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Volumn 218, Issue 3, 1998, Pages 244-250

Insulin-Like Growth Factor-I and High Protein Diet Decrease Calpain-Mediated Proteolysis in Murine Muscular Dystrophy

Author keywords

[No Author keywords available]

Indexed keywords

CALPAIN; RECOMBINANT SOMATOMEDIN C;

EID: 0031842735     PISSN: 00379727     EISSN: None     Source Type: Journal    
DOI: 10.3181/00379727-218-44294     Document Type: Article
Times cited : (22)

References (40)
  • 1
    • 2542477234 scopus 로고
    • Regulation of protein synthesis in normal and dystrophic muscle
    • Rowland LP, Ed. Amsterdam: Excerpta Medica
    • Goldberg AL, Griffin GE, Dice JF. Regulation of protein synthesis in normal and dystrophic muscle. In: Rowland LP, Ed. Pathogenesis of Human Muscular Dystrophies. Amsterdam: Excerpta Medica, pp 191-194, 1977.
    • (1977) Pathogenesis of Human Muscular Dystrophies , pp. 191-194
    • Goldberg, A.L.1    Griffin, G.E.2    Dice, J.F.3
  • 2
    • 0025287267 scopus 로고
    • Role of different proteolytic systems in the degradation of muscle proteins during denervation atrophy
    • Furono K, Goodman MN, 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
    • Furono, K.1    Goodman, M.N.2    Goldberg, A.L.3
  • 3
    • 0030638323 scopus 로고    scopus 로고
    • Regulation of skeletal muscle protein turnover during sepsis: Mechanisms and mediators
    • Cooney RN, Kimball SR, Vary TC. Regulation of skeletal muscle protein turnover during sepsis: Mechanisms and mediators. Shock 7:1-16, 1997.
    • (1997) Shock , vol.7 , pp. 1-16
    • Cooney, R.N.1    Kimball, S.R.2    Vary, T.C.3
  • 4
    • 0025988513 scopus 로고
    • Calcium-dependent and calcium-independent activities in skeletal muscle during sepsis
    • Bhattacharyya J, Thompson K, Sayeed MN. Calcium-dependent and calcium-independent activities in skeletal muscle during sepsis. Circulation Shock 35:117-122, 1991.
    • (1991) Circulation Shock , vol.35 , pp. 117-122
    • Bhattacharyya, J.1    Thompson, K.2    Sayeed, M.N.3
  • 5
    • 0027973113 scopus 로고
    • Ubiquitin changes in human biceps muscle following exercise-induced damage
    • Thompson HS, Scordilis SP. Ubiquitin changes in human biceps muscle following exercise-induced damage. Biochem Biophys Res Commun 204:1193-1198, 1994.
    • (1994) Biochem Biophys Res Commun , vol.204 , pp. 1193-1198
    • Thompson, H.S.1    Scordilis, S.P.2
  • 6
    • 0022905084 scopus 로고
    • Proteolytic enzyme activities and onset of muscular dystrophy in the chick
    • Ashmore CR, Summers PJ, Lee YB. Proteolytic enzyme activities and onset of muscular dystrophy in the chick. Exp Neurol 94:585-597, 1986.
    • (1986) Exp Neurol , vol.94 , pp. 585-597
    • Ashmore, C.R.1    Summers, P.J.2    Lee, Y.B.3
  • 7
    • 0024264074 scopus 로고
    • Calpain and calpastatin levels in dystrophic hamster skeletal muscles
    • Johnson P. Calpain and calpastatin levels in dystrophic hamster skeletal muscles. Im J Biochem Cell Biol 20:1227-1230, 1988.
    • (1988) Im J Biochem Cell Biol , vol.20 , pp. 1227-1230
    • Johnson, P.1
  • 8
    • 0026475826 scopus 로고
    • Demonstration of cathepsins B, H, and L in xenografts of normal and Duchenne muscular dystrophy muscle transplanted into nude mice
    • Takeda A, Jimi T, Wakayama Y, Misugi N, Miyake S, Kumgai T. Demonstration of cathepsins B, H, and L in xenografts of normal and Duchenne muscular dystrophy muscle transplanted into nude mice. Biochem J 288:643-648, 1992.
