메뉴 건너뛰기




Volumn 272, Issue 3 41-3, 1997, Pages

Activation of the ubiquitin pathway in rat skeletal muscle by catabolic doses of glucocorticoids

Author keywords

3 methylhistidine; corticosterone; E3 14k; proteasome; proteolysis

Indexed keywords

3 METHYLHISTIDINE; CORTICOSTERONE; GLUCOCORTICOID; MESSENGER RNA; POLYUBIQUITIN; PROTEASOME; UBIQUITIN;

EID: 0030909411     PISSN: 03636143     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpcell.1997.272.3.c1007     Document Type: Article
Times cited : (110)

References (67)
  • 1
    • 0029040739 scopus 로고
    • Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma
    • Endocrinol. Metab. 31
    • Baracos, V. E., C. DeVivo, D. H. Hoyle, and A. L. Goldberg. Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma. Am. J. Physiol. 268 (Endocrinol. Metab. 31): E996-E1006, 1995.
    • (1995) Am. J. Physiol. , vol.268
    • Baracos, V.E.1    Devivo, C.2    Hoyle, D.H.3    Goldberg, A.L.4
  • 2
    • 0015011589 scopus 로고
    • Histochemical, biochemical and contractile properties of red, white, and intermediate fibers
    • Barnard, R. J., V. R. Edgerton, T. Furukawa, and J. B. Peter. Histochemical, biochemical and contractile properties of red, white, and intermediate fibers. Am. J. Physiol. 220: 410-414, 1971.
    • (1971) Am. J. Physiol. , vol.220 , pp. 410-414
    • Barnard, R.J.1    Edgerton, V.R.2    Furukawa, T.3    Peter, J.B.4
  • 3
    • 0020503783 scopus 로고
    • Myofibrillar protein turnover: Synthesis rates of myofibrillar and sarcoplasmic protein fractions in different muscles and the changes observed during postnatal development and in response to feeding and starvation
    • Bates, P. C., and D. J. Millward. Myofibrillar protein turnover: synthesis rates of myofibrillar and sarcoplasmic protein fractions in different muscles and the changes observed during postnatal development and in response to feeding and starvation. Biochem. J. 214: 587-592, 1983.
    • (1983) Biochem. J. , vol.214 , pp. 587-592
    • Bates, P.C.1    Millward, D.J.2
  • 4
    • 0029880121 scopus 로고    scopus 로고
    • Effect of corticosterone on protein degradation in isolated rat soleus and extensor digitorum longus muscles
    • Bowes, S. B., N. C. Jackson, D. Papachristodoulou, A. M. Umpleby, and P. H. Sonksen. Effect of corticosterone on protein degradation in isolated rat soleus and extensor digitorum longus muscles. J. Endocrinol. 148: 501-507, 1996.
    • (1996) J. Endocrinol. , vol.148 , pp. 501-507
    • Bowes, S.B.1    Jackson, N.C.2    Papachristodoulou, D.3    Umpleby, A.M.4    Sonksen, P.H.5
  • 5
    • 0020353234 scopus 로고
    • Conjugation of ubiquitin to denatured hemoglobin is proportional to the rate of hemoglobin degradation in HeLa cells
    • Chin, D. T., L. Kuehl, and M. Rechsteiner. Conjugation of ubiquitin to denatured hemoglobin is proportional to the rate of hemoglobin degradation in HeLa cells. Proc. Natl. Acad. Sci. USA 79: 5857-5861, 1982.
    • (1982) Proc. Natl. Acad. Sci. USA , vol.79 , pp. 5857-5861
    • Chin, D.T.1    Kuehl, L.2    Rechsteiner, M.3
  • 6
    • 0023277545 scopus 로고
    • Single step method of RNA isolation by acid guadinium thiocyanate-phenol-chloroform extraction
    • Chomczynsky, P., and N. Sacchi. Single step method of RNA isolation by acid guadinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162: 156-159, 1987.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynsky, P.1    Sacchi, N.2
  • 8
    • 78651049191 scopus 로고
    • Influence of adrenal cortical steroids on carbohydrate metabolism in man
    • Conn, J. W., and S. S. Fajans. Influence of adrenal cortical steroids on carbohydrate metabolism in man. Metabolism 5: 114-127, 1956.
