메뉴 건너뛰기




Volumn 8, Issue 9, 2013, Pages

Characterisation and Expression of Calpain Family Members in Relation to Nutritional Status, Diet Composition and Flesh Texture in Gilthead Sea Bream (Sparus aurata)

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; CALPAIN 1; CALPAIN 2; CALPAIN 3; CARBOHYDRATE; FATTY ACID; GLUCOSE; PROTEIN; TRIACYLGLYCEROL;

EID: 84884565009     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0075349     Document Type: Article
Times cited : (53)

References (61)
  • 1
    • 84884555501 scopus 로고    scopus 로고
    • APROMAR, Ministerio de Medio Ambiente y Medio Rural y Marino. Madrid
    • APROMAR (2012) La Acuicultura Marina de Peces en España 2012. Ministerio de Medio Ambiente y Medio Rural y Marino. Madrid.
    • (2012) La Acuicultura Marina de Peces en España 2012
  • 2
    • 21144481008 scopus 로고
    • Characteristics of rainbow trout flesh: I. Chemical composition and cellularity of muscle and adipose tissues
    • Fauconneau B, Chmaitilly J, Andre S, Cardinal M, Cornet J, et al. (1993) Characteristics of rainbow trout flesh: I. Chemical composition and cellularity of muscle and adipose tissues. Sci Aliment 13: 173-187.
    • (1993) Sci Aliment , vol.13 , pp. 173-187
    • Fauconneau, B.1    Chmaitilly, J.2    Andre, S.3    Cardinal, M.4    Cornet, J.5
  • 4
    • 44949273136 scopus 로고
    • Changes in the structure and function of the epaxial muscle of rainbow trout (Oncorhynchus mykiss) in relation to ration and age: I. Growth dynamics
    • Kiessling A, Storebakken T, Åsgård T, Kiessling K-H, (1991) Changes in the structure and function of the epaxial muscle of rainbow trout (Oncorhynchus mykiss) in relation to ration and age: I. Growth dynamics. Aquaculture 93: 335-356.
    • (1991) Aquaculture , vol.93 , pp. 335-356
    • Kiessling, A.1    Storebakken, T.2    Åsgård, T.3    Kiessling, K.-H.4
  • 5
    • 0037205861 scopus 로고    scopus 로고
    • Effects of dietary protein level on muscle cellularity and flesh quality in Atlantic salmon with particular reference to gaping
    • Johnston IA, Manthri S, Alderson R, Campbell P, Mitchell D, et al. (2002) Effects of dietary protein level on muscle cellularity and flesh quality in Atlantic salmon with particular reference to gaping. Aquaculture 210: 259-283.
    • (2002) Aquaculture , vol.210 , pp. 259-283
    • Johnston, I.A.1    Manthri, S.2    Alderson, R.3    Campbell, P.4    Mitchell, D.5
  • 6
    • 77951620679 scopus 로고    scopus 로고
    • Skeletal muscle growth dynamics and expression of related genes in white and red muscles of rainbow trout fed diets with graded levels of a mixture of plant protein sources as substitutes for fishmeal
    • Alami-Durante H, Médale F, Cluzeaud M, Kaushik SJ, (2010) Skeletal muscle growth dynamics and expression of related genes in white and red muscles of rainbow trout fed diets with graded levels of a mixture of plant protein sources as substitutes for fishmeal. Aquaculture 303: 50-58.
    • (2010) Aquaculture , vol.303 , pp. 50-58
    • Alami-Durante, H.1    Médale, F.2    Cluzeaud, M.3    Kaushik, S.J.4
  • 7
    • 3142564830 scopus 로고    scopus 로고
    • Growth performance, muscle structure and flesh quality in out-of-season Atlantic salmon (Salmo salar) smolts reared under two different photoperiod regimes
    • Johnston IA, Manthri S, Bickerdike R, Dingwall A, Luijkx R, et al. (2004) Growth performance, muscle structure and flesh quality in out-of-season Atlantic salmon (Salmo salar) smolts reared under two different photoperiod regimes. Aquaculture 237: 281-300.
