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Volumn 87, Issue 3, 2011, Pages 165-174

Effects of camptothecin, etoposide and Ca2+ on caspase-3 activity and myofibrillar disruption of chicken during postmortem ageing

Author keywords

Ageing; Apoptosis; Ca2+; Camptothecin; Caspase 3; Etoposide

Indexed keywords

AGEING; APOPTOSIS; CA2+; CAMPTOTHECINS; CASPASE-3; ETOPOSIDE;

EID: 78649963628     PISSN: 03091740     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.meatsci.2010.10.002     Document Type: Article
Times cited : (70)

References (90)
  • 1
    • 0032531818 scopus 로고    scopus 로고
    • Calcium-A life and death signal
    • Berridge M.J., Bootman M.D., Lipp P. Calcium-A life and death signal. Nature 1998, 395(6703):645-648.
    • (1998) Nature , vol.395 , Issue.6703 , pp. 645-648
    • Berridge, M.J.1    Bootman, M.D.2    Lipp, P.3
  • 2
    • 0026489662 scopus 로고
    • Apoptotic cell death triggered by camptothecin or teniposide. The cell cycle specificity and effects of ionizing radiation
    • Bino G.D., Bruno S., Yi P.N., Darzynkiewicz Z. Apoptotic cell death triggered by camptothecin or teniposide. The cell cycle specificity and effects of ionizing radiation. Cell Proliferation 1992, 25(6):537-548.
    • (1992) Cell Proliferation , vol.25 , Issue.6 , pp. 537-548
    • Bino, G.D.1    Bruno, S.2    Yi, P.N.3    Darzynkiewicz, Z.4
  • 3
    • 0032152137 scopus 로고    scopus 로고
    • Changes in the calpains and calpastatin during postmortem storage of bovine muscle
    • Boehm M.L., Kendall T.L., Thompson V.F., Goll D.E. Changes in the calpains and calpastatin during postmortem storage of bovine muscle. Journal of Animal Science 1998, 76:2415-2434.
    • (1998) Journal of Animal Science , vol.76 , pp. 2415-2434
    • Boehm, M.L.1    Kendall, T.L.2    Thompson, V.F.3    Goll, D.E.4
  • 4
    • 38049108196 scopus 로고    scopus 로고
    • Effect of hydrodynamic pressure processing and aging on the tenderness and myofibrillar proteins of beef strip loins
    • Bowker B.C., Fahrenholz T.M., Paroczay E.W., Eastridge J.S., Solomon M.B. Effect of hydrodynamic pressure processing and aging on the tenderness and myofibrillar proteins of beef strip loins. Journal of Muscle Foods 2008, 19(1):74-97.
    • (2008) Journal of Muscle Foods , vol.19 , Issue.1 , pp. 74-97
    • Bowker, B.C.1    Fahrenholz, T.M.2    Paroczay, E.W.3    Eastridge, J.S.4    Solomon, M.B.5
  • 6
    • 76749106496 scopus 로고    scopus 로고
    • Arsenic trioxide induces the apoptosis in bone marrow mesenchymal stem cells by intracellular calcium signal and caspase-3 pathways
    • Cai B.-Z., Meng F.-Y., Zhu S.-L., Zhao J., Liu J.-Q., Liu C.-J., et al. Arsenic trioxide induces the apoptosis in bone marrow mesenchymal stem cells by intracellular calcium signal and caspase-3 pathways. Toxicology Letters 2010, 193(2):173-178.
    • (2010) Toxicology Letters , vol.193 , Issue.2 , pp. 173-178
    • Cai, B.-Z.1    Meng, F.-Y.2    Zhu, S.-L.3    Zhao, J.4    Liu, J.-Q.5    Liu, C.-J.6
  • 9
    • 0001383470 scopus 로고
    • Optimisation of tenderisation, ageing and tenderness
    • Dransfield E. Optimisation of tenderisation, ageing and tenderness. Meat Science 1994, 36(1-2):105-121.
    • (1994) Meat Science , vol.36 , Issue.1-2 , pp. 105-121
    • Dransfield, E.1
  • 11
    • 33947615372 scopus 로고    scopus 로고
    • Alterations in mRNA expression of apoptosis-related genes BCL2, BAX, FAS, Caspase-3, and the novel member BCL2L12 after treatment of human leukemic cell line HL60 with the antineoplastic agent etoposide
    • Annals Of The New York Academy Of Sciences
    • Floros K.V., Thomadaki H., Florou D., Talieri M., Scorilas A. Alterations in mRNA expression of apoptosis-related genes BCL2, BAX, FAS, Caspase-3, and the novel member BCL2L12 after treatment of human leukemic cell line HL60 with the antineoplastic agent etoposide. Signal Transduction Pathways, Part A: Apoptotic and Extracellular Signaling 2006, 1090:89-97.
