메뉴 건너뛰기




Volumn 67, Issue 11, 2003, Pages 2455-2458

Effects of serum deprivation on myofibrillar proteolysis in chick myotube cultures

Author keywords

Calpain; Cathepsins; Myofibrillar proteolysis; Proteasome; Serum deprivation

Indexed keywords

GALLUS GALLUS;

EID: 3242879376     PISSN: 09168451     EISSN: None     Source Type: Journal    
DOI: 10.1271/bbb.67.2455     Document Type: Article
Times cited : (3)

References (27)
  • 1
    • 0018570404 scopus 로고
    • The effect of protease inhibitors and decreased temperature on the degradation of different classes of proteins in cultured hepatocytes
    • Neff, N. T., DeMartino, G. N., and Goldberg, A. L., The effect of protease inhibitors and decreased temperature on the degradation of different classes of proteins in cultured hepatocytes. J. Cell. Physiol., 101, 439-457 (1979).
    • (1979) J. Cell. Physiol. , vol.101 , pp. 439-457
    • Neff, N.T.1    DeMartino, G.N.2    Goldberg, A.L.3
  • 2
    • 0019790453 scopus 로고
    • Effect of dexamethasone, ammonium ions, and serum-deprivation on intracellular proteolysis in cultured muscle cells
    • Mayer, M., Chaouat, M., Hadar, R., Nissan, S., and Lernau, O. Z., Effect of dexamethasone, ammonium ions, and serum-deprivation on intracellular proteolysis in cultured muscle cells. J. Cell. Physiol., 109, 525-533 (1981).
    • (1981) J. Cell. Physiol. , vol.109 , pp. 525-533
    • Mayer, M.1    Chaouat, M.2    Hadar, R.3    Nissan, S.4    Lernau, O.Z.5
  • 3
    • 0021108041 scopus 로고
    • Hormone-responsive myofibrillar protease activity in cultured rat myoblasts
    • Mayer, M., Chaouat, M., Lernau, O. Z., and Nissan, S., Hormone-responsive myofibrillar protease activity in cultured rat myoblasts. FEBS Lett., 161, 239-242 (1983).
    • (1983) FEBS Lett. , vol.161 , pp. 239-242
    • Mayer, M.1    Chaouat, M.2    Lernau, O.Z.3    Nissan, S.4
  • 4
    • 0021191576 scopus 로고
    • The role of increased proteolysis in the atrophy and arrest of proliferation in serum-deprived fibroblasts
    • Gronostajski, R. M., Goldberg, A. L., and Pardee, A. B., The role of increased proteolysis in the atrophy and arrest of proliferation in serum-deprived fibroblasts. J. Cell. Physiol., 121, 189-198 (1984).
    • (1984) J. Cell. Physiol. , vol.121 , pp. 189-198
    • Gronostajski, R.M.1    Goldberg, A.L.2    Pardee, A.B.3
  • 5
    • 0021779755 scopus 로고
    • Effect of serum deprivation and replacement on proteolysis in cultured human fibroblasts
    • Berger, J. J., and Dice, J. F., Effect of serum deprivation and replacement on proteolysis in cultured human fibroblasts. Prog. Clin. Biol. Res., 180, 479-481 (1985).
    • (1985) Prog. Clin. Biol. Res. , vol.180 , pp. 479-481
    • Berger, J.J.1    Dice, J.F.2
  • 6
    • 0023002984 scopus 로고
    • Proteolysis in cultured cells during prolonged serum deprivation and replacement
    • Berger, J. J., and Dice, J. F., Proteolysis in cultured cells during prolonged serum deprivation and replacement. Am. J. Physiol., 251, C748-753 (1986).
    • (1986) Am. J. Physiol. , vol.251
    • Berger, J.J.1    Dice, J.F.2
  • 7
    • 0021175877 scopus 로고
    • Regulation of lysosomal autophagy in transformed and non-transformed mouse fibroblasts under several growth conditions
    • Knecht, E., Hernandez-Yago, J., and Grisolia, S., Regulation of lysosomal autophagy in transformed and non-transformed mouse fibroblasts under several growth conditions. Exp. Cell Res., 154, 224-232 (1984).
    • (1984) Exp. Cell Res. , vol.154 , pp. 224-232
    • Knecht, E.1    Hernandez-Yago, J.2    Grisolia, S.3
  • 8
    • 0024206530 scopus 로고
    • Endocrine regulation of protein breakdown in skeletal muscle