    • (2004) Aquaculture , vol.237 , pp. 281-300
    • Johnston, I.A.1    Manthri, S.2    Bickerdike, R.3    Dingwall, A.4    Luijkx, R.5
  • 8
    • 0029858361 scopus 로고    scopus 로고
    • Muscle cellularity in relation to somatic growth in the European sea bass Dicentrarchus labrax (L.)
    • Nathanailides C, Lopez-Albors O, Abellan E, Vazquer JM, Tyler DD, et al. (1996) Muscle cellularity in relation to somatic growth in the European sea bass Dicentrarchus labrax (L.). Aquacult Res 27: 885-889.
    • (1996) Aquacult Res , vol.27 , pp. 885-889
    • Nathanailides, C.1    Lopez-Albors, O.2    Abellan, E.3    Vazquer, J.M.4    Tyler, D.D.5
  • 9
    • 0031920959 scopus 로고    scopus 로고
    • Embryonic temperature modulates muscle growth characteristics in larval and juvenile herring (Clupea harengus)
    • Johnston IA, Cole NJ, Abercromby M, Vieira VLA, (1998) Embryonic temperature modulates muscle growth characteristics in larval and juvenile herring (Clupea harengus). J Exp Biol 201: 623-646.
    • (1998) J Exp Biol , vol.201 , pp. 623-646
    • Johnston, I.A.1    Cole, N.J.2    Abercromby, M.3    Vieira, V.L.A.4
  • 10
    • 41749101726 scopus 로고    scopus 로고
    • Temperature influence on the white muscle growth dynamics of the sea bass Dicentrarchus labrax L. Flesh quality implications at commercial size
    • López-Albors O, Abdel I, Periago MJ, Ayala MD, Alcázar AG, et al. (2008) Temperature influence on the white muscle growth dynamics of the sea bass Dicentrarchus labrax L. Flesh quality implications at commercial size. Aquaculture 277: 39-51.
    • (2008) Aquaculture , vol.277 , pp. 39-51
    • López-Albors, O.1    Abdel, I.2    Periago, M.J.3    Ayala, M.D.4    Alcázar, A.G.5
  • 11
    • 0000703491 scopus 로고
    • Endurance exercise training in the fast and slow muscles of a teleost fish (Pollachius virens)
    • Johnston IA, Moon TW, (1980) Endurance exercise training in the fast and slow muscles of a teleost fish (Pollachius virens). J Comp Physiol 135: 147-156.
    • (1980) J Comp Physiol , vol.135 , pp. 147-156
    • Johnston, I.A.1    Moon, T.W.2
  • 12
    • 0000026442 scopus 로고
    • Growth and composition of the swimming muscle of adult Atlantic salmon (Salmo salar L.) during long-term sustained swimming
    • Totland GK, Kryvi H, Jødestol KA, Christiansen EN, Tangerås A, et al. (1987) Growth and composition of the swimming muscle of adult Atlantic salmon (Salmo salar L.) during long-term sustained swimming. Aquaculture 66: 299-313.
    • (1987) Aquaculture , vol.66 , pp. 299-313
    • Totland, G.K.1    Kryvi, H.2    Jødestol, K.A.3    Christiansen, E.N.4    Tangerås, A.5
  • 13
    • 20744444140 scopus 로고    scopus 로고
    • The role of myostatin and the calcineurin signalling pathway in regulating muscle mass in response to exercise training in the rainbow trout Oncorhynchus mykiss Walbaum
    • Martin CI, Johnston IA, (2005) The role of myostatin and the calcineurin signalling pathway in regulating muscle mass in response to exercise training in the rainbow trout Oncorhynchus mykiss Walbaum. J Exp Biol 208: 2083-2090.
    • (2005) J Exp Biol , vol.208 , pp. 2083-2090
    • Martin, C.I.1    Johnston, I.A.2
  • 15
    • 33744551989 scopus 로고    scopus 로고
    • Effects of muscle proteases, endogenous protease inhibitors and myofibrils fragmentation on postmortem aging of goat meat
    • Nagaraj NS, Santhanam K, (2006) Effects of muscle proteases, endogenous protease inhibitors and myofibrils fragmentation on postmortem aging of goat meat. J Food Biochem 30: 269-291.
