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Volumn 87, Issue 10, 2008, Pages 2126-2132

Role of calpains in postmortem proteolysis in chicken muscle

Author keywords

Calpain; Chicken; Meat tenderness; Muscle; Postmortem proteolysis

Indexed keywords

AVES; BOS; MAMMALIA;

EID: 53349151929     PISSN: 00325791     EISSN: 15253171     Source Type: Journal    
DOI: 10.3382/ps.2007-00296     Document Type: Article
Times cited : (59)

References (53)
  • 1
    • 0033650175 scopus 로고    scopus 로고
    • Calpain zymography with casein or fluorescein isothiocyanate casein
    • Arthur, J. S., and D. L. Mykles. 2000. Calpain zymography with casein or fluorescein isothiocyanate casein. Methods Mol. Biol. 144:109-116.
    • (2000) Methods Mol. Biol , vol.144 , pp. 109-116
    • Arthur, J.S.1    Mykles, D.L.2
  • 2
    • 0002175969 scopus 로고    scopus 로고
    • Blanchard, P. L., and D. Mantle. 1996. Comparison of proteolytic enzyme levels in chicken, pig, lamb, and rabbit muscle at point of slaughter: Role in meat tenderisation post mortem. J. Sci. Food Agric. 71:83-91.
    • Blanchard, P. L., and D. Mantle. 1996. Comparison of proteolytic enzyme levels in chicken, pig, lamb, and rabbit muscle at point of slaughter: Role in meat tenderisation post mortem. J. Sci. Food Agric. 71:83-91.
  • 3
    • 0001383470 scopus 로고
    • Optimisation of tenderisation, ageing and tenderness
    • Dransfield, E. 1994. Optimisation of tenderisation, ageing and tenderness. Meat Sci. 36:105-121.
    • (1994) Meat Sci , vol.36 , pp. 105-121
    • Dransfield, E.1
  • 4
    • 4444281342 scopus 로고    scopus 로고
    • Breed differences in the biochemical determinism of ultimate pH in breast muscles of broilers chickens - A key role of AMP deaminase
    • El Rammouz, R., C. Berri, E. Le Bihan, R. Babilé, and X. Fernandez. 2004. Breed differences in the biochemical determinism of ultimate pH in breast muscles of broilers chickens - A key role of AMP deaminase. Poult. Sci. 83:1445-1451.
    • (2004) Poult. Sci , vol.83 , pp. 1445-1451
    • El Rammouz, R.1    Berri, C.2    Le Bihan, E.3    Babilé, R.4    Fernandez, X.5
  • 5
    • 0037306431 scopus 로고    scopus 로고
    • Differential expression of components of the proteasome pathway in rat tissues
    • Farout, L., S. Clavel, M. Lamare, Y. Briand, and M. Briand. 2003. Differential expression of components of the proteasome pathway in rat tissues. Comp. Biochem. Physiol. 134:297-305.
    • (2003) Comp. Biochem. Physiol , vol.134 , pp. 297-305
    • Farout, L.1    Clavel, S.2    Lamare, M.3    Briand, Y.4    Briand, M.5
  • 6
    • 84985294913 scopus 로고
    • Changes in titin and nebulin in post mortem bovine muscle revealed by gel electrophoresis, Western blotting and immunofluorescence microscopy
    • Fritz, J., and M. Greaser. 1991. Changes in titin and nebulin in post mortem bovine muscle revealed by gel electrophoresis, Western blotting and immunofluorescence microscopy. J. Food Sci. 56:607-610.
    • (1991) J. Food Sci , vol.56 , pp. 607-610
    • Fritz, J.1    Greaser, M.2
  • 7
    • 0002849290 scopus 로고    scopus 로고
    • Involvement of calpains in post mortem tenderisation. A review of recent research
    • Geesink, G. H., M. A. Ilian, J. D. Morgan, and R. Bickerstaffe. 2000. Involvement of calpains in post mortem tenderisation. A review of recent research. Proc. N. Z. Soc. Anim. Prod. 60:99-102.
    • (2000) Proc. N. Z. Soc. Anim. Prod , vol.60 , pp. 99-102
    • Geesink, G.H.1    Ilian, M.A.2    Morgan, J.D.3    Bickerstaffe, R.4
  • 8
    • 0033208806 scopus 로고    scopus 로고
    • Effect of calpastatin on degradation of myofibrillar proteins by μ-calpain under postmortem conditions
    • Geesink, G. H., and M. Koohmaraie. 1999. Effect of calpastatin on degradation of myofibrillar proteins by μ-calpain under postmortem conditions. J. Anim. Sci. 77:2685-2692.
