메뉴 건너뛰기




Volumn 37, Issue 4, 2012, Pages 885-898

Oxidative damage in muscular dystrophy correlates with the severity of the pathology: Role of glutathione metabolism

Author keywords

Cardiotoxin; Duchenne muscular dystrophy; Dysferlinopathy; Glutathione; Muscular dystrophy; Oxidative stress; Sarcoglycanopathy

Indexed keywords

CARDIOTOXIN; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE PEROXIDASE; GLUTATHIONE TRANSFERASE;

EID: 84862834965     PISSN: 03643190     EISSN: 15736903     Source Type: Journal    
DOI: 10.1007/s11064-011-0683-z     Document Type: Article
Times cited : (61)

References (52)
  • 2
    • 0028903251 scopus 로고
    • Isolation and characterization of distinct domains of sarcolemma and T-tubules from rat skeletal muscle
    • (Pt 1)
    • Munoz P, Rosemblatt M, Testar X, Palacin M, Zorzano A (1995) Isolation and characterization of distinct domains of sarcolemma and T-tubules from rat skeletal muscle. Biochem J 307(Pt 1): 273-280
    • (1995) Biochem J , vol.307 , pp. 273-280
    • Munoz, P.1    Rosemblatt, M.2    Testar, X.3    Palacin, M.4    Zorzano, A.5
  • 3
    • 0035190381 scopus 로고    scopus 로고
    • The dystrophin-glycoprotein complex, cellular signaling, and the regulation of cell survival in the muscular dystrophies
    • DOI 10.1002/mus.1192
    • Rando TA (2001) The dystrophin-glycoprotein complex, cellular signaling, and the regulation of cell survival in the muscular dystrophies. Muscle Nerve 24(12):1575-1594 (Pubitemid 33101403)
    • (2001) Muscle and Nerve , vol.24 , Issue.12 , pp. 1575-1594
    • Rando, T.A.1
  • 5
    • 0023125464 scopus 로고
    • Superoxide dismutases, glutathione peroxidase, and catalase in neuromuscular disease
    • DOI 10.1002/mus.880100208
    • Burr IM, Asayama K, Fenichel GM (1987) Superoxide dismutases, glutathione peroxidase, and catalase in neuromuscular disease. Muscle Nerve 10(2):150-154. doi:10.1002/mus.880100208 (Pubitemid 17004219)
    • (1987) Muscle and Nerve , vol.10 , Issue.2 , pp. 150-154
    • Burr, I.M.1    Asayama, K.2    Fenichel, G.M.3
  • 6
    • 0018758714 scopus 로고
    • Catalase, superoxide dismutase, glutathione reductase and thiobarbituric acid-reactive products in normal and dystrophic human muscle
    • DOI 10.1016/0009-8981(79)90076-7
    • Kar NC, Pearson CM (1979) Catalase, superoxide dismutase, glutathione reductase and thiobarbituric acid-reactive products in normal and dystrophic human muscle. Clin Chim Acta 94(3): 277-280 (Pubitemid 9204033)
    • (1979) Clinica Chimica Acta , vol.94 , Issue.3 , pp. 277-280
    • Kar, N.C.1    Pearson, C.M.2
  • 7
    • 19744365952 scopus 로고    scopus 로고
    • Mitochondrial respiratory chain dysfunction in various neuromuscular diseases
    • DOI 10.1016/j.jocn.2004.06.014, PII S0967586805000421
    • Jongpiputvanich S, Sueblinvong T, Norapucsunton T (2005) Mitochondrial respiratory chain dysfunction in various neuromuscular diseases. J Clin Neurosci 12(4):426-428. doi:10.1016/j.jocn.2004.06.014 (Pubitemid 40745228)
    • (2005) Journal of Clinical Neuroscience , vol.12 , Issue.4 , pp. 426-428
    • Jongpiputvanich, S.1    Sueblinvong, T.2    Norapucsunton, T.3
  • 9
    • 0018874942 scopus 로고
    • Blood levels of superoxide dismutase and glutathione peroxidase in Duchenne muscular dystrophy
    • DOI 10.1016/0009-8981(80)90467-2
