메뉴 건너뛰기




Volumn 287, Issue 4 50-4, 2004, Pages

IGF-I stimulates muscle growth by suppressing protein breakdown and expression of atrophy-related ubiquitin ligases, atrogin-1 and MuRF1

Author keywords

3 methylhistidine; Glucocorticoids; Insulin; Phosphatidylinositol 3 kinase Akt pathway

Indexed keywords

3 METHYLHISTIDINE; CALCINEURIN; CELL PROTEIN; DEXAMETHASONE; GLUCOCORTICOID; INSULIN; MESSENGER RNA; MITOGEN ACTIVATED PROTEIN KINASE; MUSCLE PROTEIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE B; SOMATOMEDIN C; TRANSCRIPTION FACTOR NFAT; UBIQUITIN PROTEIN LIGASE;

EID: 4544293878     PISSN: 01931849     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpendo.00073.2004     Document Type: Article
Times cited : (523)

References (57)
  • 1
    • 0021996291 scopus 로고
    • Protein turnover in different types of skeletal muscle during experimental hyperthyroidism in rats
    • Angeras U and Hasselgren PO. Protein turnover in different types of skeletal muscle during experimental hyperthyroidism in rats, Acta Endocrinol 109: 90-95, 1985.
    • (1985) Acta Endocrinol , vol.109 , pp. 90-95
    • Angeras, U.1    Hasselgren, P.O.2
  • 2
    • 0029040739 scopus 로고
    • Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma
    • Baracos VE, DeVivo C, Hoyle DH, and Goldberg AL. Activation of the ATP-ubiquitin-proteasome pathway in skeletal muscle of cachectic rats bearing a hepatoma. Am J Physiol Endocrinol Metab 268: E996-E1006, 1995.
    • (1995) Am J Physiol Endocrinol Metab , vol.268
    • Baracos, V.E.1    DeVivo, C.2    Hoyle, D.H.3    Goldberg, A.L.4
  • 5
    • 0035499454 scopus 로고    scopus 로고
    • Ten years of protein kinase B signalling: A hard Akt to follow
    • Brazil DP and Hemmings BA. Ten years of protein kinase B signalling: a hard Akt to follow. Trends Biochem Sci 26: 657-664, 2001.
    • (2001) Trends Biochem Sci , vol.26 , pp. 657-664
    • Brazil, D.P.1    Hemmings, B.A.2
  • 8
    • 0034464615 scopus 로고    scopus 로고
    • Insulin-like growth factor I reduces ubiquitin and ubiquitin-conjugating enzyme gene expression but does not inhibit muscle proteolysis in septic rats
    • Fang CH, Li BG, Sun X, and Hasselgren PO. Insulin-like growth factor I reduces ubiquitin and ubiquitin-conjugating enzyme gene expression but does not inhibit muscle proteolysis in septic rats. Endocrinology 141: 2743-2751, 2000.
    • (2000) Endocrinology , vol.141 , pp. 2743-2751
    • Fang, C.H.1    Li, B.G.2    Sun, X.3    Hasselgren, P.O.4
  • 9
    • 0025287267 scopus 로고
    • Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy
    • Furuno K, Goodman MN, and Goldberg AL. 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
  • 10
    • 0041424822 scopus 로고    scopus 로고
    • Molecular mechanisms modulating muscle mass
    • Glass D. Molecular mechanisms modulating muscle mass. Trends Mol Med 9: 344-350, 2003.
    • (2003) Trends Mol Med , vol.9 , pp. 344-350
    • Glass, D.1
  • 11
    • 0037318822 scopus 로고    scopus 로고
    • Signalling pathways that mediate skeletal muscle hypertrophy and atrophy
    • Glass DJ. Signalling pathways that mediate skeletal muscle hypertrophy and atrophy. Nat Cell Biol 5: 87-90, 2003.
    • (2003) Nat Cell Biol , vol.5 , pp. 87-90
    • Glass, D.J.1
  • 12
    • 0018741336 scopus 로고
    • Influence of insulin and contractile activity on muscle size and protein balance
    • Goldberg AL. Influence of insulin and contractile activity on muscle size and protein balance. Diabetes 28: 18-24, 1979.
