tenderness. In Expression, regulation and role of proteinases in muscle development and meat quality; A. Ouali; D. Demeyer and F. Smulders, Eds.; ECCEAMST (European Consortium for Continuing Education in Advanced Meat Science): Utrecht, The Netherlands, 1995a; pp 39–412

    Google Scholar 

  • Koohmaraie, M.; Shackelford, S. D.; Muggli-Cockett, N. E.; Stone, R. T. Effect of the beta-adrenergic agonist L644,969 on muscle growth, endogenous proteinase activities, and postmortem proteolysis in wether lambs. J. Anim. Sci 1991 69, 4823–4835

    CAS  Google Scholar 

  • Koohmaraie, M.; Shackelford, S. D.; Wheeler, T. L.; Lonergan, S. M.; Doumit, M. E. A muscle hypertrophy condition in lamb (callipyge): characterization of effects on muscle growth and meat quality traits. J. Anim. Sci 1995b,73,596–3607

    CAS  Google Scholar 

  • Kumamoto, T.; Kleese, W. C.; Cong, J. Y.; Goll, D. E.; Pierce, P. R.; Allen, R. E. Localization of the Ca(2+)-dependent proteinases and their inhibitor in normal, fasted, and denervated rat skeletal muscle. Anat. Rec 1992 32,60–77

    CAS  Google Scholar 

  • Kwak, K. B.; Chung, S. S.; Kim, O. M.; Kang, M. S.; Ha, D. B.; Chung, C. H. Increase in the level of m-calpain correlates with the elevated cleavage offilamin during myogenic differentiation of embryonic muscle cells. Biochim. Biophys. Acta 1993 175,243–249

    CAS  Google Scholar 

  • Labeit, S.; Gautel, M.; Lakey, A.; Trinick, J. Towards a molecular understanding of titin. Embo. J 1992 1,1711–1716

    CAS  Google Scholar 

  • Labeit, S.; Gibson, T.; Lakey, A.; Leonard, K.; Zeviani, M.; Knight, P.; Wardale, J.; Trinick, J. Evidence that nebulin is a protein-ruler in muscle thin filaments [published erratum appears in FEBS Lett. 1991 Dec 16;295(1–3):232]. FEBS Lett 1991 282, 313–316

    CAS  Google Scholar 

  • Labeit, S.; Kolmerer, B.; Linke, W. A. The giant protein titin. Emerging roles in physiology and pathophysiology Circ. Res 1997 80, 290–294

    CAS  Google Scholar 

  • Linke, W. A.; Popov, V. I.; Pollack, G. H. Passive and active tension in single cardiac myofibrils. Biophys. J 1994 67, 782–792

    CAS  Google Scholar 

  • Lonergan, S. M.; Huff-Lonergan, E.; Payne, D. M. Purification and partial characterization of a high molecular weight bovine skeletal muscle calpastatin. FASEB J 1997 11, A58

    Google Scholar 

  • Lonergan, S. M.; Huff-Lonergan, E.; Wiegand, B. R.; Kriese, L. A. The relationship of calpastatin activity to Warner-Bratzler shear force duging aging of top loin steaks from Brangus cattle. J. Anim. Sci 1997, (Suppl. 1)75, 12

    Google Scholar 

  • Lusby, M. L.; Ridpath, J. F.; Parrish, F. C., Jr.; Robson, R. M. Effect of postmortem storage on degradation of the recently discovered myofibrillar protein titin in bovine longissimus muscle. J. Food Sci 1983 48, 1789–1790,1795

    Google Scholar 

  • Ma, H.; Yang, H. Q.; Takano, E.; Lee, W. J.; Hatanaka, M.; Maki, M. Requirement of different subdomains of calpastatin for calpain inhibition and for binding to calmodulin-like domains. J. Biochem. (Tokyo) 1993 113, 591–599

    CAS  Google Scholar 

  • Maki, M.; Bagci, H.; Hamaguchi, K.; Ueda, M.; Murachi, T.; Hatanaka, M. Inhibition of calpain by a synthetic oli-gopeptide corresponding to an exon of the human calpastatin gene. J. Biol. Chem 1989 264,18866–18869