    • (1992) Biochem J , vol.288 , pp. 643-648
    • Takeda, A.1    Jimi, T.2    Wakayama, Y.3    Misugi, N.4    Miyake, S.5    Kumgai, T.6
  • 11
    • 0030957105 scopus 로고    scopus 로고
    • Metabolic and structural effects of IGF-I and high protein diet on dystrophic hamster skeletal muscle
    • Zdanowicz MM, Teichberg S, Moyse J, O'Connor M, Slonim AE. Metabolic and structural effects of IGF-I and high protein diet on dystrophic hamster skeletal muscle. Proc Soc Exp Biol Med 215:168-173, 1997.
    • (1997) Proc Soc Exp Biol Med , vol.215 , pp. 168-173
    • Zdanowicz, M.M.1    Teichberg, S.2    Moyse, J.3    O'Connor, M.4    Slonim, A.E.5
  • 12
    • 0023235910 scopus 로고
    • Decreased myofibrillar proteolysis after refeeding requires dietary proteins or amino acids
    • Goodman M, Gomez M. Decreased myofibrillar proteolysis after refeeding requires dietary proteins or amino acids. Am J Physiol 253:E52-E58, 1987.
    • (1987) Am J Physiol , vol.253
    • Goodman, M.1    Gomez, M.2
  • 13
    • 78651145203 scopus 로고
    • Micromethods for measuring phenylalanine and tyrosine in serum
    • Wong PWK, O'Flynn ME, Inouye T. Micromethods for measuring phenylalanine and tyrosine in serum. Clin Chem 10:1098-1104, 1964.
    • (1964) Clin Chem , vol.10 , pp. 1098-1104
    • Wong, P.W.K.1    O'Flynn, M.E.2    Inouye, T.3
  • 15
    • 0025777215 scopus 로고
    • Simple spectrophotometric assay for calcium-activated neutral proteases (calpains)
    • Moss D, Guiterrez Y, Perez R, Kobayashi H. Simple spectrophotometric assay for calcium-activated neutral proteases (calpains). Pharmacol Biochem Behav 39:495-497, 1991.
    • (1991) Pharmacol Biochem Behav , vol.39 , pp. 495-497
    • Moss, D.1    Guiterrez, Y.2    Perez, R.3    Kobayashi, H.4
  • 17
    • 0030695478 scopus 로고    scopus 로고
    • Pathways of ubiquitin conjugation
    • Haas AL, Siepmann TJ. Pathways of ubiquitin conjugation. FASEB J 11:1257-1268, 1997.
    • (1997) FASEB J , vol.11 , pp. 1257-1268
    • Haas, A.L.1    Siepmann, T.J.2
  • 18
    • 0003078684 scopus 로고
    • Multisample Hypothesis
    • Kurtz B, Ed. Englewood Cliffs, NJ: Prentice-Hall
    • Zar JH. Multisample Hypothesis. In: Kurtz B, Ed. Biostatistical Analysis. Englewood Cliffs, NJ: Prentice-Hall, pp162-183, 1984.
    • (1984) Biostatistical Analysis , pp. 162-183
    • Zar, J.H.1
  • 19
    • 0026442757 scopus 로고
    • Calpain concentration is elevated although net calcium-dependent proteolysis is suppressed in dystrophin deficient muscle
    • Spencer MJ, Tidball JG. Calpain concentration is elevated although net calcium-dependent proteolysis is suppressed in dystrophin deficient muscle. Exp Cell Res 203:107-114, 1992.
    • (1992) Exp Cell Res , vol.203 , pp. 107-114
    • Spencer, M.J.1    Tidball, J.G.2
  • 20
    • 0023219132 scopus 로고
    • Calcium-activated neutral protease and its endogenous inhibitor in tissues of dystrophic and normal mice
    • Rabbani N, Moses C, Anadaraj MPJS. Calcium-activated neutral protease and its endogenous inhibitor in tissues of dystrophic and normal mice. Biochem Med Metab Biol 37:282-286, 1987.
    • (1987) Biochem Med Metab Biol , vol.37 , pp. 282-286
    • Rabbani, N.1    Moses, C.2    Anadaraj, M.P.J.S.3
  • 21
    • 0023038510 scopus 로고
    • Calcium-activated neutral proteases and endogenous CANP inhibitor of muscle in Duchenne muscular dystrophy (DMD)
    • Reddy PA, Anadavalli TE, Anadaraj MPJS. Calcium-activated neutral proteases and endogenous CANP inhibitor of muscle in Duchenne muscular dystrophy (DMD). Clin Chim Acta 160:281-282, 1986.