    • Kettelhut, I. C., Wing, S. S., and Goldberg, A. L., Endocrine regulation of protein breakdown in skeletal muscle. Diabetes Metab. Rev., 4, 751-772 (1988).
    • (1988) Diabetes Metab. Rev. , vol.4 , pp. 751-772
    • Kettelhut, I.C.1    Wing, S.S.2    Goldberg, A.L.3
  • 9
    • 0025868336 scopus 로고
    • Studies of the alpha-actinin/actin interaction in the Z-disk by using calpain
    • Goll, D. E., Dayton, W. R., Singh, I., and Robson, R. M., Studies of the alpha-actinin/actin interaction in the Z-disk by using calpain. J. Biol. Chem., 266, 8501-8510 (1991).
    • (1991) J. Biol. Chem. , vol.266 , pp. 8501-8510
    • Goll, D.E.1    Dayton, W.R.2    Singh, I.3    Robson, R.M.4
  • 11
    • 0030016595 scopus 로고    scopus 로고
    • Structure and functions of the 20S and 26S proteasomes
    • Coux, O., Tanaka, K., and Goldberg, A. L., Structure and functions of the 20S and 26S proteasomes. Annu. Rev. Biochem., 65, 801-847 (1996).
    • (1996) Annu. Rev. Biochem. , vol.65 , pp. 801-847
    • Coux, O.1    Tanaka, K.2    Goldberg, A.L.3
  • 12
    • 0025287267 scopus 로고
    • Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy
    • Furuno, K., Goodman, M. N., and Goldberg, A. L., Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy. J. Biol. Chem., 265, 8550-8557 (1990).
    • (1990) J. Biol. Chem. , vol.265 , pp. 8550-8557
    • Furuno, K.1    Goodman, M.N.2    Goldberg, A.L.3
  • 13
    • 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., and Goldberg, A. L., Importance of the ATP-ubiquitin- proteasome pathway in the degradation of soluble and myofibrillar proteins in rabbit muscle extracts. J. Biol. Chem., 271, 26690-26697 (1996).
    • (1996) J. Biol. Chem. , vol.271 , pp. 26690-26697
    • Solomon, V.1    Goldberg, A.L.2
  • 14
    • 0026029255 scopus 로고
    • Myofibrillar proteinase, cathepsin B, and protein breakdown rates in skeletal muscle from septic rats
    • Hall-Angeras, M., Hasselgren, P. O., Dimlich, R. V., and Fischer, J. E., Myofibrillar proteinase, cathepsin B, and protein breakdown rates in skeletal muscle from septic rats. Metabolism, 40, 302-306 (1991).
    • (1991) Metabolism , vol.40 , pp. 302-306
    • Hall-Angeras, M.1    Hasselgren, P.O.2    Dimlich, R.V.3    Fischer, J.E.4
  • 15
    • 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., and Hayashi, K., Comparison of the effects of thyroxine and triiodothyronine on protein turnover and apoptosis in primary chick muscle cell cultures. Biochem. Biophys. Res. Commun., 251, 442-448 (1998).
    • (1998) Biochem. Biophys. Res. Commun. , vol.251 , pp. 442-448
    • Nakashima, K.1    Ohtsuka, A.2    Hayashi, K.3
  • 16
    • 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., and Murachi, T., Comparative specificity and kinetic studies on porcine calpain I and calpain II with naturally occurring peptides and synthetic fluorogenic substrates. J. Biol. Chem., 259, 12489-12494 (1984).
    • (1984) J. Biol. Chem. , vol.259 , pp. 12489-12494
    • Sasaki, T.1    Kikuchi, T.2    Yumoto, N.3    Yoshimura, N.4    Murachi, T.5
  • 17
    • 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., and Goldberg, A. L., A high molecular weight protease in the cytosol of rat liver. I. Purification, enzymological properties, and tissue distribution. J. Biol. Chem., 261, 15197-15203 (1986).
    • (1986) J. Biol. Chem. , vol.261 , pp. 15197-15203
    • Tanaka, K.1    Ii, K.2    Ichihara, A.3    Waxman, L.4    Goldberg, A.L.5
  • 18
    • 0019765848 scopus 로고
    • Cathepsin B., Cathepsin H., and Cathepsin L.
    • Barrett, A. J., and Kirschke, H., Cathepsin B., Cathepsin H., and Cathepsin L. Methods Enzymol., 80, 535-561 (1981).
    • (1981) Methods Enzymol. , vol.80 , pp. 535-561
    • Barrett, A.J.1    Kirschke, H.2