    • Burri BJ, Chan SG, Berry AJ, Yarnell SK (1980) Blood levels of superoxide dismutase and glutathione peroxidase in Duchenne muscular dystrophy. Clin Chim Acta 105(2):249-255 (Pubitemid 10078348)
    • (1980) Clinica Chimica Acta , vol.105 , Issue.2 , pp. 249-255
    • Burri, B.J.1    Chan, S.G.2    Berry, A.J.3    Yarnell, S.K.4
  • 10
    • 42649127060 scopus 로고    scopus 로고
    • Isoprostanes in dystrophinopathy: Evidence of increased oxidative stress
    • DOI 10.1016/j.braindev.2007.11.005, PII S0387760407002483
    • Grosso S, Perrone S, Longini M, Bruno C, Minetti C, Gazzolo D, Balestri P, Buonocore G (2008) Isoprostanes in dystrophinopathy: evidence of increased oxidative stress. Brain Dev 30(6): 391-395. doi:10.1016/j.braindev.2007.11.005 (Pubitemid 351602223)
    • (2008) Brain and Development , vol.30 , Issue.6 , pp. 391-395
    • Grosso, S.1    Perrone, S.2    Longini, M.3    Bruno, C.4    Minetti, C.5    Gazzolo, D.6    Balestri, P.7    Buonocore, G.8
  • 11
    • 15444353991 scopus 로고    scopus 로고
    • Differential protein oxidation in Duchenne and Becker muscular dystrophy
    • Haycock JW, Mac Neil S, Mantle D (1998) Differential protein oxidation in Duchenne and Becker muscular dystrophy. Neuro Report 9(10):2201-2207 (Pubitemid 28338206)
    • (1998) NeuroReport , vol.9 , Issue.10 , pp. 2201-2207
    • Haycock, J.W.1    Mac Neil, S.2    Mantle, D.3
  • 12
    • 16644399758 scopus 로고    scopus 로고
    • Early onset of lipofuscin accumulation in dystrophin-deficient skeletal muscles of DMD patients and mdx mice
    • DOI 10.1023/B:HIJO.0000045947.83628.a7
    • Nakae Y, Stoward PJ, Kashiyama T, Shono M, Akagi A, Matsuzaki T, Nonaka I (2004) Early onset of lipofuscin accumulation in dystrophin-deficient skeletal muscles of DMD patients and mdx mice. J Mol Histol 35(5):489-499 (Pubitemid 41410964)
    • (2004) Journal of Molecular Histology , vol.35 , Issue.5 , pp. 489-499
    • Nakae, Y.1    Stoward, P.J.2    Kashiyama, T.3    Shono, M.4    Akagi, A.5    Matsuzaki, T.6    Nonaka, I.7
  • 14
    • 0030861564 scopus 로고    scopus 로고
    • Oxidative stress as a potential pathogenic mechanism in an animal model of Duchenne muscular dystrophy
    • DOI 10.1016/S0960-8966(97)00096-5, PII S0960896697000965
    • Ragusa RJ, Chow CK, Porter JD (1997) Oxidative stress as a potential pathogenic mechanism in an animal model of Duchenne muscular dystrophy. Neuromuscul Disord 7(6-7):379-386 (Pubitemid 27445322)
    • (1997) Neuromuscular Disorders , vol.7 , Issue.6-7 , pp. 379-386
    • Ragusa, R.J.1    Chow, C.K.2    Porter, J.D.3
  • 15
    • 33645450207 scopus 로고    scopus 로고
    • Sarcolemmal damage in dystrophin deficiency is modulated by synergistic interactions between mechanical and oxidative/nitrosative stresses
    • quiz 1404-1275. doi:10.2353/ajpath.2006.050683
    • Dudley RW, Danialou G, Govindaraju K, Lands L, Eidelman DE, Petrof BJ (2006) Sarcolemmal damage in dystrophin deficiency is modulated by synergistic interactions between mechanical and oxidative/nitrosative stresses. Am J Pathol 168(4): 1276-1287; quiz 1404-1275. doi:10.2353/ajpath.2006.050683
    • (2006) Am J Pathol , vol.168 , Issue.4 , pp. 1276-1287
    • Dudley, R.W.1    Danialou, G.2    Govindaraju, K.3    Lands, L.4    Eidelman, D.E.5    Petrof, B.J.6
  • 16
    • 0022480606 scopus 로고
    • Activities of antioxidant enzymes in muscle, liver and lung of chickens with inherited muscular dystrophy