    • (1999) J. Anim. Sci , vol.77 , pp. 2685-2692
    • Geesink, G.H.1    Koohmaraie, M.2
  • 9
    • 0034264486 scopus 로고    scopus 로고
    • Ionic strength-induced inactivation of μ-calpain in postmortem muscle
    • Geesink, G. H., and M. Koohmaraie. 2000. Ionic strength-induced inactivation of μ-calpain in postmortem muscle. J. Anim. Sci. 78:2336-2343.
    • (2000) J. Anim. Sci , vol.78 , pp. 2336-2343
    • Geesink, G.H.1    Koohmaraie, M.2
  • 10
    • 33749402662 scopus 로고    scopus 로고
    • μ-Calpain is essential for postmortem proteolysis of muscle proteins
    • Geesink, G. H., S. Kuchay, A. H. Chishti, and M. Koohmaraie. 2006. μ-Calpain is essential for postmortem proteolysis of muscle proteins. J. Anim. Sci. 84:2834-2840.
    • (2006) J. Anim. Sci , vol.84 , pp. 2834-2840
    • Geesink, G.H.1    Kuchay, S.2    Chishti, A.H.3    Koohmaraie, M.4
  • 11
    • 33646015361 scopus 로고    scopus 로고
    • Calpain 3/p94 is not involved in postmortem proteolysis
    • Geesink, G. H., R. G. Taylor, and M. Koohmaraie. 2005. Calpain 3/p94 is not involved in postmortem proteolysis. J. Anim. Sci. 83:1646-1652.
    • (2005) J. Anim. Sci , vol.83 , pp. 1646-1652
    • Geesink, G.H.1    Taylor, R.G.2    Koohmaraie, M.3
  • 13
    • 84987361482 scopus 로고
    • Polyacrylamide disc gel electrophoresis of fresh and aged chicken muscle proteins in sodium dodecylsulfate
    • Hay, J. D., R. W. Currie, and F. H. Wolfe. 1973. Polyacrylamide disc gel electrophoresis of fresh and aged chicken muscle proteins in sodium dodecylsulfate. J. Food Sci. 38:987-990.
    • (1973) J. Food Sci , vol.38 , pp. 987-990
    • Hay, J.D.1    Currie, R.W.2    Wolfe, F.H.3
  • 14
    • 0030141091 scopus 로고    scopus 로고
    • Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle
    • 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.
    • (1996) J. Anim. Sci , vol.74 , pp. 993-1008
    • Huff-Lonergan, E.1    Mitsuhashi, T.2    Beekman, D.D.3    Parrish Jr, F.C.4    Olson, D.G.5    Robson, R.M.6
  • 15
    • 43949173699 scopus 로고
    • The concentration of free magnesium and free calcium ions both increase in skeletal muscle fibers entering rigor mortis
    • Jeacoke, R. 1993. The concentration of free magnesium and free calcium ions both increase in skeletal muscle fibers entering rigor mortis. Meat Sci. 35:27-45.
    • (1993) Meat Sci , vol.35 , pp. 27-45
    • Jeacoke, R.1
  • 16
    • 33646518594 scopus 로고    scopus 로고
    • Changes in concentration of sarcoplasmic free calcium during post mortem ageing of meat
    • Ji, J. R., and K. Takahashi. 2006. Changes in concentration of sarcoplasmic free calcium during post mortem ageing of meat. Meat Sci. 73:395-403.
    • (2006) Meat Sci , vol.73 , pp. 395-403
    • Ji, J.R.1    Takahashi, K.2
  • 17
    • 0026591107 scopus 로고
    • 2+-dependent proteases (calpains) in postmortem proteolysis and meat tenderness
    • 2+-dependent proteases (calpains) in postmortem proteolysis and meat tenderness. Biochimie 74:239-245.
    • (1992) Biochimie , vol.74 , pp. 239-245
    • Koohmaraie, M.1
  • 18
    • 0002514983 scopus 로고
    • Muscle proteinases and meat aging
    • Koohmaraie, M. 1994. Muscle proteinases and meat aging. Meat Sci. 36:93-104.
    • (1994) Meat Sci , vol.36 , pp. 93-104
    • Koohmaraie, M.1
  • 19
    • 0030305245 scopus 로고    scopus 로고
    • Biochemical factors regulating the toughening and tenderization processes of meat
    • Koohmaraie, M. 1996. Biochemical factors regulating the toughening and tenderization processes of meat. Meat Sci. 43:193-201.