    • (1956) Metabolism , vol.5 , pp. 114-127
    • Conn, J.W.1    Fajans, S.S.2
  • 9
    • 0028881695 scopus 로고
    • Sensitivity and protein turnover response to glucocorticoids are different in skeletal muscle from adult and old rats. Lack of regulation of the ubiquitin-proteasome proteolytic pathway in aging
    • Dardevet, D., C. Sornet, D. Taillandier, I. Savary, D. Attaix, and J. Grizard. Sensitivity and protein turnover response to glucocorticoids are different in skeletal muscle from adult and old rats. Lack of regulation of the ubiquitin-proteasome proteolytic pathway in aging. J. Clin. Invest. 96: 2113-2119, 1995.
    • (1995) J. Clin. Invest. , vol.96 , pp. 2113-2119
    • Dardevet, D.1    Sornet, C.2    Taillandier, D.3    Savary, I.4    Attaix, D.5    Grizard, J.6
  • 10
    • 0028817382 scopus 로고
    • Burn injury stimulates multiple proteolytic pathways in skeletal muscle, including the ubiquitin-energy-dependent pathway
    • Fang, C.-H., G. Tiao, H. James, C. Ogle, J. E. Fisher, and P.-O. Hasselgren. Burn injury stimulates multiple proteolytic pathways in skeletal muscle, including the ubiquitin-energy-dependent pathway. J. Am. Coll. Surg. 180: 161-170, 1995.
    • (1995) J. Am. Coll. Surg. , vol.180 , pp. 161-170
    • Fang, C.-H.1    Tiao, G.2    James, H.3    Ogle, C.4    Fisher, J.E.5    Hasselgren, P.-O.6
  • 12
    • 0022423216 scopus 로고
    • Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate dehydrogenase multigenic family
    • Fort, P., M. Piechaczyc, S. El Salbrouty, C. Dany, P. Jeanteur, and J. M. Blanchard. Various rat adult tissues express only one major mRNA species from the glyceraldehyde-3-phosphate dehydrogenase multigenic family. Nucleic Acids Res. 13: 1431-1442, 1985.
    • (1985) Nucleic Acids Res. , vol.13 , pp. 1431-1442
    • Fort, P.1    Piechaczyc, M.2    El Salbrouty, S.3    Dany, C.4    Jeanteur, P.5    Blanchard, J.M.6
  • 13
    • 0027266801 scopus 로고
    • Tumor necrosis factor-α increases the ubiquitinization of rat skeletal muscle proteins
    • García-Martínez, C., N. Agell, M. Llovera, F. J. López-Soriano, and J. M. Argiles. Tumor necrosis factor-α increases the ubiquitinization of rat skeletal muscle proteins. FEBS Lett. 323: 211-214, 1993.
    • (1993) FEBS Lett. , vol.323 , pp. 211-214
    • García-Martínez, C.1    Agell, N.2    Llovera, M.3    López-Soriano, F.J.4    Argiles, J.M.5
  • 15
    • 0027163954 scopus 로고
    • Glucocorticoid regulation of insulin receptor and substrate IRS-1 tyrosine phosphorylation in rat skeletal muscle in vivo
    • Giorgino, F., A. Almahfouz, L. J. Goodyear, and R. J. Smith. Glucocorticoid regulation of insulin receptor and substrate IRS-1 tyrosine phosphorylation in rat skeletal muscle in vivo. J. Clin. Invest. 91: 2020-2030, 1993.
    • (1993) J. Clin. Invest. , vol.91 , pp. 2020-2030
    • Giorgino, F.1    Almahfouz, A.2    Goodyear, L.J.3    Smith, R.J.4
  • 16
    • 0014690578 scopus 로고
    • Protein turnover in skeletal muscle II. Effects of denervation and cortisone on protein catabolism in skeletal muscle
    • Goldberg, A. L. Protein turnover in skeletal muscle II. Effects of denervation and cortisone on protein catabolism in skeletal muscle. J. Biol. Chem. 244: 3223-3229, 1969.