    • (1979) Diabetes , vol.28 , pp. 18-24
    • Goldberg, A.L.1
  • 13
    • 0014690566 scopus 로고
    • Protein turnover in skeletal muscle. I. Protein catabolism during work-induced hypertrophy and growth induced with growth hormone
    • Goldberg AL. Protein turnover in skeletal muscle. I. Protein catabolism during work-induced hypertrophy and growth induced with growth hormone. J Biol Chem 244: 3217-3222, 1969.
    • (1969) J Biol Chem , vol.244 , pp. 3217-3222
    • Goldberg, A.L.1
  • 14
    • 0014506782 scopus 로고
    • Effects of disuse and denervation on amino acid transport by skeletal muscle
    • Goldberg AL and Goodman HM. Effects of disuse and denervation on amino acid transport by skeletal muscle. Am J Physiol 216: 1116-1119, 1969.
    • (1969) Am J Physiol , vol.216 , pp. 1116-1119
    • Goldberg, A.L.1    Goodman, H.M.2
  • 15
    • 0035807969 scopus 로고    scopus 로고
    • Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy
    • Gomes MD, Lecker SH, Jagoe RT, Navon A, and Goldberg AL. Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy. Proc Natl Acad Sci USA 98: 14440-14445, 2001.
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 14440-14445
    • Gomes, M.D.1    Lecker, S.H.2    Jagoe, R.T.3    Navon, A.4    Goldberg, A.L.5
  • 16
    • 0023550729 scopus 로고
    • Myofibrillar protein breakdown in skeletal muscle is diminished in rats with chronic streptozocin-induced diabetes
    • Goodman M. Myofibrillar protein breakdown in skeletal muscle is diminished in rats with chronic streptozocin-induced diabetes. Diabetes 36: 100-105, 1987.
    • (1987) Diabetes , vol.36 , pp. 100-105
    • Goodman, M.1
  • 18
    • 0021917182 scopus 로고
    • The ATP dependence of the degradation of short- and long-lived proteins in growing fibroblasts
    • Gronostajski RM, Pardee AB, and Goldberg AL. The ATP dependence of the degradation of short- and long-lived proteins in growing fibroblasts. J Biol Chem 260: 3344-3349, 1985.
    • (1985) J Biol Chem , vol.260 , pp. 3344-3349
    • Gronostajski, R.M.1    Pardee, A.B.2    Goldberg, A.L.3
  • 19
    • 0028507737 scopus 로고
    • Effects of serum and insulin-like growth factor I on protein degradation and protease gene expression in rat L8 myotubes
    • Hong D and Forsberg NE. Effects of serum and insulin-like growth factor I 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.1    Forsberg, N.E.2
  • 20
    • 0036845620 scopus 로고    scopus 로고
    • Patterns of gene expression in atrophying skeletal muscles: Response to food deprivation
    • Jagoe RT, Lecker SH, Gomes M, and Goldberg AL. Patterns of gene expression in atrophying skeletal muscles: response to food deprivation. FASEB J 16: 1697-1712, 2002.
    • (2002) FASEB J , vol.16 , pp. 1697-1712
    • Jagoe, R.T.1    Lecker, S.H.2    Gomes, M.3    Goldberg, A.L.4
  • 21
    • 0032909280 scopus 로고    scopus 로고
    • Preventive effects of insulin-like growth factor-I on steroid-induced muscle atrophy
    • Kanda F, Takatani K, Okuda S, Matsushita T, and Chihara K. Preventive effects of insulin-like growth factor-I on steroid-induced muscle atrophy. Muscle Nerve 22: 213-217, 1999.
    • (1999) Muscle Nerve , vol.22 , pp. 213-217
    • Kanda, F.1    Takatani, K.2    Okuda, S.3    Matsushita, T.4    Chihara, K.5
  • 22
    • 0023261107 scopus 로고
    • Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis
    • Kayali AG, Young VR, and Goodman MN. Sensitivity of myofibrillar proteins to glucocorticoid-induced muscle proteolysis. Am J Physiol Endocrinol Metab 252: E621-E626, 1987.