    • (1996) Meat Sci , vol.43 , pp. 193-201
    • Koohmaraie, M.1
  • 20
    • 0030330032 scopus 로고    scopus 로고
    • Meat toughening does not occur when rigor shortening is prevented
    • Koohmaraie, M., E. Doumit, and T. L. Wheeler. 1996. Meat toughening does not occur when rigor shortening is prevented. J. Anim. Sci. 74:2935-2942.
    • (1996) J. Anim. Sci , vol.74 , pp. 2935-2942
    • Koohmaraie, M.1    Doumit, E.2    Wheeler, T.L.3
  • 21
    • 33745648075 scopus 로고    scopus 로고
    • Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system
    • Koohmaraie, M., and G. H. Geesink. 2006. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Sci. 74:34-43.
    • (2006) Meat Sci , vol.74 , pp. 34-43
    • Koohmaraie, M.1    Geesink, G.H.2
  • 23
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.1
  • 24
    • 0036313464 scopus 로고    scopus 로고
    • Changes in proteasome activity during postmortem aging of bovine muscle
    • Lamare, M., R. Taylor, L. Farout, Y. Briand, and M. Briand. 2002. Changes in proteasome activity during postmortem aging of bovine muscle. Meat Sci. 61:199-204.
    • (2002) Meat Sci , vol.61 , pp. 199-204
    • Lamare, M.1    Taylor, R.2    Farout, L.3    Briand, Y.4    Briand, M.5
  • 26
    • 0000376784 scopus 로고
    • Postmortem evolution of rheological properties of the myofibrillar structure
    • Lepetit, J., P. Salé, and A. Ouali. 1986. Postmortem evolution of rheological properties of the myofibrillar structure. Meat Sci. 16:161-174.
    • (1986) Meat Sci , vol.16 , pp. 161-174
    • Lepetit, J.1    Salé, P.2    Ouali, A.3
  • 27
    • 1942540733 scopus 로고    scopus 로고
    • Effects of autolysis on properties of μ- and m-calpain
    • Li, H., V. F. Thompson, and D. E. Goll. 2004. Effects of autolysis on properties of μ- and m-calpain. Biochim. Biophys. Acta 1691:91-103.
    • (2004) Biochim. Biophys. Acta , vol.1691 , pp. 91-103
    • Li, H.1    Thompson, V.F.2    Goll, D.E.3
  • 28
    • 84987313519 scopus 로고
    • The 30,000-dalton component of tender bovine longissimus muscle
    • MacBride, M. A., and F. C. Parrish. 1977. The 30,000-dalton component of tender bovine longissimus muscle. J. Food Sci. 42:1627-1629.
    • (1977) J. Food Sci , vol.42 , pp. 1627-1629
    • MacBride, M.A.1    Parrish, F.C.2
  • 29
    • 0030678069 scopus 로고    scopus 로고
    • Physical and biochemical effects of broiler breast tenderization by aging after pre-rigor deboning
    • McKee, S. R., E. M. Hirschler, and A. R. Sams. 1997. Physical and biochemical effects of broiler breast tenderization by aging after pre-rigor deboning. J. Food Sci. 62:959-962.
    • (1997) J. Food Sci , vol.62 , pp. 959-962
    • McKee, S.R.1    Hirschler, E.M.2    Sams, A.R.3
  • 30
    • 0030306560 scopus 로고    scopus 로고
    • The origin of the 30 kDa component appearing during post-mortem ageing of bovine muscle
    • Negishi, H., E. Yamamoto, and T. Kuwata. 1996. The origin of the 30 kDa component appearing during post-mortem ageing of bovine muscle. Meat Sci. 42:289-303.
    • (1996) Meat Sci , vol.42 , pp. 289-303
    • Negishi, H.1    Yamamoto, E.2    Kuwata, T.3
  • 31
    • 0031092826 scopus 로고    scopus 로고
    • Nurmahmudi, and A. R. Sams. 1997. Tenderizing spent fowl meat with calcium chloride. 3. Biochemical characteristics of tenderized breast meat. Poult. Sci. 76:543-547.
    • Nurmahmudi, , and A. R. Sams. 1997. Tenderizing spent fowl meat with calcium chloride. 3. Biochemical characteristics of tenderized breast meat. Poult. Sci. 76:543-547.