    • (1969) J. Biol. Chem. , vol.244 , pp. 3223-3229
    • Goldberg, A.L.1
  • 17
    • 2442437350 scopus 로고
    • Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells
    • Goldstein, G., M. Scheid, U. Hammerling, E. A. Boyse, D. H. Schlesinger, and H. D. Niall. Isolation of a polypeptide that has lymphocyte-differentiating properties and is probably represented universally in living cells. Proc. Natl. Acad. Sci. USA 72: 11-15, 1975.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.72 , pp. 11-15
    • Goldstein, G.1    Scheid, M.2    Hammerling, U.3    Boyse, E.A.4    Schlesinger, D.H.5    Niall, H.D.6
  • 18
    • 0024486752 scopus 로고
    • UbiA, the major polyubiquitin locus in Ceanorhabditis elegans, has unusual structural features and is constitutively expressed
    • Graham, R. W., D. Jones, and E. P. Candido. UbiA, the major polyubiquitin locus in Ceanorhabditis elegans, has unusual structural features and is constitutively expressed. Mol. Cell. Biol. 9: 268-277, 1989.
    • (1989) Mol. Cell. Biol. , vol.9 , pp. 268-277
    • Graham, R.W.1    Jones, D.2    Candido, E.P.3
  • 19
    • 0028897653 scopus 로고
    • Coordinated induction of the ubiquitin conjugation pathway accompanies the developmentally programmed death of insect skeletal muscle
    • Haas, A. L., O. Baboshina, B. Williams, and L. M. Schwartz. Coordinated induction of the ubiquitin conjugation pathway accompanies the developmentally programmed death of insect skeletal muscle. J. Biol. Chem. 270: 9407-9412, 1995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 9407-9412
    • Haas, A.L.1    Baboshina, O.2    Williams, B.3    Schwartz, L.M.4
  • 20
    • 0023115331 scopus 로고
    • The dynamics of ubiquitin pools within cultured human lung fibroblasts
    • Haas, A. L., and P. M. Bright. The dynamics of ubiquitin pools within cultured human lung fibroblasts. J. Biol. Chem. 262: 345-351, 1987.
    • (1987) J. Biol. Chem. , vol.262 , pp. 345-351
    • Haas, A.L.1    Bright, P.M.2
  • 21
    • 0020479562 scopus 로고
    • The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis
    • Haas, A. L., and I. A. Rose. The mechanism of ubiquitin activating enzyme. A kinetic and equilibrium analysis. J. Biol. Chem. 257: 10329-10337, 1982.
    • (1982) J. Biol. Chem. , vol.257 , pp. 10329-10337
    • Haas, A.L.1    Rose, I.A.2
  • 22
    • 0025293425 scopus 로고
    • Corticosterone alone does not explain increased muscle proteolysis in septic rats
    • Hall-Angerås, M., U. Angerås, P. O. Hasselgren, and J. E. Fischer. Corticosterone alone does not explain increased muscle proteolysis in septic rats. J. Surg. Res. 48: 368-372, 1990.
    • (1990) J. Surg. Res. , vol.48 , pp. 368-372
    • Hall-Angerås, M.1    Angerås, U.2    Hasselgren, P.O.3    Fischer, J.E.4
  • 23
    • 0028507737 scopus 로고
    • Effects of serum and insulin-like growth factor-1 on protein degradation and protease gene expression in rat L8 myotubes
    • Hong, D. H., and N. E. Forsberg. Effects of serum and insulin-like growth factor-1 on protein degradation and protease gene expression in rat L8 myotubes. J. Anim. Sci. 72: 2279-2288, 1994.
    • (1994) J. Anim. Sci. , vol.72 , pp. 2279-2288
    • Hong, D.H.1    Forsberg, N.E.2
  • 26
    • 0025051529 scopus 로고
    • Insulin-and thyroid hormone-independent adaptation of myofibrillar proteolysis to glucocorticoids
    • Endocrinol. Metab. 22
    • Kayali, A. G., M. N. Goodman, J. Lin, and R. Young. Insulin-and thyroid hormone-independent adaptation of myofibrillar proteolysis to glucocorticoids. Am. J. Physiol. 259 (Endocrinol. Metab. 22): E699-E705, 1990.
    • (1990) Am. J. Physiol. , vol.259
    • Kayali, A.G.1    Goodman, M.N.2    Lin, J.3    Young, R.4
  • 27
    • 0023261107 scopus 로고
    • Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis
    • Endocrinol. Metab. 15
    • Kayali, A. G., V. R. Young, and M. N. Goodman. Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis. Am. J. Physiol. 252 (Endocrinol. Metab. 15): E621-E626, 1987.