    • (1986) Clin Chim Acta , vol.160 , pp. 281-282
    • Reddy, P.A.1    Anadavalli, T.E.2    Anadaraj, M.P.J.S.3
  • 22
    • 0026717398 scopus 로고
    • Increased leakage of calcium ion from the sarcoplasmic reticulum of the mdx mouse
    • Takagi A, Kojima S, Ida M, Araki M. Increased leakage of calcium ion from the sarcoplasmic reticulum of the mdx mouse. J Neurol Sci 110:160-164, 1992.
    • (1992) J Neurol Sci , vol.110 , pp. 160-164
    • Takagi, A.1    Kojima, S.2    Ida, M.3    Araki, M.4
  • 23
    • 0028334735 scopus 로고
    • Defective muscle basement membrane and lack of M-laminin in the dystrophic dy/dy mouse
    • Xu H, Christmas P, Wu X, Wewer U, Engvall E. Defective muscle basement membrane and lack of M-laminin in the dystrophic dy/dy mouse. Proc Natl Acad Sci USA 91:5572-5576, 1994.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 5572-5576
    • Xu, H.1    Christmas, P.2    Wu, X.3    Wewer, U.4    Engvall, E.5
  • 24
    • 0025762140 scopus 로고
    • An endogenous inhibitor of calcium-activated neutral protease in UMX 7.1 hamster dystrophy
    • Nakamyra M, Imajoh-Ohumi S, Suzuki K, Kawashima S. An endogenous inhibitor of calcium-activated neutral protease in UMX 7.1 hamster dystrophy. Muscle Nerve 14:701-708, 1991.
    • (1991) Muscle Nerve , vol.14 , pp. 701-708
    • Nakamyra, M.1    Imajoh-Ohumi, S.2    Suzuki, K.3    Kawashima, S.4
  • 25
    • 0022479243 scopus 로고
    • Evidence that lysosomes are not involved in the degradation of proteins in rat skeletal muscle
    • Lowell BB, Ruderman WB, Goodman MN. Evidence that lysosomes are not involved in the degradation of proteins in rat skeletal muscle. Biochem J 234:237-240, 1986.
    • (1986) Biochem J , vol.234 , pp. 237-240
    • Lowell, B.B.1    Ruderman, W.B.2    Goodman, M.N.3
  • 26
    • 0025822933 scopus 로고
    • Immunolocalization of ubiquitin in muscle biopsies of patients with inclusion body myositis and occulopharyngeal muscular dystrophy
    • Askansas K, Serdaroglu P, Engel N, Alvarez R. Immunolocalization of ubiquitin in muscle biopsies of patients with inclusion body myositis and occulopharyngeal muscular dystrophy. Neurosci Lett 130:73-76, 1991.
    • (1991) Neurosci Lett , vol.130 , pp. 73-76
    • Askansas, K.1    Serdaroglu, P.2    Engel, N.3    Alvarez, R.4
  • 27
    • 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, 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
  • 28
    • 0029000181 scopus 로고
    • Increase in levels of polyubiquitin and proteosome mRNA in skeletal muscle during starvation and denervation atrophy
    • Medina R, Wing SS, Goldberg AL. Increase in levels of polyubiquitin and proteosome 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
  • 29
    • 0016431688 scopus 로고
    • Effect of insulin, glucose, and amino acids on protein turnover in rat diaphragm
    • Fulks RM, Li JB, Goldberg AL. Effect 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.M.1    Li, J.B.2    Goldberg, A.L.3
  • 30
    • 2542503699 scopus 로고
    • Reversal of diet-induced catabolism by infusion of recombinant IGF-I in humans
    • Clemmons DR, Smith-Banks A, Celinker AC. Reversal of diet-induced catabolism by infusion of recombinant IGF-I in humans. J Clin Endocrinol Metab 74:142-147, 1992.
    • (1992) J Clin Endocrinol Metab , vol.74 , pp. 142-147
    • Clemmons, D.R.1    Smith-Banks, A.2    Celinker, A.C.3
  • 31
    • 0027103153 scopus 로고