    • Murphy ME, Kehrer JP (1986) Activities of antioxidant enzymes in muscle, liver and lung of chickens with inherited muscular dystrophy. Biochem Biophys Res Commun 134(2):550-556 (Pubitemid 16070533)
    • (1986) Biochemical and Biophysical Research Communications , vol.134 , Issue.2 , pp. 550-556
    • Murphy, M.E.1    Kehrer, J.P.2
  • 17
    • 0024369931 scopus 로고
    • Increased susceptibility to lipid peroxidation in skeletal muscles of dystrophic hamsters
    • Salminen A, Kihlstrom M (1989) Increased susceptibility to lipid peroxidation in skeletal muscles of dystrophic hamsters. Experientia 45(8):747-749 (Pubitemid 19198322)
    • (1989) Experientia , vol.45 , Issue.8 , pp. 747-749
    • Salminen, A.1    Kihlstrom, M.2
  • 18
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72:248-254
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 19
    • 84862869807 scopus 로고    scopus 로고
    • Analysis of calpain 3 protein in muscle biopsies of different muscular dystrophies from India
    • (in press)
    • Renjini R, Gayathri N, Nalini A, Srinivas Bharath MM (2011) Analysis of Calpain 3 protein in muscle biopsies of different muscular dystrophies from India. Indian J Med Res (in press)
    • (2011) Indian J Med Res
    • Renjini, R.1    Gayathri, N.2    Nalini, A.3    Srinivas Bharath, M.M.4
  • 20
    • 0029937563 scopus 로고    scopus 로고
    • Identification of a murine TEF-1-related gene expressed after mitogenic stimulation of quiescent fibroblasts and during myogenic differentiation
    • DOI 10.1074/jbc.271.23.13786
    • Hsu DK, Guo Y, Alberts GF, Copeland NG, Gilbert DJ, Jenkins NA, Peifley KA, Winkles JA (1996) Identification of a murine TEF-1-related gene expressed after mitogenic stimulation of quiescent fibroblasts and during myogenic differentiation. J Biol Chem 271(23):13786-13795 (Pubitemid 26187990)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.23 , pp. 13786-13795
    • Hsu, D.K.W.1    Guo, Y.2    Alberts, G.F.3    Copeland, N.G.4    Gilbert, D.J.5    Jenkins, N.A.6    Peifley, K.A.7    Winkles, J.A.8
  • 21
    • 4344638224 scopus 로고    scopus 로고
    • Glutathione depletion impairs myogenic differentiation of murine skeletal muscle C2C12 cells through sustained NF-κB activation
    • Ardite E, Barbera JA, Roca J, Fernandez-Checa JC (2004) Glutathione depletion impairs myogenic differentiation of murine skeletal muscle C2C12 cells through sustained NF-kappaB activation. Am J Pathol 165(3):719-728 (Pubitemid 39129280)
    • (2004) American Journal of Pathology , vol.165 , Issue.3 , pp. 719-728
    • Ardite, E.1    Barbera, J.A.2    Roca, J.3    Fernandez-Checa, J.C.4
  • 22
    • 36249019785 scopus 로고    scopus 로고
    • Integrating glutathione metabolism and mitochondrial dysfunction with implications for Parkinson's disease: A dynamic model
    • DOI 10.1016/j.neuroscience.2007.08.028, PII S0306452207010135
    • Vali S, Mythri RB, Jagatha B, Padiadpu J, Ramanujan KS, Andersen JK, Gorin F, Bharath MM (2007) Integrating glutathione metabolism and mitochondrial dysfunction with implications for Parkinson's disease: a dynamic model. Neuroscience 149(4):917-930. doi:10.1016/j.neuroscience.2007.08.028 (Pubitemid 350130291)
    • (2007) Neuroscience , vol.149 , Issue.4 , pp. 917-930
    • Vali, S.1    Mythri, R.B.2    Jagatha, B.3    Padiadpu, J.4    Ramanujan, K.S.5    Andersen, J.K.6    Gorin, F.7    Bharath, M.M.S.8
  • 23
    • 0037108921 scopus 로고    scopus 로고