    • (2006) Signal Transduction Pathways, Part A: Apoptotic and Extracellular Signaling , vol.1090 , pp. 89-97
    • Floros, K.V.1    Thomadaki, H.2    Florou, D.3    Talieri, M.4    Scorilas, A.5
  • 12
    • 0036133827 scopus 로고    scopus 로고
    • Meat tenderization by calcium chloride after osmotic dehydration
    • Gerelt B., Ikeuchi Y., Nishiumi T., Suzuki A. Meat tenderization by calcium chloride after osmotic dehydration. Meat Science 2002, 60(3):237-244.
    • (2002) Meat Science , vol.60 , Issue.3 , pp. 237-244
    • Gerelt, B.1    Ikeuchi, Y.2    Nishiumi, T.3    Suzuki, A.4
  • 13
    • 0031783728 scopus 로고    scopus 로고
    • DNA repair, cell cycle progression and cell death following camptothecin treatment in two murine lymphoma L5178Y sublines
    • Gradzka I., Skierski J., Szumiel I. DNA repair, cell cycle progression and cell death following camptothecin treatment in two murine lymphoma L5178Y sublines. Cell Biochemistry And Function 1998, 16(4):239-252.
    • (1998) Cell Biochemistry And Function , vol.16 , Issue.4 , pp. 239-252
    • Gradzka, I.1    Skierski, J.2    Szumiel, I.3
  • 18
    • 0028126638 scopus 로고
    • Identification of the 30kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T
    • Ho C.Y., Stromer M.H., Robson R.M. Identification of the 30kDa polypeptide in post mortem skeletal muscle as a degradation product of troponin-T. Biochimie 1994, 76(5):369-375.
    • (1994) Biochimie , vol.76 , Issue.5 , pp. 369-375
    • Ho, C.Y.1    Stromer, M.H.2    Robson, R.M.3
  • 19
    • 0036613820 scopus 로고    scopus 로고
    • The degradation of myofibrillar proteins in beef and lamb using denaturing electrophoresis-An overview
    • Hopkins D.L., Thompson J.M. The degradation of myofibrillar proteins in beef and lamb using denaturing electrophoresis-An overview. Journal of Muscle Foods 2002, 13(2):81-102.
    • (2002) Journal of Muscle Foods , vol.13 , Issue.2 , pp. 81-102
    • Hopkins, D.L.1    Thompson, J.M.2
  • 20
    • 60749113370 scopus 로고    scopus 로고
    • Influence of caspase3 selective inhibitor on proteolysis of chicken skeletal muscle proteins during post mortem aging
    • Huang M., Huang F., Xu X.L., Zhou G.H. Influence of caspase3 selective inhibitor on proteolysis of chicken skeletal muscle proteins during post mortem aging. Food Chemistry 2009, 115(1):181-186.
    • (2009) Food Chemistry , vol.115 , Issue.1 , pp. 181-186
    • Huang, M.1    Huang, F.2    Xu, X.L.3    Zhou, G.H.4
  • 21
    • 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., Mitsuhashi T., Beekman D.D., Parrish F.C., Olson D.G., Robson R.M. Proteolysis of specific muscle structural proteins by μ-calpain at low pH and temperature is similar to degradation in postmortem bovine muscle. Journal of Animal Science 1996, 74(5):993-1008.
    • (1996) Journal of Animal Science , vol.74 , Issue.5 , pp. 993-1008
    • Huff-Lonergan, E.1    Mitsuhashi, T.2    Beekman, D.D.3    Parrish, F.C.4    Olson, D.G.5    Robson, R.M.6
  • 22
    • 0035609543 scopus 로고    scopus 로고
    • Characterization of peptides released from rabbit skeletal muscle troponin-T by μ-calpain under conditions of low temperature and high ionic strength
    • Hughes M.C., Geary S., Dransfield E., McSweeney P.L.H., O'Neill E.E. Characterization of peptides released from rabbit skeletal muscle troponin-T by μ-calpain under conditions of low temperature and high ionic strength. Meat Science 2001, 59(1):61-69.