    • Role of insulin-like growth factors and growth hormone in reversing catabolic states
    • Clemmons DR, Underwood LE. Role of insulin-like growth factors and growth hormone in reversing catabolic states. Horm Res 38:37-40, 1992.
    • (1992) Horm Res , vol.38 , pp. 37-40
    • Clemmons, D.R.1    Underwood, L.E.2
  • 32
    • 0029950661 scopus 로고    scopus 로고
    • The combined action of two thyroidal proteases releases T4 from dominant hormone-forming site of thyroglobulin
    • Dunn AD, Myers HE, Dunn JT. The combined action of two thyroidal proteases releases T4 from dominant hormone-forming site of thyroglobulin. Endocrinology 137:3279-3285, 1996.
    • (1996) Endocrinology , vol.137 , pp. 3279-3285
    • Dunn, A.D.1    Myers, H.E.2    Dunn, J.T.3
  • 33
    • 0023678686 scopus 로고    scopus 로고
    • Cysteine proteinases from human thyroids and their actions on thyroglobulin
    • Dunn AD, Dunn JT. Cysteine proteinases from human thyroids and their actions on thyroglobulin. Endocrinology 123:1089-1097, 1997.
    • (1997) Endocrinology , vol.123 , pp. 1089-1097
    • Dunn, A.D.1    Dunn, J.T.2
  • 34
    • 2542431364 scopus 로고
    • Hormonal regulation of protein synthesis and degradation in skeletal muscle
    • Goldberg AL, Tischler M, DeMartino G, Grifin G. Hormonal regulation of protein synthesis and degradation in skeletal muscle. Fed Proc 39:30-37, 1980.
    • (1980) Fed Proc , vol.39 , pp. 30-37
    • Goldberg, A.L.1    Tischler, M.2    Demartino, G.3    Grifin, G.4
  • 35
    • 0030003967 scopus 로고    scopus 로고
    • The sarcoplasmic reticulum calcium pump is functionally altered in dystrophic muscle
    • Kargacin ME, Kargacin GJ. The sarcoplasmic reticulum calcium pump is functionally altered in dystrophic muscle. Biochim Biophys Acta 1290:4-8, 1996.
    • (1996) Biochim Biophys Acta , vol.1290 , pp. 4-8
    • Kargacin, M.E.1    Kargacin, G.J.2
  • 36
    • 0026717398 scopus 로고
    • Increased leakage of calcium ion from the sarcoplasmic reticulum of the mdx mouse
    • Takagi A, Kojima S, Ida M, Araki M. Increased leakage of calcium ion from the sarcoplasmic reticulum of the mdx mouse. J Neurol Sci 110:160-164, 1992.
    • (1992) J Neurol Sci , vol.110 , pp. 160-164
    • Takagi, A.1    Kojima, S.2    Ida, M.3    Araki, M.4
  • 37
    • 0021684232 scopus 로고
    • Myopathy and growth failure in debrancher enzyme deficiency: Improvement with high-protein nocturnal enteral therapy
    • Slonim AE, Coleman RA, Moses WS. Myopathy and growth failure in debrancher enzyme deficiency: Improvement with high-protein nocturnal enteral therapy. J Pediatr 105:906-911, 1984.
    • (1984) J Pediatr , vol.105 , pp. 906-911
    • Slonim, A.E.1    Coleman, R.A.2    Moses, W.S.3
  • 39
    • 0020080838 scopus 로고
    • Reversal of debrancher deficiency myopathy by the use of high-protein nutrition
    • Slonim AE, Weisberg C, Benke P, Evans OB, Burr IM. Reversal of debrancher deficiency myopathy by the use of high-protein nutrition. Ann Neurol 11:420-422, 1982.
    • (1982) Ann Neurol , vol.11 , pp. 420-422
    • Slonim, A.E.1    Weisberg, C.2    Benke, P.3    Evans, O.B.4    Burr, I.M.5
  • 40
    • 0011846629 scopus 로고
    • Effects of oral branched-chain amino acid administration in the treatment of cancer cachexia
    • Cangiao C. Effects of oral branched-chain amino acid administration in the treatment of cancer cachexia. Clin Res 42:129A, 1994.
    • (1994) Clin Res , vol.42
    • Cangiao, C.1


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