    CAS  Google Scholar 

  • Maki, M.; Hatanaka, H.; Takano, E.; Murachi, T. Structure-function relationship of calpastatins. In Intracellular calcium-dependent proteolysis; R. L. Mellgren and T. Murachi, Eds.; CRC Press: Boca Raton, Florida, 1990; pp 37–54

    Google Scholar 

  • Maki, M.; Ma, H.; Takano, E.; Adachi, Y.; Lee, W. J.; Hatanaka, M.; Murachi, T. Calpastatins: biochemical and molecular biological studies. Biomed. Biochim. Acta 1991 50, 509–516

    CAS  Google Scholar 

  • Maki, M.; Takano, E.; Mori, H.; Kannagi, R.; Murachi, T.; Hatanaka, M. Repetitive region of calpastatin is a functional unit of the proteinase inhibitor. Biochem. Biophys. Res. Commun 1987a 143,300–308

    CAS  Google Scholar 

  • Maki, M.; Takano, E.; Mori, H.; Sato, A.; Murachi, T.; Hatanaka, M. All four internally repetitive domains of pig calpastatin possess inhibitory activities against calpains I and II FEBSLett 1987b 223, 174–180

    CAS  Google Scholar 

  • Maki, M.; Takano, E.; Osawa, T.; Ooi, T.; Murachi, T.; Hatanaka, M. Analysis of structure-function relationship of pig calpastatin by expression of mutated cDNAs in Escherichia coli. J. Biol. Chem 1988 263,10254–61

    CAS  Google Scholar 

  • Maruyama, K. Connectin, an elastic protein of striated muscle. Biophys. Chem 1994 50,73–85

    CAS  Google Scholar 

  • Matsuura, T.; Kimura, S.; Ohtsuka, S.; Maruyama, K. Isolation and characterization of 1,200 kDa peptide of al pha-connectin. J. Biochem. (Tokyo) 1991 110, 474–478

    CAS  Google Scholar 

  • Mellgren, R. L. Calcium-dependent proteases: an enzyme system active at cellular membranes? FASEB J 1987 1, 110–115

    CAS  Google Scholar 

  • Mellgren, R. L.; Carr, T. C. The protein inhibitor of calcium-dependent proteases: purification from bovine heart and possible mechanisms of regulation. Arch. Biochem. Biophys 1983 225,779–786

    CAS  Google Scholar 

  • Mellgren, R. L.; Mericle, M. T.; Lane, R. D. Proteolysis of the calcium-dependent protease inhibitor by myocardial calcium-dependent protease. Arch. Biochem. Biophys 1986 246, 233–239

    CAS  Google Scholar 

  • Mellgren, R. L.; Nettey, M. S.; Mericle, M. T.; Renno, W.; Lane, R. D. An improved purification procedure for calpastatin, the inhibitor protein specific for the intracellular calcium-dependent proteinases, calpains. Prep. Biochem 1988 18, 183–197

    CAS  Google Scholar 

  • Melloni, E.; Sparatore, B.; Salamino, F.; Michetti, M.; Pontremoli, S. Cytosolic calcium dependent neutral proteinase of human erythrocytes: the role of calcium ions on the molecular and catalytic properties of the enzyme. Biochem. Biophys. Res. Commun 1982 107, 1053–1059

    CAS  Google Scholar 

  • Michetti, M.; Salamino, F.; Melloni, E.; Pontremoli, S. Reversible inactivation of calpain isoforms by nitric oxide. Biochem. Biophys. Res. Commun 1995 207, 1009–10014

    CAS  Google Scholar 

  • Murachi, T. Intracellular regulatory system involving calpain and calpastatin. Biochem. Int 1989 18, 263–294

    CAS  Google Scholar 

  • Nakamura, M.; Inomata, M.; Imajoh, S.; Suzuki, K.; Kawashima, S. Fragmentation of an endogenous inhibitor upon complex formation with high-and low-Ca2+-requiring forms of calcium-activated neutral proteases. Biochemistry 1989 28, 449–455

