PL EN


Preferences help
enabled [disable] Abstract
Number of results
2005 | 52 | 2 | 449-452
Article title

The involvement of oxidative stress in determining the severity and progress of pathological processes in dystrophin-deficient muscles.

Content
Title variants
Languages of publication
EN
Abstracts
EN
In both forms of muscular dystrophy, the severe Duchenne’s muscular dystrophy (DMD) with lifespan shortened to about 20 years and the milder Becker dystrophy (BDM) with normal lifespan, the gene defect is located at chromosome locus Xp21. The location is the same in the experimental model of DMD in the mdx mice. As the result of the gene defect a protein called dystrophin is either not synthesized, or is produced in traces. Although the structure of this protein is rather well established there are still many controversies about the dystrophin function. The most accepted suggestion supposes that it stabilizes sarcolemma in the course of the contraction-relaxation cycle. Solving the problem of dystrophin function is a prerequisite for introduction of an effective therapy. Among the different factors which might be responsible for the appearance and progress of dystrophic changes in muscles there is an excessive action of oxidative stress. In this review data indicating the influence of oxidative stress on the severity of the pathologic processes in dystrophy are discussed. Several pieces of data indicating the action of oxidative damage to different macromolecules in DMD/BDM are presented. Special attention is devoted to the degree of oxidative damage to muscle proteins, the activity of neuronal nitric oxide synthase (nNOS) and their involvement in defining the severity of the dystrophic processes. It is indicated that the severity of the morbid process is related to the degree of oxidative damage to muscle proteins and the decrease of the nNOS activity in muscles. Estimation of the degree of the destructive action of oxidative stress in muscular dystrophy may be a useful marker facilitating introduction of an effective antioxidant therapy and regulation of nNOS activity.
Year
Volume
52
Issue
2
Pages
449-452
Physical description
Dates
published
2005
received
2005-01-06
revised
2005-05-06
accepted
2005-05-25
References
  • Bredt DS (1999) Endogenous nitric oxide synthesis: biological functions and pathophysiology. Free Radic Res 31: 577-596.
  • Brenman JE, Chao DS, Xia H, Aldape K, Bredt DS (1995) Nitric oxide synthase complexed with dystrophin and absent from skeletal muscle sarcolemma in Duchenne muscular dystrophy. Cell 82: 743-752.
  • Brown RH (1995) Free radicals, programmed death and muscular dystrophy. Curr Opin Neurol 8: 373-378.
  • Chang WJ, Iannaccone ST, Lau KS, Masters BS, McCabe TJ, McMillan K, Padre RC, Spencer MJ, Tidball JG, Stull JT (1996) Neuronal nitric oxide synthase and dystrophin-deficient muscular dystrophy. Proc Nat Acad Sci USA 93: 9142-9147.
  • Crosbie RH (2001) NO vascular control in Duchenne muscular dystrophy. Nat Med 7: 27-29.
  • Degl’Innocenti D, Pieri A, Rosati F, Ramponi G (1999) Oxidative stress and calcium homeostasis in skin fibroblasts. IUBMB Life 48: 391-396.
  • Franco A, Lansman JB (1990) Calcium entry through stretch-inactivated ion channels in mdx myotubes. Nature 344: 670-673.
  • Gee SH, Madhavan R, Levinson SR, Caldwell JH, Sealock R, Froehner SC (1998) Interaction of muscle and brain sodium channels with multiple members of the syntrophin family of dystrophin-associated proteins. J Neurosci 18: 128-137.
  • Gucuyener K, Ergenekon E, Erbas D, Pinarli G, Serdaroglu A (2000) The serum nitric oxide levels in patients with Duchenne muscular dystrophy. Brain Dev 22: 181-183.
  • Haycock JW, Jones P, Harris JB, Mantle D (1996a) Differential susceptibility of human skeletal muscle proteins to free radical induced oxidative damage: a histochemical, immunocytochemical and electron microscopical study in vitro. Acta Neuropathol 92: 331-340.