    • (2001) Meat Science , vol.59 , Issue.1 , pp. 61-69
    • Hughes, M.C.1    Geary, S.2    Dransfield, E.3    McSweeney, P.L.H.4    O'Neill, E.E.5
  • 23
    • 0142200878 scopus 로고    scopus 로고
    • Does the newly discovered calpain 10 play a role in meat tenderization during post-mortem storage?
    • Ilian M.A., Bekhit A.E.-D.A., Bickerstaffe R. Does the newly discovered calpain 10 play a role in meat tenderization during post-mortem storage?. Meat Science 2004, 66(2):317-327.
    • (2004) Meat Science , vol.66 , Issue.2 , pp. 317-327
    • Ilian, M.A.1    Bekhit, A.E.-D.A.2    Bickerstaffe, R.3
  • 24
    • 0142200869 scopus 로고    scopus 로고
    • The relationship between meat tenderization, myofibril fragmentation and autolysis of calpain 3 during post-mortem aging
    • Ilian M.A., Bekhit A.E.-D.A., Bickerstaffe R. The relationship between meat tenderization, myofibril fragmentation and autolysis of calpain 3 during post-mortem aging. Meat Science 2004, 66(2):387-397.
    • (2004) Meat Science , vol.66 , Issue.2 , pp. 387-397
    • Ilian, M.A.1    Bekhit, A.E.-D.A.2    Bickerstaffe, R.3
  • 25
    • 25844432267 scopus 로고    scopus 로고
    • Studies of the effect of hydrostatic pressure pretreatment on thermal gelation of chicken myofibrils and pork meat patty
    • Iwasaki T., Noshiroya K., Saitoh N., Okano K., Yamamoto K. Studies of the effect of hydrostatic pressure pretreatment on thermal gelation of chicken myofibrils and pork meat patty. Food Chemistry 2006, 95(3):474-483.
    • (2006) Food Chemistry , vol.95 , Issue.3 , pp. 474-483
    • Iwasaki, T.1    Noshiroya, K.2    Saitoh, N.3    Okano, K.4    Yamamoto, K.5
  • 26
    • 0032546795 scopus 로고    scopus 로고
    • Caspase-3 is required for α-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis
    • Jänicke R.U., Ng P., Sprengart M.L., Porter A.G. Caspase-3 is required for α-fodrin cleavage but dispensable for cleavage of other death substrates in apoptosis. Journal of Biological Chemistry 1998, 273(25):15540-15545.
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.25 , pp. 15540-15545
    • Jänicke, R.U.1    Ng, P.2    Sprengart, M.L.3    Porter, A.G.4
  • 27
    • 0029780802 scopus 로고    scopus 로고
    • The clinical pharmacology of etoposide: An update
    • Joel S. The clinical pharmacology of etoposide: An update. Cancer Treatment Reviews 1996, 22(3):179-221.
    • (1996) Cancer Treatment Reviews , vol.22 , Issue.3 , pp. 179-221
    • Joel, S.1
  • 28
    • 33749376502 scopus 로고    scopus 로고
    • Changes in caspase activity during the postmortem conditioning period and its relationship to shear force in porcine longissimus muscle
    • Kemp C.M., Bardsley R.G., Parr T. Changes in caspase activity during the postmortem conditioning period and its relationship to shear force in porcine longissimus muscle. Journal of Animal Science 2006, 84:2841-2846.
    • (2006) Journal of Animal Science , vol.84 , pp. 2841-2846
    • Kemp, C.M.1    Bardsley, R.G.2    Parr, T.3
  • 29
    • 46749084702 scopus 로고    scopus 로고
    • The effect of recombinant caspase 3 on myofibrillar proteins in porcine skeletal muscle
    • Kemp C.M., Parr T. The effect of recombinant caspase 3 on myofibrillar proteins in porcine skeletal muscle. Animal 2008, 2(08):1254-1264.
    • (2008) Animal , vol.2 , Issue.8 , pp. 1254-1264
    • Kemp, C.M.1    Parr, T.2
  • 30
    • 0037403232 scopus 로고    scopus 로고
    • Changes in structure of psoas major and minor and semitendinosus muscles of calves, heifers and cows during post-mortem ageing
    • Kolczak T., Pospiech E., Palka K., Lacki J. Changes in structure of psoas major and minor and semitendinosus muscles of calves, heifers and cows during post-mortem ageing. Meat Science 2003, 64(1):77-83.