    CAS  Google Scholar 

  • Nave, R.; Furst, D. O.; Weber, K. Visualization of the polarity of isolated titin molecules: a single globular head on a long thin rod as the M band anchoring domain? J. Cell Biol 1989 109,2177–2187

    CAS  Google Scholar 

  • Nishimura, T.; Goll, D. E. Binding of calpain fragments to calpastatin. J. Biol. Chem 1991 266,11842–11850

    CAS  Google Scholar 

  • O’Shea, J. M.; Robson, R. M.; Huiatt, T. W.; Hartzer, M. K.; Stromer, M. H. Purified desmin from adult mammalian skeletal muscle: a peptide mapping comparison with desmins from adult mammalian and avian smooth muscle. Biochem. Biophys. Res. Commun 1979 89, 972–980

    Google Scholar 

  • Otsuka, Y.; Goll, D. E. Purification of the Ca2+-dependent proteinase inhibitor from bovine cardiac muscle and its interaction with the millimolar Ca2+-dependent proteinase. J. Biol. Chem 1987 262, 5839–5851

    CAS  Google Scholar 

  • Pardo, J. V.; Siliciano, J. D.; Craig, S. W. A vinculin-containing cortical lattice in skeletal muscle: transverse lattice elements (“costameres”) mark sites of attachment between myofibrils and sarcolemma. Proc. Natl. Acad. Sci. USA 1983 80, 1008–1012

    CAS  Google Scholar 

  • Pearlstone, J. R.; Smillie, L. B. Binding of troponin-T fragments to several types of tropomyosin. Sensitivity to Ca2+ in the presence of troponin-C. J. Biol. Chem 1982 257,10587–10592

    CAS  Google Scholar 

  • Penny, I. F.; Dransfield, E. Relationship between toughness and troponin-T in conditioned beef. Meat Sci 1979 3, 135–141

    CAS  Google Scholar 

  • Pontremoli, S.; Melloni, E.; Sparatore, B.; Salamino, F.; Michetti, M.; Sacco, O.; Horecker, B. L. Role of phospholipids in the activation of the Ca2’-dependent neutral proteinase of human erythrocytes. Biochem. Biophys. Res. Commun 1985 129, 389–395

    CAS  Google Scholar 

  • Pontremoli, S.; Melloni, E.; Viotti, P. L.; Michetti, M.; Salamino, F.; Horecker, B. L. Identification of two calpastatin forms in rat skeletal muscle and their susceptibility to digestion by homologous calpains. Arch. Biochem. Biophys 1991 288, 646–652

    CAS  Google Scholar 

  • Pontremoli, S.; Viotti, P. L.; Michetti, M.; Salamino, F.; Sparatore, B.; Melloni, E. Modulation of inhibitory efficiency of rat skeletal muscle calpastatin by phosphorylation. Biochem. Biophys. Res. Commun 1992 187 751–759

    CAS  Google Scholar 

  • Porter, G. A.; Dmytrenko, G. M.; Winkelmann, J. C.; Bloch, R. J. Dystrophin colocalizes with beta-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle. J. Cell Biol 1992 117,997–1005

    CAS  Google Scholar 

  • Price, M. G.; Caprette, D. R.; Gomer, R. H. Different temporal patterns of expression result in the same type, amount, and distribution of filamin (ABP) in cardiac and skeletal myofibrils. Cell Motil. Cytoskeleton 1994 27 248–261

    CAS  Google Scholar 

  • Pringle, T. D.; Calkins, C. R.; Koohmaraie, M.; Jones, S. J. Effects over time of feeding a beta-adrenergic agonist to wether lambs on animal performance, muscle growth, endogenous muscle proteinase activities, and meat tenderness. J. Anim. Sci 1993 71, 636–644

    CAS  Google Scholar 

  • Richardson, F. L.; Stromer, M. H.; Huiatt, T. W.; Robson, R. M. Immunoelectron and immunofluorescence localization of desmin in mature avian muscles. Eur. J. Cell Biol 1981 26, 91–101