    • (1987) Am. J. Physiol. , vol.252
    • Kayali, A.G.1    Young, V.R.2    Goodman, M.N.3
  • 28
    • 0020460813 scopus 로고
    • The differing responses of four muscle types to dexamethasone treatment in the rat
    • Kelly, F. J., and D. F. Goldspink. The differing responses of four muscle types to dexamethasone treatment in the rat. Biochem. J. 208: 147-151, 1982.
    • (1982) Biochem. J. , vol.208 , pp. 147-151
    • Kelly, F.J.1    Goldspink, D.F.2
  • 29
    • 0024405575 scopus 로고
    • Elevation of plasma epinephrine concentration inhibits protolysis and leucine oxydation in man via beta-adrenergic mechanisms
    • Kraenzlin, M. E., U. Keller, A. Keller, A. Thelin, M. J. Arnaud, and W. Stauffachjer. Elevation of plasma epinephrine concentration inhibits protolysis and leucine oxydation in man via beta-adrenergic mechanisms. J. Clin. Invest. 84: 388-393, 1989.
    • (1989) J. Clin. Invest. , vol.84 , pp. 388-393
    • Kraenzlin, M.E.1    Keller, U.2    Keller, A.3    Thelin, A.4    Arnaud, M.J.5    Stauffachjer, W.6
  • 32
    • 0022969340 scopus 로고
    • Regulation of myofibrillar protein degradation in rat skeletal muscle during brief and prolonged starvation
    • Lowell, B. B., N. B. Ruderman, and M. N. Goodman. Regulation of myofibrillar protein degradation in rat skeletal muscle during brief and prolonged starvation. Metabolism 35: 1121-1127, 1986.
    • (1986) Metabolism , vol.35 , pp. 1121-1127
    • Lowell, B.B.1    Ruderman, N.B.2    Goodman, M.N.3
  • 33
    • 0015972243 scopus 로고
    • Rat myofibrillar protease: Enzyme properties and adaptive changes in conditions of muscle protein degradation
    • Mayer, M., R. Amin, and E. Shafrir. Rat myofibrillar protease: enzyme properties and adaptive changes in conditions of muscle protein degradation. Arch. Biochem. Biophys. 161: 20-25, 1974.
    • (1974) Arch. Biochem. Biophys. , vol.161 , pp. 20-25
    • Mayer, M.1    Amin, R.2    Shafrir, E.3
  • 34
    • 0020356706 scopus 로고
    • Glucocorticoid action on protein synthesis and protein breakdown in isolated skeletal muscles
    • McGrath, J. A., and D. F. Goldspink. Glucocorticoid action on protein synthesis and protein breakdown in isolated skeletal muscles. Biochem. J. 206: 641-645, 1982.
    • (1982) Biochem. J. , vol.206 , pp. 641-645
    • McGrath, J.A.1    Goldspink, D.F.2
  • 35
    • 0026006653 scopus 로고
    • Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy
    • Medina, R., S. S. Wing, A. Haas, and A. L. Goldberg. Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy. Biomed. Biochim. Acta 50: 347-356, 1991.
    • (1991) Biomed. Biochim. Acta , vol.50 , pp. 347-356
    • Medina, R.1    Wing, S.S.2    Haas, A.3    Goldberg, A.L.4
  • 36
    • 0027403853 scopus 로고
    • Intron and intronless transcription of the chicken polyubiquitin gene UbII
    • Mezquita, J., B. López-Ibor, M. Pau, and C. Mezquita. Intron and intronless transcription of the chicken polyubiquitin gene UbII. FEBS Lett. 319: 244-248, 1993.
    • (1993) FEBS Lett. , vol.319 , pp. 244-248
    • Mezquita, J.1    López-Ibor, B.2    Pau, M.3    Mezquita, C.4
  • 37
    • 0017272271 scopus 로고
    • The relative importance of protein synthesis and breakdown in the regulation of muscle mass
    • Millward, D. J., P. J. Garlick, D. O. Nnanyelugo, and J. C. Waterlow. The relative importance of protein synthesis and breakdown in the regulation of muscle mass. Biochem. J. 156: 185-188, 1976.