    • (2003) Meat Science , vol.64 , Issue.1 , pp. 77-83
    • Kolczak, T.1    Pospiech, E.2    Palka, K.3    Lacki, J.4
  • 31
    • 0032732751 scopus 로고    scopus 로고
    • Thapsigargin enhances camptothecin-induced apoptosis in cardiomyocytes
    • Kong J.Y., Rabkin S.W. Thapsigargin enhances camptothecin-induced apoptosis in cardiomyocytes. Pharmacology & Toxicology 1999, 85(s1):212-220.
    • (1999) Pharmacology & Toxicology , vol.85 , Issue.S1 , pp. 212-220
    • Kong, J.Y.1    Rabkin, S.W.2
  • 32
    • 43049134457 scopus 로고    scopus 로고
    • Thermal effects on chicken and salmon muscles: Tenderness, cook loss, area shrinkage, collagen solubility and microstructure
    • Kong F., Tang J., Lin M., Rasco B. Thermal effects on chicken and salmon muscles: Tenderness, cook loss, area shrinkage, collagen solubility and microstructure. LWT-Food Science and Technology 2008, 41(7):1210-1222.
    • (2008) LWT-Food Science and Technology , vol.41 , Issue.7 , pp. 1210-1222
    • Kong, F.1    Tang, J.2    Lin, M.3    Rasco, B.4
  • 33
    • 0026591107 scopus 로고
    • 2+-dependent proteases (calpains) in post mortem proteolysis and meat tenderness
    • 2+-dependent proteases (calpains) in post mortem proteolysis and meat tenderness. Biochimie 1992, 74(3):239-245.
    • (1992) Biochimie , vol.74 , Issue.3 , pp. 239-245
    • Koohmaraie, M.1
  • 34
    • 0002514983 scopus 로고
    • Muscle proteinases and meat aging
    • Koohmaraie M. Muscle proteinases and meat aging. Meat Science 1994, 36(1-2):93-104.
    • (1994) Meat Science , vol.36 , Issue.1-2 , pp. 93-104
    • Koohmaraie, M.1
  • 35
    • 0030305245 scopus 로고    scopus 로고
    • Biochemical factors regulating the toughening and tenderization processes of meat
    • Koohmaraie M. Biochemical factors regulating the toughening and tenderization processes of meat. Meat Science 1996, 43(Supplement 1):193-201.
    • (1996) Meat Science , vol.43 , Issue.SUPPL. 1 , pp. 193-201
    • Koohmaraie, M.1
  • 37
    • 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., Geesink G.H. Contribution of postmortem muscle biochemistry to the delivery of consistent meat quality with particular focus on the calpain system. Meat Science 2006, 74(1):34-43.
    • (2006) Meat Science , vol.74 , Issue.1 , pp. 34-43
    • Koohmaraie, M.1    Geesink, G.H.2
  • 39
    • 55949091941 scopus 로고    scopus 로고
    • A novel calpain inhibitor, ((1S)-1((((1S)-1-benzyl-3-cyclopropylamino-2, 3-di-oxopropyl)amino)carbonyl)-3-methylbutyl) carbamic acid 5-methoxy-3-oxapentyl ester, protects neuronal cells from cerebral ischemia-induced damage in mice
    • Koumura A., Nonaka Y., Hyakkoku K., Oka T., Shimazawa M., Hozumi I., et al. A novel calpain inhibitor, ((1S)-1((((1S)-1-benzyl-3-cyclopropylamino-2, 3-di-oxopropyl)amino)carbonyl)-3-methylbutyl) carbamic acid 5-methoxy-3-oxapentyl ester, protects neuronal cells from cerebral ischemia-induced damage in mice. Neuroscience 2008, 157(2):309-318.
    • (2008) Neuroscience , vol.157 , Issue.2 , pp. 309-318
    • Koumura, A.1    Nonaka, Y.2    Hyakkoku, K.3    Oka, T.4    Shimazawa, M.5    Hozumi, I.6
  • 40
    • 0041355298 scopus 로고    scopus 로고
    • In situ investigation of the calcium-induced proteolytic and salting-in mechanisms causing tenderization in calcium-enhanced muscle
    • Lawrence T.E., Dikeman M.E., Stephens J.W., Obuz E., Davis J.R. In situ investigation of the calcium-induced proteolytic and salting-in mechanisms causing tenderization in calcium-enhanced muscle. Meat Science 2004, 66(1):69-75.