    • (1987) Am J Physiol Endocrinol Metab , vol.252
    • Kayali, A.G.1    Young, V.R.2    Goodman, M.N.3
  • 24
    • 12244252222 scopus 로고    scopus 로고
    • Slowing muscle atrophy: Putting the brakes on protein breakdown
    • Lecker SH and Goldberg AL. Slowing muscle atrophy: putting the brakes on protein breakdown. J Physiol 545: 729, 2002.
    • (2002) J Physiol , vol.545 , pp. 729
    • Lecker, S.H.1    Goldberg, A.L.2
  • 25
    • 0032947267 scopus 로고    scopus 로고
    • Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states
    • Lecker SH, Solomon V, Mitch WE, and Goldberg AL. Muscle protein breakdown and the critical role of the ubiquitin-proteasome pathway in normal and disease states. J Nutr 129: 227S-237S, 1999.
    • (1999) J Nutr , vol.129
    • Lecker, S.H.1    Solomon, V.2    Mitch, W.E.3    Goldberg, A.L.4
  • 26
    • 0032751546 scopus 로고    scopus 로고
    • Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats
    • Lecker SH, Solomon V, Price SR, Kwon YT, Mitch WE, and Goldberg AL. Ubiquitin conjugation by the N-end rule pathway and mRNAs for its components increase in muscles of diabetic rats. J Clin Invest 104: 1411-1420, 1999.
    • (1999) J Clin Invest , vol.104 , pp. 1411-1420
    • Lecker, S.H.1    Solomon, V.2    Price, S.R.3    Kwon, Y.T.4    Mitch, W.E.5    Goldberg, A.L.6
  • 27
    • 0021248108 scopus 로고
    • Effects of food deprivation and refeeding on total protein and actomyosin degradation
    • Li J and Wassner S. Effects of food deprivation and refeeding on total protein and actomyosin degradation. Am J Physiol Endocrinol Metab 246: E32-E37, 1984.
    • (1984) Am J Physiol Endocrinol Metab , vol.246
    • Li, J.1    Wassner, S.2
  • 28
  • 29
    • 0033696398 scopus 로고    scopus 로고
    • NF-κB mediates the protein loss induced by TNF-α in differentiated skeletal muscle myotubes
    • Li YP and Reid MB. NF-κB mediates the protein loss induced by TNF-α in differentiated skeletal muscle myotubes. Am J Physiol Regul Integr Comp Physiol 279: R1165-R1170, 2000.
    • (2000) Am J Physiol Regul Integr Comp Physiol , vol.279
    • Li, Y.P.1    Reid, M.B.2
  • 30
    • 0037053304 scopus 로고    scopus 로고
    • Ubiquitin (UbC) expression in muscle cells is increased by glucocorticoids through a mechanism involving Sp1 and MEK1
    • Marinovic A, Zheng B, Mitch W, and Price S. Ubiquitin (UbC) expression in muscle cells is increased by glucocorticoids through a mechanism involving Sp1 and MEK1. J Biol Chem 277: 16673-16681, 2002.
    • (2002) J Biol Chem , vol.277 , pp. 16673-16681
    • Marinovic, A.1    Zheng, B.2    Mitch, W.3    Price, S.4
  • 31
    • 0036544533 scopus 로고    scopus 로고
    • Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1
    • McElhinny A, Kakinuma K, Sorimachi H, Labeit S, and Gregorio C. Muscle-specific RING finger-1 interacts with titin to regulate sarcomeric M-line and thick filament structure and may have nuclear functions via its interaction with glucocorticoid modulatory element binding protein-1. J Cell Biol 157: 125-136, 2002.
    • (2002) J Cell Biol , vol.157 , pp. 125-136
    • McElhinny, A.1    Kakinuma, K.2    Sorimachi, H.3    Labeit, S.4    Gregorio, C.5
  • 32
    • 0029000181 scopus 로고
    • Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy
    • Medina R, Wing SS, and Goldberg AL. Increase in levels of polyubiquitin and proteasome mRNA in skeletal muscle during starvation and denervation atrophy. Biochem J 307: 631-637, 1995.