    • (2006) J Food Biochem , vol.30 , pp. 269-291
    • Nagaraj, N.S.1    Santhanam, K.2
  • 16
    • 82755189495 scopus 로고    scopus 로고
    • Calpains- an elaborate proteolytic system
    • Ono Y, Sorimachi H, (2012) Calpains- an elaborate proteolytic system. Biochim Biophys Acta 1824: 224-236.
    • (2012) Biochim Biophys Acta , vol.1824 , pp. 224-236
    • Ono, Y.1    Sorimachi, H.2
  • 18
    • 0028905205 scopus 로고
    • Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A
    • Richard I, Broux O, Allamand V, Fougerousse F, Chiannilkulchai N, et al. (1995) Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2A. Cell 81: 27-40.
    • (1995) Cell , vol.81 , pp. 27-40
    • Richard, I.1    Broux, O.2    Allamand, V.3    Fougerousse, F.4    Chiannilkulchai, N.5
  • 21
    • 11144273211 scopus 로고    scopus 로고
    • Identification and molecular characterization of the rainbow trout calpains (Capn1 and Capn2): their expression in muscle wasting during starvation
    • Salem M, Nath J, Rexroad CE, Killefer J, Yao J, (2005) Identification and molecular characterization of the rainbow trout calpains (Capn1 and Capn2): their expression in muscle wasting during starvation. Comp Biochem Physiol B Biochem Mol Biol 140: 63-71.
    • (2005) Comp Biochem Physiol B Biochem Mol Biol , vol.140 , pp. 63-71
    • Salem, M.1    Nath, J.2    Rexroad, C.E.3    Killefer, J.4    Yao, J.5
  • 22
    • 77949275252 scopus 로고    scopus 로고
    • Characterisation of capn1, capn2-like, capn3 and capn11 genes in Atlantic halibut (Hippoglossus hippoglossus L.): transcriptional regulation across tissues and in skeletal muscle at distinc nutritional states
    • Macqueen DJ, Meischke L, Manthri S, Anwar A, Solberg C, et al. (2010) Characterisation of capn1, capn2-like, capn3 and capn11 genes in Atlantic halibut (Hippoglossus hippoglossus L.): transcriptional regulation across tissues and in skeletal muscle at distinc nutritional states. Gene 453: 45-58.
    • (2010) Gene , vol.453 , pp. 45-58
    • Macqueen, D.J.1    Meischke, L.2    Manthri, S.3    Anwar, A.4    Solberg, C.5
  • 23
    • 40849094418 scopus 로고    scopus 로고
    • Characterization and comparative expression of zebrafish calpain system genes during early development
    • Lepage SE, Bruce AE, (2008) Characterization and comparative expression of zebrafish calpain system genes during early development. Dev Dyn 237: 819-829.
    • (2008) Dev Dyn , vol.237 , pp. 819-829
    • Lepage, S.E.1    Bruce, A.E.2
  • 24
    • 84875110634 scopus 로고    scopus 로고
    • Effect of nutrient restriction and re-feeding on calpain family genes in skeletal muscle of channel catfish (Ictalurus punctatus)
    • Preziosa E, Liu S, Terova G, Gao X, Liu H, et al. (2013) Effect of nutrient restriction and re-feeding on calpain family genes in skeletal muscle of channel catfish (Ictalurus punctatus). PLoS ONE 8: e59404.
    • (2013) PLoS ONE , vol.8
    • Preziosa, E.1    Liu, S.2    Terova, G.3    Gao, X.4    Liu, H.5
  • 25
    • 77954966042 scopus 로고    scopus 로고
    • A newly classified vertebrate calpain protease, directly ancestral to CAPN1 and 2, episodically evolved a restricted physiological function in placental mammals
    • Macqueen DJ, Delbridge ML, Manthri S, Johnston IA, (2010) A newly classified vertebrate calpain protease, directly ancestral to CAPN1 and 2, episodically evolved a restricted physiological function in placental mammals. Mol Biol Evol 27: 1886-1902.
    • (2010) Mol Biol Evol , vol.27 , pp. 1886-1902
    • Macqueen, D.J.1    Delbridge, M.L.2    Manthri, S.3    Johnston, I.A.4
  • 26
    • 22144478238 scopus 로고    scopus 로고
    • Characterization of calpastatin gene in fish: its potential role in muscle growth and fillet quality
    • Salem M, Yao J, Rexroad CE, Kenney PB, Semmens K, et al. (2005) Characterization of calpastatin gene in fish: its potential role in muscle growth and fillet quality. Comp Biochem Physiol B Biochem Mol Biol 141: 488-497.