    • Semi-quantitative estimation of heme/hemoprotein with dichlorodihydrofluorescin diacetate
    • DOI 10.1016/S0003-2697(02)00248-8, PII S0003269702002488
    • Ohashi T, Kakimoto K, Sokawa Y, Taketani S (2002) Semiquantitative estimation of heme/hemoprotein with dichlorodihy-drofluorescin diacetate. Anal Biochem 308(2):392-395 (Pubitemid 35177155)
    • (2002) Analytical Biochemistry , vol.308 , Issue.2 , pp. 392-395
    • Ohashi, T.1    Kakimoto, K.2    Sokawa, Y.3    Taketani, S.4
  • 24
    • 77950296916 scopus 로고    scopus 로고
    • Bioconjugates of curcumin display improved protection against glutathione depletion mediated oxidative stress in a dopaminergic neuronal cell line: Implications for parkinson's disease
    • doi:10.1016/j.bmc.2010.02.029
    • Harish G, Venkateshappa C, Mythri RB, Dubey SK, Mishra K, Singh N, Vali S, Bharath MM (2010) Bioconjugates of curcumin display improved protection against glutathione depletion mediated oxidative stress in a dopaminergic neuronal cell line: implications for Parkinson's disease. Bioorg Med Chem 18(7):2631-2638. doi:10.1016/j.bmc.2010.02.029
    • (2010) Bioorg Med Chem , vol.18 , Issue.7 , pp. 2631-2638
    • Harish, G.1    Venkateshappa, C.2    Mythri, R.B.3    Dubey, S.K.4    Mishra, K.5    Singh, N.6    Vali, S.7    Bharath, M.M.8
  • 25
    • 0032947765 scopus 로고    scopus 로고
    • Expression of matrix metalloproteinases 2 and 9 in regenerating skeletal muscle: A study in experimentally injured and mdx muscles
    • DOI 10.1006/dbio.1998.9107
    • Kherif S, Lafuma C, Dehaupas M, Lachkar S, Fournier JG, Verdiere-Sahuque M, Fardeau M, Alameddine HS (1999) Expression of matrix metalloproteinases 2 and 9 in regenerating skeletal muscle: a study in experimentally injured and mdx muscles. Dev Biol 205(1):158-170. doi:10.1006/dbio.1998.9107 (Pubitemid 29042665)
    • (1999) Developmental Biology , vol.205 , Issue.1 , pp. 158-170
    • Kherif, S.1    Lafuma, C.2    Dehaupas, M.3    Lachkar, S.4    Fournier, J.-G.5    Verdiere-Sahuque, M.6    Fardeau, M.7    Alameddine, H.S.8
  • 26
    • 0018384650 scopus 로고
    • Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction
    • DOI 10.1016/0003-2697(79)90738-3
    • Ohkawa H, Ohishi N, Yagi K (1979) Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction. Anal Biochem 95(2):351-358 (Pubitemid 9194347)
    • (1979) Analytical Biochemistry , vol.95 , Issue.2 , pp. 351-358
    • Ohkawa, H.1    Ohishi, N.2    Yagi, K.3
  • 27
    • 79961207643 scopus 로고    scopus 로고
    • Evaluation of markers of oxidative stress, antioxidant function and astrocytic proliferation in the striatum and frontal cortex of Parkinson's disease brains
    • doi:10.1007/s11064-011-0471-9
    • Mythri RB, Venkateshappa C, Harish G, Mahadevan A, Muthane UB, Yasha TC, Srinivas Bharath MM, Shankar SK (2011) Evaluation of markers of oxidative stress, antioxidant function and astrocytic proliferation in the striatum and frontal cortex of Parkinson's disease brains. Neurochem Res 36(8):1452-1463. doi:10.1007/s11064-011-0471-9
    • (2011) Neurochem Res , vol.36 , Issue.8 , pp. 1452-1463
    • Mythri, R.B.1    Venkateshappa, C.2    Harish, G.3    Mahadevan, A.4    Muthane, U.B.5    Yasha, T.C.6    Srinivas Bharath, M.M.7    Shankar, S.K.8
  • 29
    • 33846464996 scopus 로고    scopus 로고
    • Mitochondrial complex I inhibition in Parkinson's disease: How can curcumin protect mitochondria?