    • (2004) Meat Science , vol.66 , Issue.1 , pp. 69-75
    • Lawrence, T.E.1    Dikeman, M.E.2    Stephens, J.W.3    Obuz, E.4    Davis, J.R.5
  • 41
    • 69149091652 scopus 로고    scopus 로고
    • Inhibition of P-glycoprotein by wogonin is involved with the potentiation of etoposide-induced apoptosis in cancer cells
    • Annals Of The New York Academy Of Sciences
    • Lee E., Enomoto R., Koshiba C., Hirano H. Inhibition of P-glycoprotein by wogonin is involved with the potentiation of etoposide-induced apoptosis in cancer cells. Natural compounds and their role in apoptotic cell signaling pathways 2009, 1171:132-136.
    • (2009) Natural compounds and their role in apoptotic cell signaling pathways , vol.1171 , pp. 132-136
    • Lee, E.1    Enomoto, R.2    Koshiba, C.3    Hirano, H.4
  • 43
    • 0031706064 scopus 로고    scopus 로고
    • Camptothecin induces differentiation, tissue transglutaminase and apoptosis in cultured keratinocytes
    • Lin X.-r., Wilkinson D.I., Farber E.M. Camptothecin induces differentiation, tissue transglutaminase and apoptosis in cultured keratinocytes. Experimental Dermatology 1998, 7(4):179-183.
    • (1998) Experimental Dermatology , vol.7 , Issue.4 , pp. 179-183
    • Lin, X.-R.1    Wilkinson, D.I.2    Farber, E.M.3
  • 44
    • 0037163133 scopus 로고    scopus 로고
    • Calcium and calpain as key mediators of apoptosis-like death induced by vitamin D compounds in breast cancer cells
    • Mathiasen I.S., Sergeev I.N., Bastholm L., Elling F., Norman A.W., Jaattela M. Calcium and calpain as key mediators of apoptosis-like death induced by vitamin D compounds in breast cancer cells. Journal of Biological Chemistry 2002, 277(34):30738-30745.
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.34 , pp. 30738-30745
    • Mathiasen, I.S.1    Sergeev, I.N.2    Bastholm, L.3    Elling, F.4    Norman, A.W.5    Jaattela, M.6
  • 47
    • 0036019634 scopus 로고    scopus 로고
    • Contribution of major structural changes in myofibrils to rabbit meat tenderisation during ageing
    • Mestre Prates J.A., Garcia e Costa F.J.S., Ribeiro A.M.R., Dias Correia A.A. Contribution of major structural changes in myofibrils to rabbit meat tenderisation during ageing. Meat Science 2002, 61(1):103-113.
    • (2002) Meat Science , vol.61 , Issue.1 , pp. 103-113
    • Mestre Prates, J.A.1    Garcia e Costa, F.J.S.2    Ribeiro, A.M.R.3    Dias Correia, A.A.4
  • 49
    • 37749045821 scopus 로고    scopus 로고
    • Properties of refrigerated ground beef treated with potassium lactate and sodium diacetate
    • Miros, lstrok, Fik, a., Surówka, K., Bo, zdot, & Firek, e. (2008). Properties of refrigerated ground beef treated with potassium lactate and sodium diacetate. Journal of The Science Of Food And Agriculture, 88(1), 91-99.
    • (2008) Journal of The Science Of Food And Agriculture , vol.88 , Issue.1 , pp. 91-99
    • Miros1    lstrok2    Fik, A.3    Surówka, K.4    Bo, Z.5    Firek, E.6
  • 50
    • 31544474287 scopus 로고    scopus 로고
    • Acrolein produces nitric oxide through the elevation of intracellular calcium levels to induce apoptosis in human umbilical vein endothelial cells: Implications for smoke angiopathy
    • Misonou Y., Asahi M., Yokoe S., Miyoshi E., Taniguchi N. Acrolein produces nitric oxide through the elevation of intracellular calcium levels to induce apoptosis in human umbilical vein endothelial cells: Implications for smoke angiopathy. Nitric Oxide 2006, 14(2):180-187.
    • (2006) Nitric Oxide , vol.14 , Issue.2 , pp. 180-187
    • Misonou, Y.1    Asahi, M.2    Yokoe, S.3    Miyoshi, E.4    Taniguchi, N.5
  • 52
    • 0942300430 scopus 로고    scopus 로고
    • N-terminal amino acid sequences of troponin T fragments, including 30kDa one, produced during postmortem aging of bovine longissimus muscle
    • Muroya S., Kitamura S.-i., Tanabe S., Nishimura T., Nakajima I., Chikuni K. N-terminal amino acid sequences of troponin T fragments, including 30kDa one, produced during postmortem aging of bovine longissimus muscle. Meat Science 2004, 67(1):19-24.