    CAS  Google Scholar 

  • Robson, R. M. Intermediate filaments. Curr. Opinion Cell Biol 1989 1,36–43

    CAS  Google Scholar 

  • Robson, R. M. Myofibrillar and cytoskeletal structures and proteins in mature skeletal muscle cells. In Expression of tissue proteinases and regulation of protein degradation as related to meat quality; D. I. Demeyer, Smulders, F.J.M., Ed.; ECCEAMST (European Consortium for Continuing Education in Advanced Meat Science): Utrecht, The Netherlands, 1995; pp 267–288

    Google Scholar 

  • Robson, R. M.; Huff-Lonergan, E.; Parrich, F. C., Jr.; Ho, C.-Y.; Stromer, M. H.; Huiatt, T. W.; Bellin, R. M.; Semett, S. W. Proc. Recip. Meat Conf; American Meat Science Association 1997; 50 43–52

    Google Scholar 

  • Robson, R. M.; Huiatt, T. W.; Parrish, F. C., Jr. Proc. Recip. Meat Conf American Meat Science Association 1991; 44, 7–20

    CAS  Google Scholar 

  • Root, D. D.; Wang, K. Calmodulin-sensitive interaction of human nebulin fragments with actin and myosin. Biochemistry 1994 33, 12581–12591

    CAS  Google Scholar 

  • Salamino, F.; De Tullio, R.; Mengotti, P.; Melloni, E.; Pontremoli, S. Differential regulation of mu-and m-calpainin rat hearts perfused with Cat’ and cAMP. Biochem. Biophys. Res. Commun 1994 202, 1197–1203

    CAS  Google Scholar 

  • Schollmeyer, J. E. Possible role of calpain I and calpain Il in differentiating muscle. Exp. Cell Res 1986a 163, 413–422

    CAS  Google Scholar 

  • Schollmeyer, J. E. Role of Ca“ and Ca’-activated protease in myoblast fusion. Exp. Cell Res 1986b 162, 411–422

    CAS  Google Scholar 

  • Shackelford, S. D.; Koohmaraie, M.; Cundiff, L. V.; Gregory, K. E.; Rohrer, G. A.; Savell, J. W. 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 1994 72,857–863

    CAS  Google Scholar 

  • Shackelford, S. D.; Koohmaraie, M.; Miller, M. F.; Crouse, J. D.; Reagan, J. O. An evaluation of tenderness of the longissimus muscle of Angus by Hereford versus Brahman crossbred heifers. J. Anim. Sci 1991a 69, 171–177

    CAS  Google Scholar 

  • Shackelford, S. D.; Koohmaraie, M.; Whipple, G.; Wheeler, T. L.; Miller, J. D.; Reagan, J. O. Predictors of tenderness: Development and verification. J. Food Sci 1991b 56, 11–30

    Google Scholar 

  • Shannon, J. D.; Goll, D. E. Properties of a protein that is purified from bovine skeletal muscle that inhibits the Ca2+-dependent proteinase. Prog. Clin. Biol. Res 1985 180, 257–259

    CAS  Google Scholar 

  • Shih, C. L.; Chen, M. J.; Linse, K.; Wang, K. Molecular contacts between nebulin and actin: cross-linking of nebulin modules to the N-terminus of actin. Biochemistry 1997 36, 1814–1825

    CAS  Google Scholar 

  • Straub, V.; Bittner, R. E.; Leger, J. J.; Voit, T. Direct visualization of the dystrophin network on skeletal muscle fiber membrane. J. Cell Biol 1992 119, 1183–1191

    CAS  Google Scholar 

  • Suzuki, K. The structure of calpains and the calpain gene. In Intracellular calcium-dependent proteolysis; R. L. Mellgren and T. Murachi, Eds.; CRC Press: Boca Raton, Floroda, 1990; pp 25–35

    Google Scholar 

  • Suzuki, K.; Saido, T. C.; Hirai, S. Modulation of cellular signals by calpain. Ann. N. Y. Acad. Sci 1992 674, 218–227