  • Haycock JW, Mac Neil S, Jones PJ, Harris JB, Mantle D (1996b) Oxidative damage to muscle protein in Duchenne muscular dystrophy. NeuroReport 8: 357-361.
  • Haycock JW, Mac Neil S, Mantle D (1998a) Differential protein oxidation in Duchenne and Becker muscular dystrophy. NeuroReport 9: 2201-2207.
  • Hunter M, Ian S, Mohamed JB (1986b) Plasma antioxidants and lipid peroxidation products in Duchenne muscular dystrophy. Clin Chim Acta 255: 123-132.
  • Irintchev A, Wernig A (1987) Muscle damage and repair in voluntarily running mice: strain and muscle differences. Cell Tissue Res 249: 509-521.
  • 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: 277-280.
  • Kasai T, Abeyana K, Hashiguchi T, Fukunaga H, Osame M, Maruyama I (2004) Decreased total nitric oxide production in patients with Duchenne muscular dystrophy. J Biomed Sci 11: 534-537.
  • Koenig M, Monaco AP, Kunkel CM (1988) The complete sequence of dystrophin predicts a rod-shaped cytosketal protein. Cell 53: 219-228.
  • Kong J, Anderson JE (1999) Dystrophin is required for organizing large acetylocholine receptor aggregates. Brain Res 839: 298-304.
  • Levine RL, Williams JA, Stadman ER, Shacter E (1994) Carbonyl assays for determination of oxidatively modified proteins. Methods Enzymol 233: 346-357.
  • Matkovics B, Laszlo A, Szabo L (1982) A comparative study of superoxide dismutase, catalase and lipid peroxidation in red blood cells from muscular dystrophy patients and normal controls. Clin Chim Acta 118: 289-292.
  • Mechler F, Imre S, Dioszeghy P (1984) Lipid peroxidation and superoxide dismutase activity in muscle and erythrocytes in Duchenne muscular dystrophy. J Neurol Sci 63: 279-83.
  • Mendell JR, Engel WK, Derrer EC (1971) Duchenne muscular dystrophy: Functional ischemia reproduces characteristic lesions. Science 172: 1143-1145.
  • Murphy ME, Kehrer JP (1989) Oxidative stress and muscular dystrophy. Chem-Biol Interact 69: 101-178.
  • 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: 489-499.
  • Niebroj-Dobosz I, Fidziańska A, Hausmanowa-Petrusewicz I (2001) Does normal nitric oxide synthase prevent pathologic muscle changes in dystrophin deficiency? Basic Appl Myol 11: 105-110.
  • Niebroj-Dobosz I, Fidziańska A, Hausmanowa-Petrusewicz I (2002) Oxidative damage to muscle proteins in dystrophinopathies. Acta Myol 21: 12-17.
  • Ragusa RJ, Chow CK, Porter JD (1997) Oxidative stress as a potential pathogenic mechanism in animal model of Duchenne muscular dystrophy. Neuromuscul Disord 7: 379-380.
  • Rodrigues MCh, Tarnopolsky MA (2003) Patients with dystrophinopathy show evidence of increased oxidative stress. Free Radic Biol Med 34: 1217-1220.
  • Slater TF (1984) Free-radical mechanisms in tissue injury. Biochem J 222: 1-15.
  • Tidball JG, Lavergne B, Lau KS, Spencer MJ, Stull JT, Wehling M (1998) Mechanical loading regulates NOS expression and activity in developing and adult skeletal muscle. Am J Physiol 82: C260-266.
  • Wink DA, Hanbauer I, Krishna MC, DeGraff W, Gamson J, Mitchell JB (1993) Nitric oxide protects against cellular damage and cytotoxity from reactive oxygen species. Proc Natl Acad Sci USA 90: 9813-9817.
  • Wink DA, Cook JA, Pacelli R, Liebman J, Krishna MC, Mitchell JB (1995) Nitric oxide (NO) protects against cellular damage by reactive oxygen species. Toxicol Lett 82-83: 221-226.
  • Woodford FP, Whitehead TP (1998) Is measuring serum antioxidant capacity clinically useful? Ann Clin Biochem 35: 48-56.
  • Zubrzycka-Gaarn EE, Bulman DE, Karpati G, Burghes AH, Belfall B, Klamut HJ, Talbot J, Hodges RS, Ray PN, Worton RG (1988) The Duchenne muscular dystrophy gene product is localized in sarcolemma of human skeletal muscle. Nature 333: 466-469.
Document Type
Publication order reference
YADDA identifier
bwmeta1.element.bwnjournal-article-abpv52i2p449kz
Identifiers
JavaScript is turned off in your web browser. Turn it on to take full advantage of this site, then refresh the page.