  • 19
    • 1642576105 scopus 로고
    • Cathepsin D and other carboxyl protease
    • ed. Dingle, J. T., North-Holland, Amsterdam
    • Barrett, A. J., and Kirschke, H., Cathepsin D and other carboxyl protease. In "A Laboratry Hand Book", ed. Dingle, J. T., North-Holland, Amsterdam, pp. 19-147 (1977).
    • (1977) A Laboratry Hand Book , pp. 19-147
    • Barrett, A.J.1    Kirschke, H.2
  • 21
    • 0019313444 scopus 로고
    • A rapid, sensitive method for the determination of 3-methylhistidine levels in urine and plasma using high-pressure liquid chromatography
    • Wassner, S. J., Schlitzer, J. L., and Li, J. B., A rapid, sensitive method for the determination of 3-methylhistidine levels in urine and plasma using high-pressure liquid chromatography. Anal. Biochem., 104, 284-289 (1980).
    • (1980) Anal. Biochem. , vol.104 , pp. 284-289
    • Wassner, S.J.1    Schlitzer, J.L.2    Li, J.B.3
  • 22
    • 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, V. R., Alexis, S. D., Baliga, B. S., Munro, H. N., and Muecke, W., Metabolism of administered 3-methylhistidine. Lack of muscle transfer ribonucleic acid charging and quantitative excretion as 3-methylhistidine and its N-acetyl derivative. J. Biol. Chem., 247, 3592-3600 (1972).
    • (1972) J. Biol. Chem. , vol.247 , pp. 3592-3600
    • Young, V.R.1    Alexis, S.D.2    Baliga, B.S.3    Munro, H.N.4    Muecke, W.5
  • 23
    • 0030008051 scopus 로고    scopus 로고
    • Measurement of protein degradation by release of labelled 3-methylhistidine from skeletal muscle and non-muscle cells
    • Thompson, M. G., Palmer, R. M., Thom, A., Mackie, S. C., Morrison, S. C., and Harris, C. I., Measurement of protein degradation by release of labelled 3-methylhistidine from skeletal muscle and non-muscle cells. J. Cell. Physiol., 166, 506-511 (1996).
    • (1996) J. Cell. Physiol. , vol.166 , pp. 506-511
    • Thompson, M.G.1    Palmer, R.M.2    Thom, A.3    Mackie, S.C.4    Morrison, S.C.5    Harris, C.I.6
  • 24
    • 0036702869 scopus 로고    scopus 로고
    • Effects of the thyroid hormone on differentiation, growth, and proteolysis in cultured muscle cells during serum deprivation
    • Doi, J., Shinbori, Y., Ohtsuka, A., and Hayashi, K., Effects of the thyroid hormone on differentiation, growth, and proteolysis in cultured muscle cells during serum deprivation. J. Nutr. Sci. Vitaminol., 48, 265-269 (2002).
    • (2002) J. Nutr. Sci. Vitaminol. , vol.48 , pp. 265-269
    • Doi, J.1    Shinbori, Y.2    Ohtsuka, A.3    Hayashi, K.4
  • 25
    • 0030093797 scopus 로고    scopus 로고
    • τ-methylhistidine concentration is a sensitive index of myofibrillar protein degradation during starvation in rats
    • τ-methylhistidine concentration is a sensitive index of myofibrillar protein degradation during starvation in rats. Biosci. Biotechnol. Biochem., 60, 501-502 (1996).
    • (1996) Biosci. Biotechnol. Biochem. , vol.60 , pp. 501-502
    • Nagasawa, T.1    Yoshizawa, F.2    Nishizawa, N.3
  • 26
    • 0020688213 scopus 로고
    • Structures and functions of lysosomal thiol proteinases and their endogenous inhibitor
    • Katunuma, N., and Kominami, E., Structures and functions of lysosomal thiol proteinases and their endogenous inhibitor. Curr. Top. Cell. Regul., 22, 71-101 (1983).
    • (1983) Curr. Top. Cell. Regul. , vol.22 , pp. 71-101
    • Katunuma, N.1    Kominami, E.2
  • 27
    • 0027460118 scopus 로고
    • Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting
    • Wing, S. S., and Goldberg, A. L., Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am. J. Physiol., 264, E668-676 (1993).
    • (1993) Am. J. Physiol. , vol.264
    • Wing, S.S.1    Goldberg, A.L.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.