    • (1976) Biochem. J. , vol.156 , pp. 185-188
    • Millward, D.J.1    Garlick, P.J.2    Nnanyelugo, D.O.3    Waterlow, J.C.4
  • 38
    • 0028212481 scopus 로고
    • Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasome
    • Mitch, W. E., R. Medina, S. Greiber, R. C. May, B. K. England, S. R. Price, J. L. Bailey, and A. L. Goldberg. Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasome. J. Clin. Invest. 93: 2127-2133, 1994.
    • (1994) J. Clin. Invest. , vol.93 , pp. 2127-2133
    • Mitch, W.E.1    Medina, R.2    Greiber, S.3    May, R.C.4    England, B.K.5    Price, S.R.6    Bailey, J.L.7    Goldberg, A.L.8
  • 39
    • 0027266849 scopus 로고
    • Homologous down regulation of the glucocorticoid receptor: The molecular machinery
    • Oakley, R. H., and J. A. Cidlowski. Homologous down regulation of the glucocorticoid receptor: the molecular machinery. Crit. Rev. Eukaryotic Gene Expr. 3: 63-88, 1993.
    • (1993) Crit. Rev. Eukaryotic Gene Expr. , vol.3 , pp. 63-88
    • Oakley, R.H.1    Cidlowski, J.A.2
  • 40
    • 0020521619 scopus 로고
    • Time course of the effect of catabolic doses of corticosterone on protein turnover in rat skeletal muscle and liver
    • Odedra, B. R., P. C. Bates, and D. J. Millward. Time course of the effect of catabolic doses of corticosterone on protein turnover in rat skeletal muscle and liver. Biochem. J. 214: 617-627, 1983.
    • (1983) Biochem. J. , vol.214 , pp. 617-627
    • Odedra, B.R.1    Bates, P.C.2    Millward, D.J.3
  • 41
    • 0026599990 scopus 로고
    • Reduction of corticosterone-induced muscle proteolysis and growth retardation by a combined treatment with insulin, testosterone and high-protein-high-fat diet in rats
    • Ohtsuka, A., K. Hayashi, T. Noda, and Y. Tomita. Reduction of corticosterone-induced muscle proteolysis and growth retardation by a combined treatment with insulin, testosterone and high-protein-high-fat diet in rats. J. Nutr. Sci. Vitaminol. 38: 83-92, 1992.
    • (1992) J. Nutr. Sci. Vitaminol. , vol.38 , pp. 83-92
    • Ohtsuka, A.1    Hayashi, K.2    Noda, T.3    Tomita, Y.4
  • 43
    • 0017613512 scopus 로고
    • A simplification of the protein assay method of Lowry et al. which is more generally applicable
    • Peterson, G. L. A simplification of the protein assay method of Lowry et al. which is more generally applicable. Anal. Biochem. 83: 346-356, 1977.
    • (1977) Anal. Biochem. , vol.83 , pp. 346-356
    • Peterson, G.L.1
  • 44
    • 0027972943 scopus 로고
    • Acidosis and glucocorticoids concomitantly increase ubiquitin and proteasome subunit mRNAs in rat muscle
    • Cell Physiol. 36
    • Price, S. R., B. K. England, J. L. Bailey, K. Van Vreede, and W. E. Mitch. Acidosis and glucocorticoids concomitantly increase ubiquitin and proteasome subunit mRNAs in rat muscle. Am. J. Physiol. 267 (Cell Physiol. 36): C955-C960, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Price, S.R.1    England, B.K.2    Bailey, J.L.3    Van Vreede, K.4    Mitch, W.E.5
  • 45
    • 0001090861 scopus 로고
    • Effects of glucocorticoids on muscle protein turnover in perfused rat hemicorpus
    • Endocrinol. Metab. 1
    • Rannels, S. R., and L. S. Jefferson. Effects of glucocorticoids on muscle protein turnover in perfused rat hemicorpus. Am. J. Physiol. 238 (Endocrinol. Metab. 1): E564-E572, 1980.
    • (1980) Am. J. Physiol. , vol.238
    • Rannels, S.R.1    Jefferson, L.S.2
  • 46
    • 0018004269 scopus 로고
    • Glucocorticoid effects on peptide chain initiation in skeletal muscle and heart
    • Endocrinol. Metab. Gastrointest. Physiol. 4
    • Rannels, S. R., D. E. Rannels, A. L. Pegg, and L. S. Jefferson. Glucocorticoid effects on peptide chain initiation in skeletal muscle and heart. Am. J. Physiol. 235 (Endocrinol. Metab. Gastrointest. Physiol. 4): E134-E139, 1978.
