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Volumn 271, Issue 2 34-2, 1996, Pages

Role of different proteolytic pathways in degradation of muscle protein from streptozotocin-diabetic rats

Author keywords

adenosine triphosphate dependent proteolysis; calcium dependent proteolysis; lysosomal proteolysis; protein synthesis

Indexed keywords

ADENOSINE TRIPHOSPHATE; CALCIUM ION; CALPAIN; CYCLOHEXIMIDE; FATTY ACID; INSULIN; LYSOSOME ENZYME; MUSCLE PROTEIN; PHENYLALANINE;

EID: 0029741353     PISSN: 01931849     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpendo.1996.271.2.e340     Document Type: Article
Times cited : (115)

References (31)
  • 1
    • 0022996079 scopus 로고
    • Maintenance of normal length improves protein balance and energy status in isolated rat skeletal muscles
    • Cell Physiol. 20
    • Baracos, V. E., and A. L. Goldberg. Maintenance of normal length improves protein balance and energy status in isolated rat skeletal muscles. Am J. Physiol. 251 (Cell Physiol. 20): C588-C596, 1986.
    • (1986) Am J. Physiol. , vol.251
    • Baracos, V.E.1    Goldberg, A.L.2
  • 2
    • 2242473862 scopus 로고
    • Thyroid hormones control lysosomal enzyme activities in liver and skeletal muscle
    • DeMartino, G. N., and A. L. Goldberg. Thyroid hormones control lysosomal enzyme activities in liver and skeletal muscle. Proc Natl. Acad. Sci. USA 75: 1369-1373, 1978.
    • (1978) Proc Natl. Acad. Sci. USA , vol.75 , pp. 1369-1373
    • DeMartino, G.N.1    Goldberg, A.L.2
  • 3
    • 4344639664 scopus 로고
    • Microdetermination of long-chain fatty acids in plasma and tissues
    • Dole, V. P., and H. Meinertz. Microdetermination of long-chain fatty acids in plasma and tissues. J. Biol. Chem. 235: 2595-2599, 1960.
    • (1960) J. Biol. Chem. , vol.235 , pp. 2595-2599
    • Dole, V.P.1    Meinertz, H.2
  • 4
    • 0023122440 scopus 로고
    • Rat muscle protein turnover and redox state in progressive diabetes
    • Fagan, J. M., S. Satarug, P. Cook, and M. E. Tischler. Rat muscle protein turnover and redox state in progressive diabetes. Life Sci. 40: 783-790, 1987.
    • (1987) Life Sci. , vol.40 , pp. 783-790
    • Fagan, J.M.1    Satarug, S.2    Cook, P.3    Tischler, M.E.4
  • 5
    • 0022975889 scopus 로고
    • Red blood cells contain a pathway for the degadation of oxidant-damaged hemoglobin that does not require ATP or ubiquitin
    • Fagan, J. M., L. Waxman, and A. L. Goldberg. Red blood cells contain a pathway for the degadation of oxidant-damaged hemoglobin that does not require ATP or ubiquitin. J. Biol. Chem. 261: 5705-5713, 1986.
    • (1986) J. Biol. Chem. , vol.261 , pp. 5705-5713
    • Fagan, J.M.1    Waxman, L.2    Goldberg, A.L.3
  • 6
    • 0023185556 scopus 로고
    • Skeletal muscle and liver contain a soluble ATP + ubiquitin-dependent proteolytic system
    • Fagan, J. M., L. Waxman, and A. L. Goldberg. Skeletal muscle and liver contain a soluble ATP + ubiquitin-dependent proteolytic system. Biochem. J. 243: 335-343, 1987.
    • (1987) Biochem. J. , vol.243 , pp. 335-343
    • Fagan, J.M.1    Waxman, L.2    Goldberg, A.L.3
  • 7
    • 0016431688 scopus 로고
    • Effects of insulin, glucose and amino acids on protein turnover in rat diaphragm
    • Fulks, R., J. B. Li, and A. L. Goldberg. Effects of insulin, glucose and amino acids on protein turnover in rat diaphragm. J. Biol. Chem. 250: 290-298, 1975.
    • (1975) J. Biol. Chem. , vol.250 , pp. 290-298
    • Fulks, R.1    Li, J.B.2    Goldberg, A.L.3
  • 8
    • 0022466140 scopus 로고
    • The activation of protein degradation in muscle by calcium or muscle injury does not involve a lysosomal mechanism
    • Furuno, K., and A. L. Goldberg. The activation of protein degradation in muscle by calcium or muscle injury does not involve a lysosomal mechanism. Biochem. J. 237: 859-864, 1986.
    • (1986) Biochem. J. , vol.237 , pp. 859-864
    • Furuno, K.1    Goldberg, A.L.2
  • 9
    • 0025287267 scopus 로고
    • Role of different proteolytic systems in the degradation of muscle protein during denervation atrophy
    • Furuno, K., M. N. Goodman, and A. L. Goldberg. Role of different proteolytic systems in the degradation of muscle protein 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