    • (2005) Comp Biochem Physiol B Biochem Mol Biol , vol.141 , pp. 488-497
    • Salem, M.1    Yao, J.2    Rexroad, C.E.3    Kenney, P.B.4    Semmens, K.5
  • 27
    • 17944373246 scopus 로고    scopus 로고
    • Postmortem degradation of white fish skeletal muscle sea bass, (Dicentrarchus labrax): fat diet effects on in situ dystrophin proteolysis during the prerigor stage
    • Bonnal C, Raynaud F, Astier F, Lebart MC, Marcilhac A, et al. (2001) Postmortem degradation of white fish skeletal muscle sea bass, (Dicentrarchus labrax): fat diet effects on in situ dystrophin proteolysis during the prerigor stage. Mar Biotech 3: 172-180.
    • (2001) Mar Biotech , vol.3 , pp. 172-180
    • Bonnal, C.1    Raynaud, F.2    Astier, F.3    Lebart, M.C.4    Marcilhac, A.5
  • 29
    • 0038010444 scopus 로고    scopus 로고
    • Organoleptic and volatile aroma compounds comparison of wild and cultured gilthead sea bream: sensory differences and possible chemical basis
    • Grigorakis K, Taylor KDA, Alexis MN, (2003) Organoleptic and volatile aroma compounds comparison of wild and cultured gilthead sea bream: sensory differences and possible chemical basis. Aquaculture 225: 109-119.
    • (2003) Aquaculture , vol.225 , pp. 109-119
    • Grigorakis, K.1    Taylor, K.D.A.2    Alexis, M.N.3
  • 30
    • 78650299368 scopus 로고    scopus 로고
    • Quality differences of gilthead sea bream from distinct production systems in Southern Europe: Intensive, integrated, semi-intensive or extensive systems
    • Valente LMP, Cornet J, Donnay-Moreno C, Gouygou JP, Bergé JP, et al. (2011) Quality differences of gilthead sea bream from distinct production systems in Southern Europe: Intensive, integrated, semi-intensive or extensive systems. Food Control 22: 708-717.
    • (2011) Food Control , vol.22 , pp. 708-717
    • Valente, L.M.P.1    Cornet, J.2    Donnay-Moreno, C.3    Gouygou, J.P.4    Bergé, J.P.5
  • 31
    • 34248663955 scopus 로고    scopus 로고
    • The single-step method of RNA isolation by acid guanidinium thiucyanate-phenol-chloroform extraction: twenty-something years on
    • Chomczynski P, Sacchi N, (2006) The single-step method of RNA isolation by acid guanidinium thiucyanate-phenol-chloroform extraction: twenty-something years on. Nat Protoc 1: 581-585.
    • (2006) Nat Protoc , vol.1 , pp. 581-585
    • Chomczynski, P.1    Sacchi, N.2
  • 32
    • 84860790588 scopus 로고    scopus 로고
    • Fast skeletal muscle transcriptome of the gilthead sea bream (Sparus aurata) determined by next generation sequencing
    • García de la Serrana D, Estevez A, Andree K, Johnston IA, (2012) Fast skeletal muscle transcriptome of the gilthead sea bream (Sparus aurata) determined by next generation sequencing. BMC Genomics 13: 181.
    • (2012) BMC Genomics , vol.13 , pp. 181
    • García de la Serrana, D.1    Estevez, A.2    Andree, K.3    Johnston, I.A.4
  • 33
    • 0035710746 scopus 로고    scopus 로고
    • Analysis of relative gene expression data using realtime quantitative PCR and the 2(-delta delta C(T)) method
    • Livak KJ, Schmittgen TD, (2001) Analysis of relative gene expression data using realtime quantitative PCR and the 2(-delta delta C(T)) method. Methods 25: 402-408.
    • (2001) Methods , vol.25 , pp. 402-408
    • Livak, K.J.1    Schmittgen, T.D.2
  • 34
    • 0347752388 scopus 로고    scopus 로고
    • GeneNote: whole genome expression profiles in normal human tissues
    • Shmueli O, Horn-Saban S, Chalifa-Caspi V, Shmoish M, Ophir R, et al. (2003) GeneNote: whole genome expression profiles in normal human tissues. C R Biol 326: 1067-1072.