  • 32
    • 23344432106 scopus 로고    scopus 로고
    • Effect of processing on turkey meat quality and proteolysis
    • Obanor, F., J. D. Morton, G. H. Geesink, and R. Bickerstaffe. 2005. Effect of processing on turkey meat quality and proteolysis. Poult. Sci. 84:1123-1128.
    • (2005) Poult. Sci , vol.84 , pp. 1123-1128
    • Obanor, F.1    Morton, J.D.2    Geesink, G.H.3    Bickerstaffe, R.4
  • 33
    • 44949286385 scopus 로고
    • Modeling of the formation of pale, soft and exudative meat effects of chilling regime and rate and extent of glycolysis
    • Offer, G. 1991. Modeling of the formation of pale, soft and exudative meat effects of chilling regime and rate and extent of glycolysis. Meat Sci. 30:157-184.
    • (1991) Meat Sci , vol.30 , pp. 157-184
    • Offer, G.1
  • 34
    • 84985046283 scopus 로고
    • Effect of post mortem storage and calcium activated factor on the myofibrillar proteins of bovine skeletal muscle
    • Olson, D. G., F. C. Parrish, W. R. Dayton, and D. E. Goll. 1977. Effect of post mortem storage and calcium activated factor on the myofibrillar proteins of bovine skeletal muscle. J. Food Sci. 42:117-124.
    • (1977) J. Food Sci , vol.42 , pp. 117-124
    • Olson, D.G.1    Parrish, F.C.2    Dayton, W.R.3    Goll, D.E.4
  • 35
    • 0026539218 scopus 로고
    • Proteolytic and physicocohemical mechanisms involved in meat texture development
    • Ouali, A. 1992. Proteolytic and physicocohemical mechanisms involved in meat texture development. Biochimie 74:251-265.
    • (1992) Biochimie , vol.74 , pp. 251-265
    • Ouali, A.1
  • 37
    • 0000852182 scopus 로고
    • Relationship between toughness and troponin T in condition beef
    • Penny, I. F., and E. Dransfield. 1979. Relationship between toughness and troponin T in condition beef. Meat Sci. 3:135-141.
    • (1979) Meat Sci , vol.3 , pp. 135-141
    • Penny, I.F.1    Dransfield, E.2
  • 38
    • 0029048989 scopus 로고
    • Casein zymography: A method to study μ-calpain, m-calpain, and their inhibitory agents
    • Raser, K. J., A. Posner, and K. K. Wang. 1995. Casein zymography: A method to study μ-calpain, m-calpain, and their inhibitory agents. Arch. Biochem. Biophys. 319:211-216.
    • (1995) Arch. Biochem. Biophys , vol.319 , pp. 211-216
    • Raser, K.J.1    Posner, A.2    Wang, K.K.3
  • 39
    • 0033478347 scopus 로고    scopus 로고
    • The effect of proteasome on myofibrillar structures in bovine skeletal muscle
    • Robert, N., M. Briand, R. Taylor, and Y. Briand. 1999. The effect of proteasome on myofibrillar structures in bovine skeletal muscle. Meat Sci. 51:149-153.
    • (1999) Meat Sci , vol.51 , pp. 149-153
    • Robert, N.1    Briand, M.2    Taylor, R.3    Briand, Y.4
  • 41
    • 0009972943 scopus 로고
    • Characterization of rigor mortis development in four broiler muscles
    • Sams, A. R., and D. M. Janky. 1991. Characterization of rigor mortis development in four broiler muscles. Poult. Sci. 70:1003-1009.
    • (1991) Poult. Sci , vol.70 , pp. 1003-1009
    • Sams, A.R.1    Janky, D.M.2
  • 42
    • 0034392314 scopus 로고    scopus 로고
    • The measurement of pH in raw and frozen turkey pectoralis superficialis muscle
    • Santé, V., and X. Fernandez. 2000. The measurement of pH in raw and frozen turkey pectoralis superficialis muscle. Meat Sci. 55:503-506.
    • (2000) Meat Sci , vol.55 , pp. 503-506
    • Santé, V.1    Fernandez, X.2
  • 43
    • 53349119927 scopus 로고    scopus 로고
    • SAS Institute. 1989. SAS/STAT User's Guide for Personal Computers. Release 6.03. SAS Institute Inc., Cary, NC.
    • SAS Institute. 1989. SAS/STAT User's Guide for Personal Computers. Release 6.03. SAS Institute Inc., Cary, NC.
  • 44
    • 23044459313 scopus 로고    scopus 로고
    • Postmortem changes in chicken muscle
    • Schreurs, F. J. G. 2000. Postmortem changes in chicken muscle. World's Poult. Sci. J. 56:319-346.