    • (2004) Meat Science , vol.67 , Issue.1 , pp. 19-24
    • Muroya, S.1    Kitamura, S.-I.2    Tanabe, S.3    Nishimura, T.4    Nakajima, I.5    Chikuni, K.6
  • 53
    • 67349262992 scopus 로고    scopus 로고
    • A non-destructive method to monitor changes in a troponin T peptide in beef drip with a monoclonal antibody
    • Muroya S., Oe M., Nakajima I., Shibata M., Chikuni K. A non-destructive method to monitor changes in a troponin T peptide in beef drip with a monoclonal antibody. Meat Science 2009, 83(1):155-160.
    • (2009) Meat Science , vol.83 , Issue.1 , pp. 155-160
    • Muroya, S.1    Oe, M.2    Nakajima, I.3    Shibata, M.4    Chikuni, K.5
  • 56
    • 0034992876 scopus 로고    scopus 로고
    • D-galactosamine/lipopolysaccharide-induced fulminant hepatic failure resulting in reduction of lethality
    • D-galactosamine/lipopolysaccharide-induced fulminant hepatic failure resulting in reduction of lethality. Hepatology 2001, 33(6):1441-1450.
    • (2001) Hepatology , vol.33 , Issue.6 , pp. 1441-1450
    • Nakama, T.1    Hirono, S.2    Moriuchi, A.3    Hasuike, S.4    Nagata, K.5    Hori, T.6
  • 57
    • 0029854806 scopus 로고    scopus 로고
    • Non-erythroid α-spectrin breakdown by calpain and interleukin 1 β-converting-enzyme-like protease(s) in apoptotic cells: Contributory roles of both protease families in neuronal apoptosis
    • Nath R., Raser K.J., Stafford D., Hajimohammadreza I., Posner A., Allen H., et al. Non-erythroid α-spectrin breakdown by calpain and interleukin 1 β-converting-enzyme-like protease(s) in apoptotic cells: Contributory roles of both protease families in neuronal apoptosis. Biochemical Journal 1996, 319(3):683-690.
    • (1996) Biochemical Journal , vol.319 , Issue.3 , pp. 683-690
    • Nath, R.1    Raser, K.J.2    Stafford, D.3    Hajimohammadreza, I.4    Posner, A.5    Allen, H.6
  • 58
    • 0030306560 scopus 로고    scopus 로고
    • The origin of the 30kDa component appearing during post-mortem ageing of bovine muscle
    • Negishi H., Yamamoto E., Kuwata T. The origin of the 30kDa component appearing during post-mortem ageing of bovine muscle. Meat Science 1996, 42(3):289-303.
    • (1996) Meat Science , vol.42 , Issue.3 , pp. 289-303
    • Negishi, H.1    Yamamoto, E.2    Kuwata, T.3
  • 59
    • 0031977191 scopus 로고    scopus 로고
    • The role of calcium in apoptosis
    • Nicotera P., Orrenius S. The role of calcium in apoptosis. Cell Calcium 1998, 23(2-3):173-180.
    • (1998) Cell Calcium , vol.23 , Issue.2-3 , pp. 173-180
    • Nicotera, P.1    Orrenius, S.2
  • 60
    • 84985046283 scopus 로고
    • Effect of post-mortem storage and calcium activation factor on myofibrillar proteins of bovine skeletal muscle
    • Olsen D.G., Parrish F.C., Dayton W.R., Goll D.E. Effect of post-mortem storage and calcium activation factor on myofibrillar proteins of bovine skeletal muscle. Journal of Food Science 1977, 42(1):117-124.
    • (1977) Journal of Food Science , vol.42 , Issue.1 , pp. 117-124
    • Olsen, D.G.1    Parrish, F.C.2    Dayton, W.R.3    Goll, D.E.4
  • 63
    • 0000852182 scopus 로고
    • Relationship between toughness and troponin T in conditioned beef
    • Penny I.F., Dransfield E. Relationship between toughness and troponin T in conditioned beef. Meat Science 1979, 3(2):135-141.
    • (1979) Meat Science , vol.3 , Issue.2 , pp. 135-141
    • Penny, I.F.1    Dransfield, E.2
  • 65
    • 0032479912 scopus 로고    scopus 로고
    • Regional calpain and caspase-3 proteolysis of spectrin after traumatic brain injury
    • Pike B.R., Zhao X., Newcomb J.K., Posmantur R.M., Wang K.K., Hayes R.L. Regional calpain and caspase-3 proteolysis of spectrin after traumatic brain injury. Neuroreport 1998, 9(11):2437-2442.