  • 10
    • 16044372725 scopus 로고
    • Studies of the pathways of protein breakdown in skeletal muscle by use of protease inhibitors
    • edited by S. Ebashi. Tokyo: Univ. of Tokyo Press
    • Goldberg, A. L., T. Lockwood, and P. Rodemann. Studies of the pathways of protein breakdown in skeletal muscle by use of protease inhibitors. In: Proc. Int. Congr. Muscular Dystrophy, edited by S. Ebashi. Tokyo: Univ. of Tokyo Press, 1982, p. 207-223.
    • (1982) Proc. Int. Congr. Muscular Dystrophy , pp. 207-223
    • Goldberg, A.L.1    Lockwood, T.2    Rodemann, P.3
  • 11
    • 0023550729 scopus 로고
    • Myofibrillar protein breakdown in skeletal muscle is diminished in rats with chronic streptozotocin-induced diabetes
    • Goodman, M. N. Myofibrillar protein breakdown in skeletal muscle is diminished in rats with chronic streptozotocin-induced diabetes. Diabetes 36: 100-105, 1987.
    • (1987) Diabetes , vol.36 , pp. 100-105
    • Goodman, M.N.1
  • 12
    • 0026663539 scopus 로고
    • The ubiquitin system for protein degradation
    • Hershko, A., and A. Ciechanover. The ubiquitin system for protein degradation. Annu. Rev. Biochem. 61: 761-807, 1992.
    • (1992) Annu. Rev. Biochem. , vol.61 , pp. 761-807
    • Hershko, A.1    Ciechanover, A.2
  • 13
    • 0023933985 scopus 로고
    • The role of insulin and thyroid hormones in the regulation of muscle growth and protein turnover in response to dietary protein in the rat
    • Jepson, M. M., P. C. Bates, and D. J. Millward. The role of insulin and thyroid hormones in the regulation of muscle growth and protein turnover in response to dietary protein in the rat. Br. J. Nutr. 59: 397-415, 1988.
    • (1988) Br. J. Nutr. , vol.59 , pp. 397-415
    • Jepson, M.M.1    Bates, P.C.2    Millward, D.J.3
  • 14
    • 0024600649 scopus 로고
    • Differential regulation of the degradation of myofibrillar and total protein in skeletal muscle of rats: Effects of streptozotocin-induced diabetes, dietary protein and starvation
    • Kadowaki, M., N. Harada, S. Takahashi, T. Noguchi, and H. Naito. Differential regulation of the degradation of myofibrillar and total protein in skeletal muscle of rats: effects of streptozotocin-induced diabetes, dietary protein and starvation. J. Nutr. 119: 471-517, 1989.
    • (1989) J. Nutr. , vol.119 , pp. 471-517
    • Kadowaki, M.1    Harada, N.2    Takahashi, S.3    Noguchi, T.4    Naito, H.5
  • 15
    • 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
  • 16
    • 0024206530 scopus 로고
    • Endocrine regulation of protein breakdown in skeletal muscle
    • Kettelhut, I. C., S. S. Wing, and A. L. Goldberg. 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
  • 17
    • 0017089167 scopus 로고
    • Effects of food deprivation on protein synthesis and degradation in rat skeletal muscles
    • Li, J. B., and A. L. Goldberg. Effects of food deprivation on protein synthesis and degradation in rat skeletal muscles. Am. J Physiol. 231: 441-448, 1976.
    • (1976) Am. J Physiol. , vol.231 , pp. 441-448
    • Li, J.B.1    Goldberg, A.L.2
  • 18
    • 0028212481 scopus 로고
    • Metabolic acidosis stimulates muscle protein degradation by activating the adenosine triphosphate-dependent pathway involving ubiquitin and proteasomes
    • Mitch, W. E., R. Medina, S. Grieber, 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 proteasomes. J. Clin. Invest. 93: 2127-2133, 1994.
    • (1994) J. Clin. Invest. , vol.93 , pp. 2127-2133
    • Mitch, W.E.1    Medina, R.2    Grieber, S.3    May, R.C.4    England, B.K.5    Price, S.R.6    Bailey, J.L.7    Goldberg, A.L.8
  • 19
    • 84994945202 scopus 로고
    • Mechanism of cellular protein catabolism
    • Mortimore, G. E. Mechanism of cellular protein catabolism. Nutr. Rev. 40: 1-12, 1982.
    • (1982) Nutr. Rev. , vol.40 , pp. 1-12
    • Mortimore, G.E.1
  • 20
    • 0019234255 scopus 로고
    • 2--dependent protease (calpain) and its high molecular weight endogenous inhibitor (calpastatin)
    • 2--dependent protease (calpain) and its high molecular weight endogenous inhibitor (calpastatin). Adv. Enzyme Regul. 19: 407-424, 1981.
    • (1981) Adv. Enzyme Regul. , vol.19 , pp. 407-424