    • (2003) C R Biol , vol.326 , pp. 1067-1072
    • Shmueli, O.1    Horn-Saban, S.2    Chalifa-Caspi, V.3    Shmoish, M.4    Ophir, R.5
  • 35
    • 0032972509 scopus 로고    scopus 로고
    • PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization
    • Nakai K, Horton P, (1999) PSORT: A program for detecting sorting signals in proteins and predicting their subcellular localization. Trends Biochem Sci 24: 34-35.
    • (1999) Trends Biochem Sci , vol.24 , pp. 34-35
    • Nakai, K.1    Horton, P.2
  • 36
    • 0032077533 scopus 로고    scopus 로고
    • Using neural networks for prediction of the subcellular location of proteins
    • Reinhardt A, Hubbard T, (1998) Using neural networks for prediction of the subcellular location of proteins. Nucl Acids Res 26: 2230-2236.
    • (1998) Nucl Acids Res , vol.26 , pp. 2230-2236
    • Reinhardt, A.1    Hubbard, T.2
  • 37
    • 0032783288 scopus 로고    scopus 로고
    • The evolution of the calpain family as reflected in paralogous chromosome regions
    • Jékely G, Friedrich P, (1999) The evolution of the calpain family as reflected in paralogous chromosome regions. J Mol Evol 49: 272-281.
    • (1999) J Mol Evol , vol.49 , pp. 272-281
    • Jékely, G.1    Friedrich, P.2
  • 38
    • 79957613599 scopus 로고    scopus 로고
    • MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods
    • Tamura K, Peterson D, Peterson N, Stecher G, Nei M, et al. (2011) MEGA5: molecular evolutionary genetics analysis using maximum likelihood, evolutionary distance, and maximum parsimony methods. Mol Biol Evol 28: 2731-2739.
    • (2011) Mol Biol Evol , vol.28 , pp. 2731-2739
    • Tamura, K.1    Peterson, D.2    Peterson, N.3    Stecher, G.4    Nei, M.5
  • 39
    • 0026691182 scopus 로고
    • The rapid generation of mutation data matrices from protein sequences
    • Jones DT, Taylor WR, Thornton JM, (1992) The rapid generation of mutation data matrices from protein sequences. Comput Appl Biosci 8: 275-282.
    • (1992) Comput Appl Biosci , vol.8 , pp. 275-282
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 40
    • 0000461280 scopus 로고
    • Confidence limits on phylogenies: An approach using the bootstrap
    • Felsenstein J, (1985) Confidence limits on phylogenies: An approach using the bootstrap. Evolution 39: 783-791.
    • (1985) Evolution , vol.39 , pp. 783-791
    • Felsenstein, J.1
  • 41
    • 0024369426 scopus 로고
    • Molecular cloning of a novel mammalian calcium dependent protease distinc from m- and μ-types. Specific expression of the mRNA in skeletal muscle
    • Sorimachi H, Imajoh-Ohmi S, Emori Y, Kawasaki H, Ohno S, et al. (1989) Molecular cloning of a novel mammalian calcium dependent protease distinc from m- and μ-types. Specific expression of the mRNA in skeletal muscle. J Biol Chem 264: 20106-20111.
    • (1989) J Biol Chem , vol.264 , pp. 20106-20111
    • Sorimachi, H.1    Imajoh-Ohmi, S.2    Emori, Y.3    Kawasaki, H.4    Ohno, S.5
  • 43
    • 9944265039 scopus 로고    scopus 로고
    • Cloning of the calpain regulatory subunit cDNA from fish reveals divergent domain-v
    • Salem M, Nath J, Killefer J, (2004) Cloning of the calpain regulatory subunit cDNA from fish reveals divergent domain-v. Anim Biotechnol 15: 145-157.
    • (2004) Anim Biotechnol , vol.15 , pp. 145-157
    • Salem, M.1    Nath, J.2    Killefer, J.3
  • 44
    • 0023009016 scopus 로고
    • Isolation and sequence analysis of cDNA clones for the small subunit of rabbit calcium-dependent protease
    • Emori Y, Kawasaki H, Imajoh S, Kawashima S, Suzuki K, (1986) Isolation and sequence analysis of cDNA clones for the small subunit of rabbit calcium-dependent protease. J Biol Chem 261: 9472-9476.
