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Volumn 75, Issue 4, 2004, Pages 353-360

Myofibrillar proteolysis in chick muscle cell cultures during heat stress

Author keywords

Chick myotubes; Heat stress; Myofibrillar proteolysis; Proteasome; Protein oxidation

Indexed keywords

GALLUS GALLUS;

EID: 4444279852     PISSN: 13443941     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1740-0929.2004.00197.x     Document Type: Article
Times cited : (8)

References (51)
  • 3
    • 1642576105 scopus 로고
    • Cathepsin D and other carboxyl protease
    • Dingle JT (ed.), Academic Press, Amsterdam
    • Barrett AJ, Kirschke H. 1977. Cathepsin D and other carboxyl protease. In: Dingle JT (ed.), A Laboratory Handbook, pp. 19-147. Academic Press, Amsterdam.
    • (1977) A Laboratory Handbook , pp. 19-147
    • Barrett, A.J.1    Kirschke, H.2
  • 4
    • 0019765848 scopus 로고
    • Cathepsin B, cathepsin H, and cathepsin L.
    • Barrett AJ, Kirschke H. 1981. Cathepsin B, cathepsin H, and cathepsin L. Methods in Enzymology 80, 535-561.
    • (1981) Methods in Enzymology , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 6
    • 0023655369 scopus 로고
    • Protein damage and degradation by oxygen radicals. I. General aspects
    • Davies KJ. 1987. Protein damage and degradation by oxygen radicals. I. General aspects. Journal of Biological Chemistry 262, 9895-9901.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 9895-9901
    • Davies, K.J.1
  • 7
    • 0027276072 scopus 로고
    • Protein modification by oxidants and the role of proteolytic enzymes
    • Davies KJ. 1993. Protein modification by oxidants and the role of proteolytic enzymes. Biochemical Society of Transactions 21, 346-353.
    • (1993) Biochemical Society of Transactions , vol.21 , pp. 346-353
    • Davies, K.J.1
  • 8
    • 0023655407 scopus 로고
    • Protein damage and degradation by oxygen radicals. II. Modification of amino acids
    • Davies KJ, Delsignore ME, Lin SW. 1987. Protein damage and degradation by oxygen radicals. II. Modification of amino acids. Journal of Biological Chemistry 262, 9902-9907.
    • (1987) Journal of Biological Chemistry , vol.262 , pp. 9902-9907
    • Davies, K.J.1    Delsignore, M.E.2    Lin, S.W.3
  • 9
    • 0025287267 scopus 로고
    • Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy
    • Furuno K, Goodman MN, Goldberg AL. 1990. Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy. Journal of Biological Chemistry 265, 8550-8557.
    • (1990) Journal of Biological Chemistry , vol.265 , pp. 8550-8557
    • Furuno, K.1    Goodman, M.N.2    Goldberg, A.L.3
  • 10
    • 0028245961 scopus 로고
    • Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin by the multicatalytic proteinase complex, proteasome
    • Giulivi C, Pacifici RE, Davies KJ. 1994. Exposure of hydrophobic moieties promotes the selective degradation of hydrogen peroxide-modified hemoglobin by the multicatalytic proteinase complex, proteasome. Archives of Biochemistry Biophysics 311, 329-341.
    • (1994) Archives of Biochemistry Biophysics , vol.311 , pp. 329-341
    • Giulivi, C.1    Pacifici, R.E.2    Davies, K.J.3
  • 11
  • 13
    • 0037030584 scopus 로고    scopus 로고
    • Induction of protein catabolism and the ubiquitin-proteasome pathway by mild oxidative stress
    • Gomes-Marcondes MC, Tisdale MJ. 2002. Induction of protein catabolism and the ubiquitin-proteasome pathway by mild oxidative stress. Cancer Letter 180, 69-74.
    • (2002) Cancer Letter , vol.180 , pp. 69-74
    • Gomes-Marcondes, M.C.1    Tisdale, M.J.2
  • 15
    • 0026029255 scopus 로고
    • Myofibrillar proteinase, cathepsin B, and protein breakdown rates in skeletal muscle from septic rats