    • DOI 10.1089/ars.2006.1479
    • Mythri RB, Jagatha B, Pradhan N, Andersen J, Bharath MM (2007) Mitochondrial complex I inhibition in Parkinson's disease: how can curcumin protect mitochondria? Antioxid Redox Signal 9(3):399-408. doi:10.1089/ars.2007. 9.ft-25 (Pubitemid 46145986)
    • (2007) Antioxidants and Redox Signaling , vol.9 , Issue.3 , pp. 399-408
    • Mythri, R.B.1    Jagatha, B.2    Pradhan, N.3    Andersen, J.4    Bharath, M.M.S.5
  • 30
    • 33746546313 scopus 로고    scopus 로고
    • Increased oxidative stress in dystrophin deficient (mdx) mice masticatory muscles
    • 3rd ed edn. Cold spring Harbor Laboratory Press, New York
    • Sambrook J, Russell DW (2001) Molecular cloning, a laboratory manual, 3rd ed edn. Cold spring Harbor Laboratory Press, New York
    • (2001) Molecular Cloning, a Laboratory Manual
    • Sambrook, J.1    Russell, D.W.2
  • 31
    • 0037254750 scopus 로고    scopus 로고
    • Induction of oxidative stress in Rana ridibunda during recovery from winter hibernation
    • DOI 10.1016/S0306-4565(02)00031-1, PII S0306456502000311
    • Bagnyukova TV, Storey KB, Lushchak VI (2003) Induction of oxidative stress in Rana ridibunda during recovery from winter hibernation. J Therm Biol 28(1):21-28. doi:10.1016/s0306-4565(02)00031-1 (Pubitemid 36164273)
    • (2003) Journal of Thermal Biology , vol.28 , Issue.1 , pp. 21-28
    • Bagnyukova, T.V.1    Storey, K.B.2    Lushchak, V.I.3
  • 32
    • 0021318441 scopus 로고
    • Catalase in vitro
    • Aebi H (1984) Catalase in vitro. Methods Enzymol 105:121-126
    • (1984) Methods Enzymol , vol.105 , pp. 121-126
    • Aebi, H.1
  • 33
    • 0021288821 scopus 로고
    • Assays of glutathione peroxidase
    • Flohe L, Gunzler WA (1984) Assays of glutathione peroxidase. Methods Enzymol 105:114-121 (Pubitemid 14165378)
    • (1984) Methods in Enzymology , vol.105 , pp. 114-121
    • Flohe, L.1    Gunzler, W.A.2
  • 36
    • 0022300420 scopus 로고
    • Glutathione biosynthesis; γ-Glutamylcysteine synthetase from rat kidney
    • Seelig GF, Meister A (1985) Glutathione biosynthesis; gamma-glutamylcysteine synthetase from rat kidney. Methods Enzymol 113:379-390 (Pubitemid 16195807)
    • (1985) Methods in Enzymology , vol.113 , pp. 379-390
    • Foure Seelig, G.1    Meister, A.2
  • 37
    • 0031282148 scopus 로고    scopus 로고
    • Determination of thioredoxin reductase activity in rat liver supernatant
    • DOI 10.1006/abio.1997.2373
    • Hill KE, McCollum GW, Burk RF (1997) Determination of thioredoxin reductase activity in rat liver supernatant. Anal Biochem 253(1):123-125. doi:10.1006/abio.1997.2373 (Pubitemid 27490613)
    • (1997) Analytical Biochemistry , vol.253 , Issue.1 , pp. 123-125
    • Hill, K.E.1    McCollum, G.W.2    Burk, R.F.3
  • 38
    • 77952478110 scopus 로고    scopus 로고
    • Biochemical markers of muscular damage
    • doi: 10.1515/cclm.2010.179
    • Brancaccio P, Lippi G, Maffulli N (2010) Biochemical markers of muscular damage. Clin Chem Lab Med 48(6):757-767. doi: 10.1515/cclm.2010.179
    • (2010) Clin Chem Lab Med , vol.48 , Issue.6 , pp. 757-767