    • (1986) J Biol Chem , vol.261 , pp. 9472-9476
    • Emori, Y.1    Kawasaki, H.2    Imajoh, S.3    Kawashima, S.4    Suzuki, K.5
  • 45
    • 56949085969 scopus 로고    scopus 로고
    • Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance
    • Beckmann JS, Spencer M, (2008) Calpain 3, the "gatekeeper" of proper sarcomere assembly, turnover and maintenance. Neuromuscul Disord 18: 913-921.
    • (2008) Neuromuscul Disord , vol.18 , pp. 913-921
    • Beckmann, J.S.1    Spencer, M.2
  • 46
    • 77957073280 scopus 로고
    • Fasting and starvation
    • In: Hochachka PW, Mommsen TP editors, Elsevier Science BV
    • Navarro I, Gutierrez J (1995) Fasting and starvation. In: Hochachka PW, Mommsen TP editors. Biochemistry and Molecular Biology of Fishes, vol. 4. Elsevier Science BV. pp. 393-434.
    • (1995) Biochemistry and Molecular Biology of Fishes , vol.4 , pp. 393-434
    • Navarro, I.1    Gutierrez, J.2
  • 47
    • 0036451733 scopus 로고    scopus 로고
    • Ubiquitin-proteasome-dependent proteolysis in rainbow trout (Oncorhynchus mykiss): effect of food deprivation
    • Martin SAM, Blaney S, Bowman AS, Houlihan DF, (2002) Ubiquitin-proteasome-dependent proteolysis in rainbow trout (Oncorhynchus mykiss): effect of food deprivation. Eur. J. Physiol. 445: 257-266.
    • (2002) Eur. J. Physiol , vol.445 , pp. 257-266
    • Martin, S.A.M.1    Blaney, S.2    Bowman, A.S.3    Houlihan, D.F.4
  • 48
    • 84858343023 scopus 로고    scopus 로고
    • Effects of feeding level and sexual maturation on carcass and fillet characteristics and indices of protein degradation in rainbow trout (Oncorhynchus mykiss)
    • Cleveland BM, Kenney PB, Manor ML, Weber GM, (2012) Effects of feeding level and sexual maturation on carcass and fillet characteristics and indices of protein degradation in rainbow trout (Oncorhynchus mykiss). Aquaculture 338-341: 228-236.
    • (2012) Aquaculture , vol.338-341 , pp. 228-236
    • Cleveland, B.M.1    Kenney, P.B.2    Manor, M.L.3    Weber, G.M.4
  • 49
    • 84871291743 scopus 로고    scopus 로고
    • Development temperature has persistent effects on muscle growth responses in gilthead sea bream
    • García de la serrana D, Vieira VLA, Andree KB, Darias M, Estévez A, et al. (2012) Development temperature has persistent effects on muscle growth responses in gilthead sea bream. PLoS ONE 7: e51884.
    • (2012) PLoS ONE , vol.7
    • García de la serrana, D.1    Vieira, V.L.A.2    Andree, K.B.3    Darias, M.4    Estévez, A.5
  • 50
    • 84870367058 scopus 로고    scopus 로고
    • Dietary carbohydrate utilization by European sea bass (Dicentrarchus labrax L.) and gilthead sea bream (Sparus aurata L.) juveniles
    • Enes P, Panserat S, Kaushik S, Oliva-Teles A, (2011) Dietary carbohydrate utilization by European sea bass (Dicentrarchus labrax L.) and gilthead sea bream (Sparus aurata L.) juveniles. Rev Fish Sci 19: 201-215.
    • (2011) Rev Fish Sci , vol.19 , pp. 201-215
    • Enes, P.1    Panserat, S.2    Kaushik, S.3    Oliva-Teles, A.4
  • 53
    • 33749402662 scopus 로고    scopus 로고
    • Micro-calpain is essential for postmortem proteolysis of muscle proteins
    • Geesink GH, Kuchay S, Chishti AH, Koohmaraie M, (2006) Micro-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
  • 54
    • 0000805516 scopus 로고
    • Effect of post-mortem storage on Ca2+-dependent proteases, their inhibitor and myofibril fragmentation
    • Koohmaraie M, Seideman CS, Schollmeyer JE, Dutson TR, Course JD, (1987) Effect of post-mortem storage on Ca2+-dependent proteases, their inhibitor and myofibril fragmentation. Meat Sci 19: 187-196.