    • (1998) Neuroreport , vol.9 , Issue.11 , pp. 2437-2442
    • Pike, B.R.1    Zhao, X.2    Newcomb, J.K.3    Posmantur, R.M.4    Wang, K.K.5    Hayes, R.L.6
  • 67
    • 0032190150 scopus 로고    scopus 로고
    • Calcium signalling and the regulation of apoptosis
    • Pörn-Ares M.I., Ares M.P.S., Orrenius S. Calcium signalling and the regulation of apoptosis. Toxicology in vitro 1998, 12(5):539-543.
    • (1998) Toxicology in vitro , vol.12 , Issue.5 , pp. 539-543
    • Pörn-Ares, M.I.1    Ares, M.P.S.2    Orrenius, S.3
  • 68
    • 0001174765 scopus 로고
    • Degradation of myofibrillar protein components during post-mortem aging of chicken muscle
    • Samejima K., Wolfe F.H. Degradation of myofibrillar protein components during post-mortem aging of chicken muscle. Journal of Food Science 1976, 41(2):250-254.
    • (1976) Journal of Food Science , vol.41 , Issue.2 , pp. 250-254
    • Samejima, K.1    Wolfe, F.H.2
  • 69
    • 0036986447 scopus 로고    scopus 로고
    • Role of muscle endopeptidases and their inhibitors in meat tenderness
    • Sentandreu M.A., Coulis G., Ouali A. Role of muscle endopeptidases and their inhibitors in meat tenderness. Trends In Food Science & Technology 2002, 13(12):400-421.
    • (2002) Trends In Food Science & Technology , vol.13 , Issue.12 , pp. 400-421
    • Sentandreu, M.A.1    Coulis, G.2    Ouali, A.3
  • 73
    • 0033213973 scopus 로고    scopus 로고
    • Caspase and calpain substrates: Roles in synaptic plasticity and cell death
    • Sic L.C., Mark P.M. Caspase and calpain substrates: Roles in synaptic plasticity and cell death. Journal of Neuroscience Research 1999, 58(1):167-190.
    • (1999) Journal of Neuroscience Research , vol.58 , Issue.1 , pp. 167-190
    • Sic, L.C.1    Mark, P.M.2
  • 74
    • 0031051736 scopus 로고    scopus 로고
    • Nuclear condensation and fragmentation following cerebral hypoxia-ischemia occurs more frequently in immature than older rats
    • Sidhu R.S., Tuor U.I., Del Bigio M.R. Nuclear condensation and fragmentation following cerebral hypoxia-ischemia occurs more frequently in immature than older rats. Neuroscience Letters 1997, 223(2):129-132.
    • (1997) Neuroscience Letters , vol.223 , Issue.2 , pp. 129-132
    • Sidhu, R.S.1    Tuor, U.I.2    Del Bigio, M.R.3
  • 75
    • 2642608660 scopus 로고    scopus 로고
    • Apoptotic response of spermatogenic cells to the germ cell mutagens etoposide, adriamycin, and diepoxybutane
    • Sjöblom T., West A., Lähdetie J. Apoptotic response of spermatogenic cells to the germ cell mutagens etoposide, adriamycin, and diepoxybutane. Environmental And Molecular Mutagenesis 1998, 31(2):133-148.
    • (1998) Environmental And Molecular Mutagenesis , vol.31 , Issue.2 , pp. 133-148
    • Sjöblom, T.1    West, A.2    Lähdetie, J.3
  • 79
    • 18644383484 scopus 로고    scopus 로고
    • A skeletal muscle troponin T specific ELISA based on the use of an antibody against the soluble troponin T (16-31) fragment
    • Tsitsilonis O.E., Stoeva S., Echner H., Balafas A., Margomenou L., Katsoulas H.L., et al. A skeletal muscle troponin T specific ELISA based on the use of an antibody against the soluble troponin T (16-31) fragment. Journal of Immunological Methods 2002, 268(2):141-148.
    • (2002) Journal of Immunological Methods , vol.268 , Issue.2 , pp. 141-148
    • Tsitsilonis, O.E.1    Stoeva, S.2    Echner, H.3    Balafas, A.4    Margomenou, L.5    Katsoulas, H.L.6
  • 80
    • 14744290129 scopus 로고    scopus 로고
    • Extracellular organic compounds from the ichthyotoxic red tide alga Heterosigma akashiwo elevate cytosolic calcium and induce apoptosis in Sf9 cells
    • Twiner M.J., Chidiac P., Dixon S.J., Trick C.G. Extracellular organic compounds from the ichthyotoxic red tide alga Heterosigma akashiwo elevate cytosolic calcium and induce apoptosis in Sf9 cells. Harmful Algae 2005, 4(4):789-800.