    • Hall-Angeras M, Hasselgren PO, Dimlich RV, Fischer JE. 1991. Myofibrillar proteinase, cathepsin B, and protein breakdown rates in skeletal muscle from septic rats. Metabolism 40, 302-306.
    • (1991) Metabolism , vol.40 , pp. 302-306
    • Hall-Angeras, M.1    Hasselgren, P.O.2    Dimlich, R.V.3    Fischer, J.E.4
  • 17
    • 4444314163 scopus 로고
    • Effect of short-term exposure to heat or cold on muscle protein breakdown in rats
    • Hayashi K, Hino M, Tomita Y. 1993. Effect of short-term exposure to heat or cold on muscle protein breakdown in rats. Animal Science Technology (Japan) 64, 101-106.
    • (1993) Animal Science Technology (Japan) , vol.64 , pp. 101-106
    • Hayashi, K.1    Hino, M.2    Tomita, Y.3
  • 18
    • 0343765502 scopus 로고
    • Effect of dietary thyroxine on muscle protein metabolism and abdominal fat content in broiler chicken in hot and moderate environments
    • Hayashi K, Kukita S, Mukai M, Toyomizu M, Tomita Y. 1990. Effect of dietary thyroxine on muscle protein metabolism and abdominal fat content in broiler chicken in hot and moderate environments. Japanese Zootechnological Sciences 61, 1107-1112.
    • (1990) Japanese Zootechnological Sciences , vol.61 , pp. 1107-1112
    • Hayashi, K.1    Kukita, S.2    Mukai, M.3    Toyomizu, M.4    Tomita, Y.5
  • 20
    • 0028899142 scopus 로고
    • Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures
    • Hong DH, Forsberg NE. 1995. Effects of dexamethasone on protein degradation and protease gene expression in rat L8 myotube cultures. Molecular Cellular Endocrinology 108, 199-209.
    • (1995) Molecular Cellular Endocrinology , vol.108 , pp. 199-209
    • Hong, D.H.1    Forsberg, N.E.2
  • 21
  • 24
    • 0020688213 scopus 로고
    • Structures and functions of lysosomal thiol proteinases and their endogenous inhibitor
    • Katunuma N, Kominami E. 1983. Structures and functions of lysosomal thiol proteinases and their endogenous inhibitor. Current Topics Cellular Regulation 22, 71-101.
    • (1983) Current Topics Cellular Regulation , vol.22 , pp. 71-101
    • Katunuma, N.1    Kominami, E.2
  • 26
    • 0025857412 scopus 로고
    • Hyperthermia enhances the cytotoxic effects of reactive oxygen species to Chinese hamster cells and bovine endothelial cells in vitro
    • Lin PS, Quamo S, Ho KC, Gladding J. 1991. Hyperthermia enhances the cytotoxic effects of reactive oxygen species to Chinese hamster cells and bovine endothelial cells in vitro. Radiation Research 126, 43-51.
    • (1991) Radiation Research , vol.126 , pp. 43-51
    • Lin, P.S.1    Quamo, S.2    Ho, K.C.3    Gladding, J.4
  • 27
    • 0033558786 scopus 로고    scopus 로고
    • Enhancement of cytotoxicity of hydrogen peroxide by hyperthermia in Chinese hamster ovary cells: Role of antioxidant defenses
    • Lord-Fontaine S, Averill DA. 1999. Enhancement of cytotoxicity of hydrogen peroxide by hyperthermia in Chinese hamster ovary cells: role of antioxidant defenses. Archives of Biochemistry and Biophysics 363, 283-295.
    • (1999) Archives of Biochemistry and Biophysics , vol.363 , pp. 283-295
    • Lord-Fontaine, S.1    Averill, D.A.2
  • 28
    • 0022479243 scopus 로고
    • Evidence that lysosomes are not involved in the degradation of myofibrillar proteins in rat skeletal muscle
    • Lowell BB, Ruderman NB, Goodman MN. 1986. Evidence that lysosomes are not involved in the degradation of myofibrillar proteins in rat skeletal muscle. Biochemical Journal 234, 237-240.
    • (1986) Biochemical Journal , vol.234 , pp. 237-240
    • Lowell, B.B.1    Ruderman, N.B.2    Goodman, M.N.3
  • 30
    • 0034063282 scopus 로고    scopus 로고