    • Murachi, T.1    Tanaka, K.2    Hatanaka, M.3    Murakami, T.4
  • 21
    • 0020987544 scopus 로고
    • Protein metabolism in skeletal muscle, diaphragm, and heart of diabetic rats
    • Endocrinol. Metab. 8
    • Pain, V. M., E. C. Albertse, and P. J. Garlick. Protein metabolism in skeletal muscle, diaphragm, and heart of diabetic rats. Am. J. Physiol. 245 (Endocrinol. Metab. 8): E604-E610, 1983.
    • (1983) Am. J. Physiol. , vol.245
    • Pain, V.M.1    Albertse, E.C.2    Garlick, P.J.3
  • 22
    • 0022386288 scopus 로고
    • The effect of insulin and intermittent mechanical stretching on rates of protein synthesis and degradation in isolated rabbit muscle
    • Palmer, R. M., P. A. Bain, and P. J. Reeds. The effect of insulin and intermittent mechanical stretching on rates of protein synthesis and degradation in isolated rabbit muscle. Biochem. J. 230: 117-123, 1985.
    • (1985) Biochem. J. , vol.230 , pp. 117-123
    • Palmer, R.M.1    Bain, P.A.2    Reeds, P.J.3
  • 23
    • 0017227340 scopus 로고
    • The metabolic event of starvation
    • Saudek, C. D., and P. Felig. The metabolic event of starvation. Am. J. Med. 60: 117-126, 1976.
    • (1976) Am. J. Med. , vol.60 , pp. 117-126
    • Saudek, C.D.1    Felig, P.2
  • 24
    • 0024442483 scopus 로고
    • Skeletal muscle proteolysis in rats with, acute streptozocin-induced diabetes
    • Smith, O. L. K., C. Y. Wong, and R. A. Gelfand. Skeletal muscle proteolysis in rats with, acute streptozocin-induced diabetes. Diabetes 38: 1117-1122, 1989.
    • (1989) Diabetes , vol.38 , pp. 1117-1122
    • Smith, O.L.K.1    Wong, C.Y.2    Gelfand, R.A.3
  • 25
    • 0026085902 scopus 로고
    • Regulation of protein turnover in skeletal and cardiac muscle
    • Sugden, P. H., and S. J. Fuller. Regulation of protein turnover in skeletal and cardiac muscle. Biochem. J. 273: 21-37, 1991.
    • (1991) Biochem. J. , vol.273 , pp. 21-37
    • Sugden, P.H.1    Fuller, S.J.2
  • 26
    • 0026706577 scopus 로고
    • Dietary protein deficiency reduces lysosomal and nonlysosomal ATP-dependent proteolysis in muscle
    • Endocrinol. Metab. 26
    • Tawa, N. E., Jr., I. C. Kettelhut, and A. L. Goldberg. Dietary protein deficiency reduces lysosomal and nonlysosomal ATP-dependent proteolysis in muscle. Am. J. Physiol. 263 (Endocrinol. Metab. 26): E326-E334, 1992.
    • (1992) Am. J. Physiol. , vol.263
    • Tawa Jr., N.E.1    Kettelhut, I.C.2    Goldberg, A.L.3
  • 27
    • 0020081889 scopus 로고
    • Does leucine, leucyl-tRNA or some metabolite of leucine regulate protein synthesis and degradation in skeletal and cardiac muscle?
    • Tischler, M. E., M. Desautels, and A. L. Goldberg. Does leucine, leucyl-tRNA or some metabolite of leucine regulate protein synthesis and degradation in skeletal and cardiac muscle? J. Biol. Chem. 257: 1613-1621, 1982.
    • (1982) J. Biol. Chem. , vol.257 , pp. 1613-1621
    • Tischler, M.E.1    Desautels, M.2    Goldberg, A.L.3
  • 28
    • 0023739851 scopus 로고
    • Increased protein degradation results from elevated free calcium levels found in muscle from mds mice
    • Turner, R. R., T. Westwood, C. M. Regen, and R. A. Steinhardt. Increased protein degradation results from elevated free calcium levels found in muscle from mds mice. Nature Lond. 335: 735-738, 1988.
    • (1988) Nature Lond. , vol.335 , pp. 735-738
    • Turner, R.R.1    Westwood, T.2    Regen, C.M.3    Steinhardt, R.A.4
  • 29
    • 0000569087 scopus 로고
    • A fluorometric method for the estimation of tyrosine in plasma and tissues
    • Waalkes, T. P., and S. Udenfriend. A fluorometric method for the estimation of tyrosine in plasma and tissues. J. Lab. Clin. Med. 50: 733-736, 1957.
    • (1957) J. Lab. Clin. Med. , vol.50 , pp. 733-736
    • Waalkes, T.P.1    Udenfriend, S.2
  • 30
    • 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
  • 31
    • 0029022262 scopus 로고
    • Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and denervation atrophy
    • Wing, S. S., A. L. Haas, and A. L. Goldberg. Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and denervation atrophy. 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


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.