    • (1978) Am. J. Physiol. , vol.235
    • Rannels, S.R.1    Rannels, D.E.2    Pegg, A.L.3    Jefferson, L.S.4
  • 47
    • 0021447734 scopus 로고
    • Enhanced glucose metabolism after exercise: Modulation by local factors
    • Endocrinol. Metab. 9
    • Richter, E. A., L. P. Garetto, M. N. Goodman, and N. B. Ruderman. Enhanced glucose metabolism after exercise: modulation by local factors. Am. J. Physiol. 246 (Endocrinol. Metab. 9): E476-E482, 1984.
    • (1984) Am. J. Physiol. , vol.246
    • Richter, E.A.1    Garetto, L.P.2    Goodman, M.N.3    Ruderman, N.B.4
  • 48
    • 85003195436 scopus 로고
    • Cortisol-induced insulin resistance in man: Impaired suppression of glucose production and stimulation of glucose utilization due to a postreceptor defect of insulin action
    • Rizza, R. A., L. J. Mandarino, and J. E. Gerich. Cortisol-induced insulin resistance in man: impaired suppression of glucose production and stimulation of glucose utilization due to a postreceptor defect of insulin action. J. Clin. Endocrinol. Metab. 54: 131-138, 1982.
    • (1982) J. Clin. Endocrinol. Metab. , vol.54 , pp. 131-138
    • Rizza, R.A.1    Mandarino, L.J.2    Gerich, J.E.3
  • 49
    • 0019414602 scopus 로고
    • Effect of corticosterone and its route of administration on muscle protein breakdown, measured in vivo by urinary excretion of Nt-methylhistidine in rats: Response to different levels of dietary protein and energy
    • Santidrian, S., M. Moreyra, H. N. Munro, and V. R. Young. Effect of corticosterone and its route of administration on muscle protein breakdown, measured in vivo by urinary excretion of Nt-methylhistidine in rats: response to different levels of dietary protein and energy. Metabolism 30: 798-804, 1981.
    • (1981) Metabolism , vol.30 , pp. 798-804
    • Santidrian, S.1    Moreyra, M.2    Munro, H.N.3    Young, V.R.4
  • 50
    • 20644451980 scopus 로고
    • Adrenocortical influences on dipeptidase activity of surviving rat diaphragm
    • Schwartz, T. B., M. C. Robertson, and L. B. Holmes. Adrenocortical influences on dipeptidase activity of surviving rat diaphragm. J. Biochem. 58: 453-460, 1956.
    • (1956) J. Biochem. , vol.58 , pp. 453-460
    • Schwartz, T.B.1    Robertson, M.C.2    Holmes, L.B.3
  • 51
    • 0025322546 scopus 로고
    • Influence of glucocorticoids on skeletal muscle proteolysis in normal and diabetic-adrenalectomized eviscerated rats
    • Smith, O. L. K., C. Y. Wong, and R. A. Gelfand. Influence of glucocorticoids on skeletal muscle proteolysis in normal and diabetic-adrenalectomized eviscerated rats. Metab. Clin. Exp. 39: 6, 1990.
    • (1990) Metab. Clin. Exp. , vol.39 , pp. 6
    • Smith, O.L.K.1    Wong, C.Y.2    Gelfand, R.A.3
  • 54
    • 0027973469 scopus 로고
    • Sepsis stimulates nonlysosomal, energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle
    • Tiao, G., J. M. Fagan, N. Samuels, J. H. James, K. Hudson, M. Lieberman, J. E. Fischer, and P. O. Hasselgren. Sepsis stimulates nonlysosomal, energy-dependent proteolysis and increases ubiquitin mRNA levels in rat skeletal muscle. J. Clin. Invest. 94: 2255-2264, 1994.
    • (1994) J. Clin. Invest. , vol.94 , pp. 2255-2264
    • Tiao, G.1    Fagan, J.M.2    Samuels, N.3    James, J.H.4    Hudson, K.5    Lieberman, M.6    Fischer, J.E.7    Hasselgren, P.O.8
  • 55
    • 0020279428 scopus 로고
    • τ-methylhistidine excretion
    • τ-methylhistidine excretion. Biochem. J. 208: 593-601, 1982.