    • Hyperthermia stimulates energy-proteasome-dependent protein degradation in cultured myotubes
    • Luo GJ, Sun X, Hasselgren PO. 2000. Hyperthermia stimulates energy-proteasome-dependent protein degradation in cultured myotubes. American Journal of Physiology 278, R749-R756.
    • (2000) American Journal of Physiology , vol.278
    • Luo, G.J.1    Sun, X.2    Hasselgren, P.O.3
  • 32
    • 0024370492 scopus 로고
    • Oxidation state of tissue thiol groups and content of protein carbonyl groups in chickens with inherited muscular dystrophy
    • Murphy ME, Kehrer JP. 1989. Oxidation state of tissue thiol groups and content of protein carbonyl groups in chickens with inherited muscular dystrophy. Biochemical Journal 260, 359-364.
    • (1989) Biochemical Journal , vol.260 , pp. 359-364
    • Murphy, M.E.1    Kehrer, J.P.2
  • 35
    • 0032552928 scopus 로고    scopus 로고
    • Comparison of the effects of thyroxine and triiodothyronine on protein turnover and apoptosis in primary chick muscle cell cultures
    • Nakashima K, Ohtsuka A, Hayashi K. 1998. Comparison of the effects of thyroxine and triiodothyronine on protein turnover and apoptosis in primary chick muscle cell cultures. Biochemical Biophysical Research Communications 251, 442-448.
    • (1998) Biochemical Biophysical Research Communications , vol.251 , pp. 442-448
    • Nakashima, K.1    Ohtsuka, A.2    Hayashi, K.3
  • 36
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • Ohkawa H, Ohishi N, Yagi K. 1979. Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Analytical Biochemistry 95, 351-358.
    • (1979) Analytical Biochemistry , vol.95 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 37
    • 0029999597 scopus 로고    scopus 로고
    • Iron-induced tissue damage and cancer: The role of reactive oxygen species-free radicals
    • Okada S. 1996. Iron-induced tissue damage and cancer: the role of reactive oxygen species-free radicals. Pathology International 46, 311-332.
    • (1996) Pathology International , vol.46 , pp. 311-332
    • Okada, S.1
  • 38
    • 0027324284 scopus 로고
    • Hydrophobicity as the signal for selective degradation of hydroxyl radical-modified hemoglobin by the multicatalytic proteinase complex, proteasome
    • Pacifici RE, Kono Y, Davies KJ. 1993. Hydrophobicity as the signal for selective degradation of hydroxyl radical-modified hemoglobin by the multicatalytic proteinase complex, proteasome. Journal of Biological Chemistry 268, 15405-15411.
    • (1993) Journal of Biological Chemistry , vol.268 , pp. 15405-15411
    • Pacifici, R.E.1    Kono, Y.2    Davies, K.J.3
  • 39
    • 0021683468 scopus 로고
    • Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates
    • Sasaki T, Kikuchi T, Yumoto N, Yoshimura N, Murachi T. 1984. Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates. Journal of Biological Chemistry 259, 12489-12494.
    • (1984) Journal of Biological Chemistry , vol.259 , pp. 12489-12494
    • Sasaki, T.1    Kikuchi, T.2    Yumoto, N.3    Yoshimura, N.4    Murachi, T.5
  • 40
    • 0028905549 scopus 로고
    • Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells
    • Shang F, Taylor A. 1995. Oxidative stress and recovery from oxidative stress are associated with altered ubiquitin conjugating and proteolytic activities in bovine lens epithelial cells. Biochemical Journal 307, 297-303.
    • (1995) Biochemical Journal , vol.307 , pp. 297-303
    • Shang, F.1    Taylor, A.2
  • 41
    • 0029956781 scopus 로고    scopus 로고
    • Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts
    • Solomon V, Goldberg AL. 1996. Importance of the ATP-ubiquitin-proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. Journal of Biological Chemistry 271, 26690-26697.