    CAS  Google Scholar 

  • Suzuki, K.; Tsuji, S.; Ishiura, S.; Kimura, Y.; Kubota, S.; Imahori, K. Autolysis of calcium-activated neutral protease of chicken skeletal muscle. J. Biochem. (Tokyo) 1981 90,1787–1793

    CAS  Google Scholar 

  • Swasdison, S.; Mayne, R. Location of the integrin complex and extracellular matrix molecules at the chicken myotendinous junction. Cell Tissue Res 1989 257, 537–543

    CAS  Google Scholar 

  • Takano, E.; Maki, M.; Hatanaka, M.; Mori, H.; Zenita, K.; Sakihama, T.; Kannagi, R.; Marti, T.; Titani, K.; Mu-rachi, T. Evidence for the repetitive domain structure of pig calpastatin as demonstrated by cloning of complementary DNA. FEBSLett 1986 208, 199–202

    CAS  Google Scholar 

  • Takano, E.; Maki, M.; Mori, H.; Hatanaka, M.; Marti, T.; Titani, K.; Kannagi, R.; Ooi, T.; Murachi, T. Pig heart calpastatin: identification of repetitive domain structures and anomalous behavior in polyacrylamide gel electrophoresis. Biochemistry 1988 27, 1964–1972

    CAS  Google Scholar 

  • Takano, E.; Yumoto, N.; Kannagi, R.; Murachi, T. Molecular diversity of calpastatin in mammalian organs. Biochem. Biophys. Res. Commun 1984 122, 912–917

    CAS  Google Scholar 

  • Tanabe, R.; Tatsumi, R.; Takahashi, K. Purification and characterization of the 1,200-kDa subfragment of connectin filaments produced by 0.1 mM calcium ions. J. Biochem. (Tokyo) 1994 115, 351–355

    CAS  Google Scholar 

  • Taylor, R. G.; Geesink, G. H.; Thompson, V. F.; Koohmaraie, M.; Goll, D. E. Is Z-disk degradation responsible for postmortem tenderization? J. Anim. Sci 1995, 73, 1351–1367

    CAS  Google Scholar 

  • Tidball, J. G.; O’Halloran, T.; Burridge, K. Talin at myotendinous junctions. J. Cell Biol 1986 103, 1465–1472

    CAS  Google Scholar 

  • Trinick, J. Titin and nebulin: protein rulers in muscle? Trends Biochem. Sci 1994 19, 405–409

    CAS  Google Scholar 

  • Trombitas, K.; Pollack, G. H. Elastic properties of the titin filament in the Z-line region of vertebrate striated muscle. J. Muscle Res. Cell Motil 1993 14, 416–422

    CAS  Google Scholar 

  • Trombitas, K.; Pollack, G. H.; Wright, J.; Wang, K. Elastic properties of titin filaments demonstrated using a “freeze-break” technique. Cell Motil. Cytoskeleton 1993 24, 274–283

    CAS  Google Scholar 

  • Uemori, T.; Shimojo, T.; Asada, K.; Asano, T.; Kimizuka, F.; Kato, I.; Maki, M.; Hatanaka, M.; Murachi, T.; Hanzawa, H.; et al. Characterization of a functional domain of human calpastatin. Biochem. Biophys. Res. Commun 1990 166, 1485–1493

    CAS  Google Scholar 

  • Volk, T.; Fessier, L. I.; Fessier, J. H. A role for integrin in the formation of sarcomeric cytoarchitecture. Cell 1990 63, 525–536

    CAS  Google Scholar 

  • Wang, K. Titin/connectin and nebulin: giant protein rulers of muscle structure and function. Adv. Biophys 1996, 33, 123–134

    CAS  Google Scholar 

  • Wang, K.; Ash, J. F.; Singer, S. J.; Gomer, R. H. Filamin, a new high-molecular-weight prtotein found in smooth muscle and non-muscle cells. Proc. Natl. Acad. Sci. USA 1975 72, 4483–4486