    • (1987) Meat Sci , vol.19 , pp. 187-196
    • Koohmaraie, M.1    Seideman, C.S.2    Schollmeyer, J.E.3    Dutson, T.R.4    Course, J.D.5
  • 55
    • 0034868743 scopus 로고    scopus 로고
    • Effect of preslaughter feed withdrawal period on longissimus tenderness and the expression of calpains in the ovine
    • Ilian MA, Morton JD, Bekhit AE-D, Roberts N, Palmer B, et al. (2001) Effect of preslaughter feed withdrawal period on longissimus tenderness and the expression of calpains in the ovine. J Agric Food Chem 49: 1990-1998.
    • (2001) J Agric Food Chem , vol.49 , pp. 1990-1998
    • Ilian, M.A.1    Morton, J.D.2    Bekhit, A.E.-D.3    Roberts, N.4    Palmer, B.5
  • 56
    • 0038518444 scopus 로고    scopus 로고
    • Evaluation of single-nucleotide polymorphisms in CAPN1 for association with meat tenderness in cattle
    • Page BT, Casas E, Heaton MP, Cullen NG, Hyndman DL, et al. (2002) Evaluation of single-nucleotide polymorphisms in CAPN1 for association with meat tenderness in cattle. J Anim Sci 80: 3077-3085.
    • (2002) J Anim Sci , vol.80 , pp. 3077-3085
    • Page, B.T.1    Casas, E.2    Heaton, M.P.3    Cullen, N.G.4    Hyndman, D.L.5
  • 57
    • 33745690923 scopus 로고    scopus 로고
    • Effects of calpastatin and micro-calpain markers in beef cattle on tenderness traits
    • Casas E, White SN, Wheeler TL, Shackelford SD, Koohmaraie M, et al. (2006) Effects of calpastatin and micro-calpain markers in beef cattle on tenderness traits. J Anim Sci 84: 520-525.
    • (2006) J Anim Sci , vol.84 , pp. 520-525
    • Casas, E.1    White, S.N.2    Wheeler, T.L.3    Shackelford, S.D.4    Koohmaraie, M.5
  • 59
    • 0033089932 scopus 로고    scopus 로고
    • Relationship between skeletal muscle-specific calpain and tenderness of conditioned porcine longissimus muscle
    • Parr T, Sensky PL, Scothern GP, Bardsley RG, Buttery PJ, et al. (1999) Relationship between skeletal muscle-specific calpain and tenderness of conditioned porcine longissimus muscle. J Anim Sci 77: 661-668.
    • (1999) J Anim Sci , vol.77 , pp. 661-668
    • Parr, T.1    Sensky, P.L.2    Scothern, G.P.3    Bardsley, R.G.4    Buttery, P.J.5
  • 60
    • 0035218640 scopus 로고    scopus 로고
    • Intermuscular variations in tenderness: Association with the ubiquitous and muscle-specific calpains
    • Ilian M, Morton JD, Kent MP, Le Couteur CE, Hickford J, et al. (2001) Intermuscular variations in tenderness: Association with the ubiquitous and muscle-specific calpains. J Anim Sci 79: 122-132.
    • (2001) J Anim Sci , vol.79 , pp. 122-132
    • Ilian, M.1    Morton, J.D.2    Kent, M.P.3    Le Couteur, C.E.4    Hickford, J.5
  • 61
    • 1242326458 scopus 로고    scopus 로고
    • Possible regulation of the conventional calpain system by skeletal muscle-specific calpain, p94/calpain 3
    • Ono Y, Kakinuma K, Torii F, Irie A, Nakagawa K, et al. (2004) Possible regulation of the conventional calpain system by skeletal muscle-specific calpain, p94/calpain 3. J Biol Chem 23: 2761-2771.
    • (2004) J Biol Chem , vol.23 , pp. 2761-2771
    • Ono, Y.1    Kakinuma, K.2    Torii, F.3    Irie, A.4    Nakagawa, K.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.