    • (1996) Journal of Biological Chemistry , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 42
    • 0023235667 scopus 로고
    • Hydrogen peroxide or heat shock induces resistance to hydrogen peroxide in Chinese hamster fibroblasts
    • Spitz DR, Dewey WC, Li GC. 1987. Hydrogen peroxide or heat shock induces resistance to hydrogen peroxide in Chinese hamster fibroblasts. Journal of Cellular Physiology 131, 364-373.
    • (1987) Journal of Cellular Physiology , vol.131 , pp. 364-373
    • Spitz, D.R.1    Dewey, W.C.2    Li, G.C.3
  • 43
    • 0025301715 scopus 로고
    • Covalent modification reactions are marking steps in protein turnover
    • Stadtman ER. 1990. Covalent modification reactions are marking steps in protein turnover. Biochemistry 29, 6323-6331.
    • (1990) Biochemistry , vol.29 , pp. 6323-6331
    • Stadtman, E.R.1
  • 44
    • 0025911829 scopus 로고
    • Metal-catalyzed oxidation of proteins. Physiological consequences
    • Stadtman ER, Oliver CN. 1991. Metal-catalyzed oxidation of proteins. Physiological consequences. Journal of Biological Chemistry 266, 2005-2008.
    • (1991) Journal of Biological Chemistry , vol.266 , pp. 2005-2008
    • Stadtman, E.R.1    Oliver, C.N.2
  • 45
    • 0023009780 scopus 로고
    • A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution
    • Tanaka K, Ii K, Ichihara A, Waxman L, Goldberg AL. 1986. A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution. Journal of Biological Chemistry 261, 15197-15203.
    • (1986) Journal of Biological Chemistry , vol.261 , pp. 15197-15203
    • Tanaka, K.1    Ii, K.2    Ichihara, A.3    Waxman, L.4    Goldberg, A.L.5
  • 46
    • 0015910804 scopus 로고
    • Lipid peroxidation damage to cell components
    • Tappel AL. 1973. Lipid peroxidation damage to cell components. Federation Proceedings 32, 1870-1874.
    • (1973) Federation Proceedings , vol.32 , pp. 1870-1874
    • Tappel, A.L.1
  • 49
    • 0019313444 scopus 로고
    • A rapid, sensitive method for the determination of 3-methylhistidine levels in urine and plasma using high-pressure liquid chromatography
    • Wassner SJ, Schlitzer JL, Li JB. 1980. A rapid, sensitive method for the determination of 3-methylhistidine levels in urine and plasma using high-pressure liquid chromatography. Analytical Biochemistry 104, 284-289.
    • (1980) Analytical Biochemistry , vol.104 , pp. 284-289
    • Wassner, S.J.1    Schlitzer, J.L.2    Li, J.B.3
  • 50
    • 0015501113 scopus 로고
    • Metabolism of administered 3-methylhistidine. Lack of muscle transfer ribonucleic acid charging and quantitative excretion as 3-methylhistidine and its N-acetyl derivative
    • Young VR, Alexis SD, Baliga BS, Munro HN, Muecke W. 1972. Metabolism of administered 3-methylhistidine. Lack of muscle transfer ribonucleic acid charging and quantitative excretion as 3-methylhistidine and its N-acetyl derivative. Journal of Biological Chemistry 247, 3592-3600.
    • (1972) Journal of Biological Chemistry , vol.247 , pp. 3592-3600
    • Young, V.R.1    Alexis, S.D.2    Baliga, B.S.3    Munro, H.N.4    Muecke, W.5
  • 51
    • 0030850797 scopus 로고    scopus 로고
    • Effect of environmental temperature on muscle protein turnover and heat production in tube-fed broiler chickens
    • Yunianto VD, Hayashi K, Kaneda S, Ohtsuka A, Tomita Y. 1997. Effect of environmental temperature on muscle protein turnover and heat production in tube-fed broiler chickens. British Journal of Nutrition 77, 897-909.
    • (1997) British Journal of Nutrition , vol.77 , pp. 897-909
    • Yunianto, V.D.1    Hayashi, K.2    Kaneda, S.3    Ohtsuka, A.4    Tomita, Y.5


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