    • Brancaccio, P.1    Lippi, G.2    Maffulli, N.3
  • 41
    • 80051686721 scopus 로고    scopus 로고
    • Increased oxidative stress in dystrophin deficient (mdx) mice masticatory muscles
    • doi: 10.1016/j.etp.2010.04.006
    • Spassov A, Gredes T, Gedrange T, Pavlovic D, Lupp A, Kunert-Keil C (2010) Increased oxidative stress in dystrophin deficient (mdx) mice masticatory muscles. Exp Toxicol Pathol. doi: 10.1016/j.etp.2010.04.006
    • (2010) Exp Toxicol Pathol
    • Spassov, A.1    Gredes, T.2    Gedrange, T.3    Pavlovic, D.4    Lupp, A.5    Kunert-Keil, C.6
  • 42
    • 52049106413 scopus 로고    scopus 로고
    • Redox regulation of skeletal muscle
    • doi:10.1002/iub.72
    • Jackson MJ (2008) Redox regulation of skeletal muscle. IUBMB Life 60(8):497-501. doi:10.1002/iub.72
    • (2008) IUBMB Life , vol.60 , Issue.8 , pp. 497-501
    • Jackson, M.J.1
  • 43
    • 69149093028 scopus 로고    scopus 로고
    • Protection of dystrophic muscle cells with polyphenols from green tea correlates with improved glutathione balance and increased expression of 67LR, a receptor for (-)-epigallocatechin gallate
    • doi:10.1002/biof.34
    • Dorchies OM, Wagner S, Buetler TM, Ruegg UT (2009) Protection of dystrophic muscle cells with polyphenols from green tea correlates with improved glutathione balance and increased expression of 67LR, a receptor for (-)-epigallocatechin gallate. Biofactors 35(3):279-294. doi:10.1002/biof.34
    • (2009) Biofactors , vol.35 , Issue.3 , pp. 279-294
    • Dorchies, O.M.1    Wagner, S.2    Buetler, T.M.3    Ruegg, U.T.4
  • 44
    • 0025878107 scopus 로고
    • Glutathione depletion during experimental damage to rat skeletal muscle and its relevance to duchenne muscular dystrophy
    • Jackson MJ, Brooke MH, Kaiser K, Edwards RH (1991) Glutathione depletion during experimental damage to rat skeletal muscle and its relevance to Duchenne muscular dystrophy. Clin Sci (Lond) 80(6):559-564
    • (1991) Clin Sci (Lond) , vol.80 , Issue.6 , pp. 559-564
    • Jackson, M.J.1    Brooke, M.H.2    Kaiser, K.3    Edwards, R.H.4
  • 45
    • 79952700589 scopus 로고    scopus 로고
    • Effect of reactive oxygen and carbonyl species on crucial cellular antioxidant enzymes
    • doi:10.1016/j.cbi.2010.12.028
    • Lesgards JF, Gauthier C, Iovanna J, Vidal N, Dolla A, Stocker P (2011) Effect of reactive oxygen and carbonyl species on crucial cellular antioxidant enzymes. Chem Biol Interact 190(1):28-34. doi:10.1016/j.cbi.2010.12.028
    • (2011) Chem Biol Interact , vol.190 , Issue.1 , pp. 28-34
    • Lesgards, J.F.1    Gauthier, C.2    Iovanna, J.3    Vidal, N.4    Dolla, A.5    Stocker, P.6
  • 46
    • 68749103451 scopus 로고    scopus 로고
    • Mitochondrial abnormalities, energy deficit and oxidative stress are features of calpain 3 deficiency in skeletal muscle
    • doi:10.1093/hmg/ddp257
    • Kramerova I, Kudryashova E, Wu B, Germain S, Vandenborne K, Romain N, Haller RG, Verity MA, Spencer MJ (2009) Mitochondrial abnormalities, energy deficit and oxidative stress are features of calpain 3 deficiency in skeletal muscle. Hum Mol Genet 18(17):3194-3205. doi:10.1093/hmg/ddp257