    • (1982) Biochem. J. , vol.208 , pp. 593-601
    • Tomas, F.M.1
  • 59
    • 0024452208 scopus 로고
    • Properties of skeletal muscle fibers. II. Hormonal influences
    • Vigneron, P., J. Dainat, and F. Bacou. Properties of skeletal muscle fibers. II. Hormonal influences. Reprod. Nutr. Dev. 29: 27-53, 1989.
    • (1989) Reprod. Nutr. Dev. , vol.29 , pp. 27-53
    • Vigneron, P.1    Dainat, J.2    Bacou, F.3
  • 60
    • 0020201812 scopus 로고
    • τ-methylhistidine release: Contributions of rat skeletal muscle, GI tract, and skin
    • Endocrinol. Metab. 6
    • τ-methylhistidine release: contributions of rat skeletal muscle, GI tract, and skin. Am. J. Physiol. 243 (Endocrinol. Metab. 6): E293-E297, 1982.
    • (1982) Am. J. Physiol. , vol.243
    • Wassner, S.J.1    Li, J.B.2
  • 61
    • 0028007982 scopus 로고
    • 14-kDa ubiquitin-conjugating enzyme: Structure of the rat gene and regulation upon fasting and by insulin
    • Endocrinol. Metab. 30
    • Wing, S. S., and D. Banville. 14-kDa ubiquitin-conjugating enzyme: structure of the rat gene and regulation upon fasting and by insulin. Am. J. Physiol. 267 (Endocrinol. Metab. 30): E39-E48, 1994.
    • (1994) Am. J. Physiol. , vol.267
    • Wing, S.S.1    Banville, D.2
  • 62
    • 0027460118 scopus 로고
    • Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting
    • Endocrinol. Metab. 27
    • Wing, S. S., and A. L. Goldberg. Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am. J. Physiol. 264 (Endocrinol. Metab. 27): E668-E676, 1993.
    • (1993) Am. J. Physiol. , vol.264
    • Wing, S.S.1    Goldberg, A.L.2
  • 63
    • 0029022262 scopus 로고
    • Increase in the ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation
    • Wing, S. S., A. L. Haas, and A. L. Goldberg. Increase in the ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation. Biochem. J. 307: 639-645, 1995.
    • (1995) Biochem. J. , vol.307 , pp. 639-645
    • Wing, S.S.1    Haas, A.L.2    Goldberg, A.L.3
  • 64
    • 0028292562 scopus 로고
    • Effect of dexamethasone on muscle protein homeostasis and on calpain and calpastatin activities and gene expression in rabbits
    • Yeh, J. Y., B. R. Ou, and N. E. Forsberg. Effect of dexamethasone on muscle protein homeostasis and on calpain and calpastatin activities and gene expression in rabbits. J. Endocrinol. 141: 209-217, 1994.
    • (1994) J. Endocrinol. , vol.141 , pp. 209-217
    • Yeh, J.Y.1    Ou, B.R.2    Forsberg, N.E.3
  • 65
    • 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., S. D. Alexis, B. S. Beliga, and H. N. Munro. 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    Beliga, B.S.3    Munro, H.N.4
  • 66
    • 0018200306 scopus 로고
    • τ-methylhistidine (3-methylhistidine) and muscle protein turnover: An overview
    • τ-methylhistidine (3-methylhistidine) and muscle protein turnover: an overview. Federation Proc. 37: 2291-2300, 1978.
    • (1978) Federation Proc. , vol.37 , pp. 2291-2300
    • Young, V.R.1    Munro, H.N.2
  • 67
    • 0025836449 scopus 로고
    • The effect of interleukin-1a and the glucocorticoid receptor blocker RU 38486 on total and myofibrillar protein breakdown in skeletal muscle
    • Zamir, O., P. O. Hasseigren, D. von Allmen, and J. E. Fischer. The effect of interleukin-1a and the glucocorticoid receptor blocker RU 38486 on total and myofibrillar protein breakdown in skeletal muscle. J. Surg. Res. 50: 579-583, 1991.
    • (1991) J. Surg. Res. , vol.50 , pp. 579-583
    • Zamir, O.1    Hasseigren, P.O.2    Von Allmen, D.3    Fischer, J.E.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.