    • (2005) Harmful Algae , vol.4 , Issue.4 , pp. 789-800
    • Twiner, M.J.1    Chidiac, P.2    Dixon, S.J.3    Trick, C.G.4
  • 81
    • 42149127186 scopus 로고    scopus 로고
    • Caspase 3 is not likely involved in the postmortem tenderization of beef muscle
    • Underwood K.R., Means W.J., Du M. Caspase 3 is not likely involved in the postmortem tenderization of beef muscle. Journal of Animal Science 2008, 86:960-966.
    • (2008) Journal of Animal Science , vol.86 , pp. 960-966
    • Underwood, K.R.1    Means, W.J.2    Du, M.3
  • 83
    • 0348237070 scopus 로고    scopus 로고
    • Analytical tools for rapid, sensitive, quantitative identification of potential meat quality markers
    • Voelter W., Stoeva S., Echner H., Beck A., Schütz J., Lehmann R., et al. Analytical tools for rapid, sensitive, quantitative identification of potential meat quality markers. Journal für praktische Chemie 2000, 342(2):179-191.
    • (2000) Journal für praktische Chemie , vol.342 , Issue.2 , pp. 179-191
    • Voelter, W.1    Stoeva, S.2    Echner, H.3    Beck, A.4    Schütz, J.5    Lehmann, R.6
  • 84
    • 0033956278 scopus 로고    scopus 로고
    • Calpain and caspase: Can you tell the difference?
    • Wang K.K.W. Calpain and caspase: Can you tell the difference?. Trends In Neurosciences 2000, 23(1):20-26.
    • (2000) Trends In Neurosciences , vol.23 , Issue.1 , pp. 20-26
    • Wang, K.K.W.1
  • 86
    • 0027687749 scopus 로고
    • Effects of postmortem injection time, injection level, and concentration of calcium chloride on beef quality traits
    • Wheeler T.L., Koohmaraie M., Lansdell J.L., Siragusa G.R., Miller M.F. Effects of postmortem injection time, injection level, and concentration of calcium chloride on beef quality traits. Journal of Animal Science 1993, 71(11):2965-2974.
    • (1993) Journal of Animal Science , vol.71 , Issue.11 , pp. 2965-2974
    • Wheeler, T.L.1    Koohmaraie, M.2    Lansdell, J.L.3    Siragusa, G.R.4    Miller, M.F.5
  • 87
    • 0026825122 scopus 로고
    • Effects of lamb age, muscle type, and 24-hour activity of endogenous proteinases on postmortem proteolysis
    • Whipple G., Koohmaraie M. Effects of lamb age, muscle type, and 24-hour activity of endogenous proteinases on postmortem proteolysis. Journal of Animal Science 1992, 70:798-804.
    • (1992) Journal of Animal Science , vol.70 , pp. 798-804
    • Whipple, G.1    Koohmaraie, M.2
  • 88
    • 0011530627 scopus 로고
    • Calcium chloride marination effects on beef steak tenderness and calpain proteolytic activity
    • Whipple G., Koohmaraie M. Calcium chloride marination effects on beef steak tenderness and calpain proteolytic activity. Meat Science 1993, 33(2):265-275.
    • (1993) Meat Science , vol.33 , Issue.2 , pp. 265-275
    • Whipple, G.1    Koohmaraie, M.2
  • 89
    • 0025899138 scopus 로고
    • Programmed cell death: Apoptosis and oncogenesis
    • Williams G.T. Programmed cell death: Apoptosis and oncogenesis. Cell 1991, 65(7):1097-1098.
    • (1991) Cell , vol.65 , Issue.7 , pp. 1097-1098
    • Williams, G.T.1
  • 90
    • 0027525104 scopus 로고
    • The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme
    • Yuan J., Shaham S., Ledoux S., Ellis H.M., Horvitz H.R. The C. elegans cell death gene ced-3 encodes a protein similar to mammalian interleukin-1β-converting enzyme. Cell 1993, 75(4):641-652.
    • (1993) Cell , vol.75 , Issue.4 , pp. 641-652
    • Yuan, J.1    Shaham, S.2    Ledoux, S.3    Ellis, H.M.4    Horvitz, H.R.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.