    CAS  Google Scholar 

  • Wang, K.; Knipfer, M.; Huang, Q. Q.; van Heerden, A.; Hsu, L. C.; Gutierrez, G.; Quian, X. L.; Stedman, H. Human skeletal muscle nebulin sequence encodes a blueprint for thin filament architecture. Sequence motifs and affinity profiles of tandem repeats and terminal SH3. J. Biol. Chem 1996 271, 4304–4314

    CAS  Google Scholar 

  • Wang, K.; Wright, J. Architecture of the sarcomere matrix of skeletal muscle: immunoelectron microscopic evidence that suggests a set of parallel inextensible nebulin filaments anchored at the Z line. J. Cell Biol 1988 107,2199–2212

    CAS  Google Scholar 

  • Wheeler, T. L.; Koohmaraie, M. Effects of the beta-adrenergic agonist L644,969 on muscle protein turnover, endogenous proteinase activities, and meat tenderness in steers. J. Anim. Sci 1992 70,3035–3043

    CAS  Google Scholar 

  • Whipple, G.; Koohmaraie, M.; Dikeman, M. E.; Crouse, J. D. Predicting beef-longissimus tenderness from various biochemical and histological muscle traits. J. Anim. Sci 1990a 68, 4193–4199

    CAS  Google Scholar 

  • Whipple, G.; Koohmaraie, M.; Dikeman, M. E.; Crouse, J. D.; Hunt, M. C.; Klemm, R. D. Evaluation of attributes that affect longissimus muscle tenderness in Bos taurus and Bos indicus cattle. J. Anim. Sci 1990b 68, 2716–2728

    CAS  Google Scholar 

  • Yang, H. Q.; Ma, H.; Takano, E.; Hatanaka, M.; Maki, M. Analysis of calcium-dependent interaction between amino-terminal conserved region of calpastatin functional domain and calmodulin-like domain of mu-calpain large subunit. J. Biol. Chem 1994 269, 18977–18984

    CAS  Google Scholar 

  • Yoshizawa, T.; Sorimachi, H.; Tomioka, S.; Ishiura, S.; Suzuki, K. Calpain dissociates into subunits in the presence of calcium ions. Biochem. Biophys. Res. Commun 1995a 208, 376–383

    CAS  Google Scholar 

  • Yoshizawa, T.; Sorimachi, H.; Tomioka, S.; Ishiura, S.; Suzuki, K. A. catalytic subunit of calpain possesses full proteolytic activity. FEBSLett 1995b 358, 101–103

    CAS  Google Scholar 

  • Zot, A. S.; Potter, J. D. Structural aspects of troponin-tropomyosin regulation of skeletal muscle contraction. Annu. Rev. Biophys. Biophys. Chem 1987 16, 535–559

    CAS  Google Scholar 

Download references

Author information

Authors and Affiliations

  1. Department of Animal Science, Iowa State University, Ames, Iowa, 50011, USA

    Elisabeth Huff-Lonergan & Steven M. Lonergan

Authors
  1. Elisabeth Huff-Lonergan
    View author publications

    You can also search for this author in PubMed Google Scholar

  2. Steven M. Lonergan
    View author publications

    You can also search for this author in PubMed Google Scholar

Editor information

Editors and Affiliations

  1. University of Kentucky, Lexington, Kentucky, USA

    Youling L. Xiong

  2. The State University of New Jersey, Rutgers New Brunswick, New Jersey, USA

    Ho Chi-Tang

  3. Memorial University of Newfoundland, St. John’s, Newfoundland, Canada

    Fereidoon Shahidi

Rights and permissions

Reprints and permissions

Copyright information

© 1999 Springer Science+Business Media New York

About this chapter

Cite this chapter

Huff-Lonergan, E., Lonergan, S.M. (1999). Postmortem Mechanisms of Meat Tenderization. In: Xiong, Y.L., Chi-Tang, H., Shahidi, F. (eds) Quality Attributes of Muscle Foods. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-4731-0_16

Download citation

  • DOI: https://doi.org/10.1007/978-1-4615-4731-0_16

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4613-7144-1

  • Online ISBN: 978-1-4615-4731-0

  • eBook Packages: Springer Book Archive

Publish with us

Policies and ethics

Search

Navigation