    • (1995) Biochem J , vol.307 , pp. 631-637
    • Medina, R.1    Wing, S.S.2    Goldberg, A.L.3
  • 33
    • 0026006653 scopus 로고
    • Activation of the ubiquitin-ATP-dependent proteolytic system in skeletal muscle during fasting and denervation atrophy
    • Medina R, Wing SS, Haas A, and Goldberg AL. 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
  • 37
    • 0034735910 scopus 로고    scopus 로고
    • Metallothioneins, oxidative stress and the cardiovascular system
    • Nath R, Kumar D, Li T, and Singal PK. Metallothioneins, oxidative stress and the cardiovascular system. Toxicology 155: 17-26, 2000.
    • (2000) Toxicology , vol.155 , pp. 17-26
    • Nath, R.1    Kumar, D.2    Li, T.3    Singal, P.K.4
  • 38
    • 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, Hayashi K, Noda T, and Tomita Y. 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 (Tokyo) 38: 83-92, 1992.
    • (1992) J Nutr Sci Vitaminol (Tokyo) , vol.38 , pp. 83-92
    • Ohtsuka, A.1    Hayashi, K.2    Noda, T.3    Tomita, Y.4
  • 39
    • 0029741353 scopus 로고    scopus 로고
    • Role of different proteolytic pathways in degradation of muscle protein from streptozotocin-diabetic rats
    • Pepato MT, Migliorini RH, Goldberg AL, and Kettelhut IC. Role of different proteolytic pathways in degradation of muscle protein from streptozotocin-diabetic rats. Am J Physiol Endocrinol Metab 271: E340-E347, 1996.
    • (1996) Am J Physiol Endocrinol Metab , vol.271
    • Pepato, M.T.1    Migliorini, R.H.2    Goldberg, A.L.3    Kettelhut, I.C.4
  • 40
    • 0031892271 scopus 로고    scopus 로고
    • TNF-α insulin resistance: Summary and future prospects
    • Peraldi P and Spiegelman B. TNF-α and insulin resistance: summary and future prospects. Mol Cell Biochem 182: 169-175, 1998.
    • (1998) Mol. Cell Biochem , vol.182 , pp. 169-175
    • Peraldi, P.1    Spiegelman, B.2
  • 41
    • 0029655707 scopus 로고    scopus 로고
    • Necessary but not sufficient: The role of glucocorticoids in the acidosis-induced increase in levels of mRNAs encoding proteins of the ATP-dependent proteolytic pathway in rat muscle
    • Price SR, Bailey JL, and England BK. Necessary but not sufficient: the role of glucocorticoids in the acidosis-induced increase in levels of mRNAs encoding proteins of the ATP-dependent proteolytic pathway in rat muscle. Miner Electrolyte Metab 22: 72-75, 1996.
    • (1996) Miner Electrolyte Metab , vol.22 , pp. 72-75
    • Price, S.R.1    Bailey, J.L.2    England, B.K.3
  • 42
    • 0029861468 scopus 로고    scopus 로고
    • Muscle wasting in insulinopenic rats results from activation of the ATP-dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription
    • Price SR, Bailey JL, Wang X, Jurkovitz C, England BK, Ding X, Phillips LS, and Mitch WE. Muscle wasting in insulinopenic rats results from activation of the ATP-dependent, ubiquitin-proteasome proteolytic pathway by a mechanism including gene transcription. J Clin Invest 98: 1703-1708, 1996.
    • (1996) J Clin Invest , vol.98 , pp. 1703-1708
    • Price, S.R.1    Bailey, J.L.2    Wang, X.3    Jurkovitz, C.4    England, B.K.5    Ding, X.6    Phillips, L.S.7    Mitch, W.E.8
  • 43
    • 0027972943 scopus 로고
    • Acidosis and glucocorticoids concomitantly increase ubiquitin and proteasome subunit mRNAs in rat muscle
    • Price SR, England BK, Bailey JL, Van Vreede K, and Mitch WE. Acidosis and glucocorticoids concomitantly increase ubiquitin and proteasome subunit mRNAs in rat muscle. Am J Physiol Cell Phvsiol 267: C955-C960, 1994.