    • (2009) Hum Mol Genet , vol.18 , Issue.17 , pp. 3194-3205
    • Kramerova, I.1    Kudryashova, E.2    Wu, B.3    Germain, S.4    Vandenborne, K.5    Romain, N.6    Haller, R.G.7    Verity, M.A.8    Spencer, M.J.9
  • 47
    • 0024515328 scopus 로고
    • Lipid peroxidation and superoxide dismutase activity in muscle and erythrocytes in adult muscular dystrophies and neurogenic atrophies
    • DOI 10.1007/BF00451007
    • Dioszeghy P, Imre S, Mechler F (1989) Lipid peroxidation and superoxide dismutase activity in muscle and erythrocytes in adult muscular dystrophies and neurogenic atrophies. Eur Arch Psychiatry Neurol Sci 238(3):175-177 (Pubitemid 19097635)
    • (1989) European Archives of Psychiatry and Neurological Sciences , vol.238 , Issue.3 , pp. 175-177
    • Dioszeghy, P.1    Imre, S.2    Mechler, F.3
  • 48
    • 78650755469 scopus 로고    scopus 로고
    • Histological assessment of SJL/J mice treated with the antioxidants coenzyme Q10 and resveratrol
    • doi:10.1016/j.micron.2010.10.001
    • Potgieter M, Pretorius E, Van der Merwe CF, Beukes M, Vieira WA, Auer RE, Auer M, Meyer S (2011) Histological assessment of SJL/J mice treated with the antioxidants coenzyme Q10 and resveratrol. Micron 42(3):275-282. doi:10.1016/j.micron.2010.10.001
    • (2011) Micron , vol.42 , Issue.3 , pp. 275-282
    • Potgieter, M.1    Pretorius, E.2    Van Der Merwe, C.F.3    Beukes, M.4    Vieira, W.A.5    Auer, R.E.6    Auer, M.7    Meyer, S.8
  • 49
    • 0036710567 scopus 로고    scopus 로고
    • Glutathione, iron and Parkinson's disease
    • DOI 10.1016/S0006-2952(02)01174-7, PII S0006295202011747
    • Bharath S, Hsu M, Kaur D, Rajagopalan S, Andersen JK (2002) Glutathione, iron and Parkinson's disease. Biochem Pharmacol 64(5-6):1037-1048 (Pubitemid 35232279)
    • (2002) Biochemical Pharmacology , vol.64 , Issue.5-6 , pp. 1037-1048
    • Bharath, S.1    Hsu, M.2    Kaur, D.3    Rajagopalan, S.4    Andersen, J.K.5
  • 50
    • 34147152905 scopus 로고    scopus 로고
    • The role of free radicals in the pathophysiology of muscular dystrophy
    • DOI 10.1152/japplphysiol.01145.2006
    • Tidball JG, Wehling-Henricks M (2007) The role of free radicals in the pathophysiology of muscular dystrophy. J Appl Physiol 102(4):1677-1686 (Pubitemid 46571068)
    • (2007) Journal of Applied Physiology , vol.102 , Issue.4 , pp. 1677-1686
    • Tidball, J.G.1    Wehling-Henricks, M.2
  • 52
    • 58149151370 scopus 로고    scopus 로고
    • MicroRNA-206 is highly expressed in newly formed muscle fibers: Implications regarding potential for muscle regeneration and maturation in muscular dystrophy
    • Yuasa K, Hagiwara Y, Ando M, Nakamura A, Takeda S, Hijikata T (2008) MicroRNA-206 is highly expressed in newly formed muscle fibers: implications regarding potential for muscle regeneration and maturation in muscular dystrophy. Cell Struct Funct 33(2):163-169
    • (2008) Cell Struct Funct , vol.33 , Issue.2 , pp. 163-169
    • Yuasa, K.1    Hagiwara, Y.2    Ando, M.3    Nakamura, A.4    Takeda, S.5    Hijikata, T.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.