    • (2000) World's Poult. Sci. J , vol.56 , pp. 319-346
    • Schreurs, F.J.G.1
  • 45
    • 0036986447 scopus 로고    scopus 로고
    • Role of muscle endopeptidases and their inhibitors in meat tenderness
    • Sentandreu, M. A., G. Coulis, and A. Ouali. 2002. Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends Food Sci. Technol. 13:400-421.
    • (2002) Trends Food Sci. Technol , vol.13 , pp. 400-421
    • Sentandreu, M.A.1    Coulis, G.2    Ouali, A.3
  • 46
    • 84989992009 scopus 로고
    • A "cold shortening" effect in avian muscle
    • Smith, M. C., M. D. Judge, and W. D. Stadelman. 1969. A "cold shortening" effect in avian muscle. J. Food Sci. 34:42-46.
    • (1969) J. Food Sci , vol.34 , pp. 42-46
    • Smith, M.C.1    Judge, M.D.2    Stadelman, W.D.3
  • 47
    • 0028959934 scopus 로고
    • Identification of a third ubiquitous calpain species-Chicken muscle expresses four distinct calpains
    • Sorimachi, H., T. Tsukahara, M. Okada-Ban, H. Sugita, S. Ishiura, and K. Suzuki. 1995. Identification of a third ubiquitous calpain species-Chicken muscle expresses four distinct calpains. Biochim. Biophys. Acta 1261:381-393.
    • (1995) Biochim. Biophys. Acta , vol.1261 , pp. 381-393
    • Sorimachi, H.1    Tsukahara, T.2    Okada-Ban, M.3    Sugita, H.4    Ishiura, S.5    Suzuki, K.6
  • 49
    • 18944394460 scopus 로고    scopus 로고
    • Effects of aging prior to freezing on poultry meat tenderness
    • Thielke, S., S. K. Lhafi, and M. Kuhne. 2005. Effects of aging prior to freezing on poultry meat tenderness. Poult. Sci. 84:607-612.
    • (2005) Poult. Sci , vol.84 , pp. 607-612
    • Thielke, S.1    Lhafi, S.K.2    Kuhne, M.3
  • 50
    • 0942300420 scopus 로고    scopus 로고
    • The roles of the proteasome, and cathepsins B, L, H and D, in ostrich meat tenderisation
    • Thomas, R., H. Gondoza, L. C. Hoffman, V. Oosthuizen, and R. J. Naudé. 2004. The roles of the proteasome, and cathepsins B, L, H and D, in ostrich meat tenderisation. Meat Sci. 67:113-120.
    • (2004) Meat Sci , vol.67 , pp. 113-120
    • Thomas, R.1    Gondoza, H.2    Hoffman, L.C.3    Oosthuizen, V.4    Naudé, R.J.5
  • 51
    • 0033071697 scopus 로고    scopus 로고
    • Postmortem pH, myofibrillar fragmentation, and calpain activity in pectoralis from electrically stimulated and muscle tensioned broiler carcasses
    • Veeramuthu, G. I., and A. R. Sams. 1999. Postmortem pH, myofibrillar fragmentation, and calpain activity in pectoralis from electrically stimulated and muscle tensioned broiler carcasses. Poult. Sci. 78:272-276.
    • (1999) Poult. Sci , vol.78 , pp. 272-276
    • Veeramuthu, G.I.1    Sams, A.R.2
  • 52
    • 0035381015 scopus 로고    scopus 로고
    • Effect of postmortem storage on μ-calpain and m-calpain in ovine skeletal muscle
    • Veiseth, E., S. D. Shackelford, T. L. Wheeler, and M. Koohmaraie. 2001. Effect of postmortem storage on μ-calpain and m-calpain in ovine skeletal muscle. J. Anim. Sci. 79:1502-1508.
    • (2001) J. Anim. Sci , vol.79 , pp. 1502-1508
    • Veiseth, E.1    Shackelford, S.D.2    Wheeler, T.L.3    Koohmaraie, M.4
  • 53
    • 0028432852 scopus 로고
    • Prerigor and postrigor changes in tenderness of ovine longissimus muscle
    • Wheeler, T. L., and M. Koohmaraie. 1994. Prerigor and postrigor changes in tenderness of ovine longissimus muscle. J. Anim. Sci. 72:1232-1238.
    • (1994) J. Anim. Sci , vol.72 , pp. 1232-1238
    • Wheeler, T.L.1    Koohmaraie, M.2


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