    • (1994) Am J Physiol Cell Phvsiol , vol.267
    • Price, S.R.1    England, B.K.2    Bailey, J.L.3    Van Vreede, K.4    Mitch, W.E.5
  • 45
    • 4544357478 scopus 로고    scopus 로고
    • Expression of muscle-specific ubiquitin-protein ligases (E3s) during muscle atrophy
    • Sacheck JM. Expression of muscle-specific ubiquitin-protein ligases (E3s) during muscle atrophy (Abstract). FASEB J 17: A9578, 2003.
    • (2003) FASEB J , vol.17
    • Sacheck, J.M.1
  • 48
    • 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. 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.2
  • 49
    • 0025019455 scopus 로고
    • Atrophy of the soleus muscle by hindlimb unweighting
    • Thomason DB and Booth FW. Atrophy of the soleus muscle by hindlimb unweighting. J Appl Physiol 68: 1-12, 1990.
    • (1990) J Appl Physiol , vol.68 , pp. 1-12
    • Thomason, D.B.1    Booth, F.W.2
  • 52
    • 0025353885 scopus 로고
    • Different mechanisms of increased proteolysis in atrophy induced by denervation or unweighting of rat soleus muscle
    • Tischler ME, Rosenberg S, Satarug S, Henriksen EJ, Kirby CR, Tome M, and Chase P. Different mechanisms of increased proteolysis in atrophy induced by denervation or unweighting of rat soleus muscle. Metabolism 39: 756-763, 1990.
    • (1990) Metabolism , vol.39 , pp. 756-763
    • Tischler, M.E.1    Rosenberg, S.2    Satarug, S.3    Henriksen, E.J.4    Kirby, C.R.5    Tome, M.6    Chase, P.7
  • 53
    • 0036633921 scopus 로고    scopus 로고
    • Biochemical mechanisms of cellular catabolism
    • Tisdale M. Biochemical mechanisms of cellular catabolism. Curr Opin Clin Nutr Metab Care 5: 401-405, 2002.
    • (2002) Curr Opin Clin Nutr Metab Care , vol.5 , pp. 401-405
    • Tisdale, M.1
  • 54
    • 0032185015 scopus 로고    scopus 로고
    • Dexamethasone stimulates proteasome- and calcium-dependent proteolysis in cultured L6 myotubes
    • Wang L, Luo GJ, Wang JJ, and Hasselgren PO. Dexamethasone stimulates proteasome- and calcium-dependent proteolysis in cultured L6 myotubes. Shock 10: 298-306, 1998.
    • (1998) Shock , vol.10 , pp. 298-306
    • Wang, L.1    Luo, G.J.2    Wang, J.J.3    Hasselgren, P.O.4
  • 55
    • 0027460118 scopus 로고
    • Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting
    • Wing SS and Goldberg AL. Glucocorticoids activate the ATP-ubiquitin-dependent proteolytic system in skeletal muscle during fasting. Am J Physiol Endocrinol Metab 264: E668-E676, 1993.
    • (1993) Am J Physiol Endocrinol Metab , vol.264
    • Wing, S.S.1    Goldberg, A.L.2
  • 56
    • 0029022262 scopus 로고
    • Increase in ubiquitin-protein conjugates concomitant with the increase in proteolysis in rat skeletal muscle during starvation and atrophy denervation
    • Wing SS, Haas AL, and Goldberg AL. Increase in 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
  • 57
    • 0037401683 scopus 로고    scopus 로고
    • Sepsis upregulates the gene expression of multiple ubiquitin ligases in skeletal muscle
    • Wray CJ, Mammen JM, Hershko DD, and Hasselgren PO. Sepsis upregulates the gene expression of multiple ubiquitin ligases in skeletal muscle. Int J Biochem Cell Biol 35: 698-705, 2003.
    • (2003) Int J Biochem Cell Biol , vol.35 , pp. 698-705
    • Wray, C.J.1    Mammen, J.M.2    Hershko, D.D.3    Hasselgren, P.O.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.