2010, Número 3
<< Anterior Siguiente >>
Rev Esp Med Quir 2010; 15 (3)
Distrofias musculares en México: un enfoque clínico, bioquímico y molecular
Coral VRM, López HLB, Ruano CLÁ, Gómez DB, Fernández VF, Bahena ME
Idioma: Español
Referencias bibliográficas: 28
Paginas: 152-160
Archivo PDF: 261.34 Kb.
RESUMEN
Las distrofias musculares son un conjunto de enfermedades que se distinguen por debilidad progresiva y desgaste muscular que generalmente provocan discapacidad. En conjunto, se originan por defectos en genes que codifican para proteínas sumamente importantes para el funcionamiento de las células musculares, las cuales se pueden dividir en proteínas de matriz extracelular, de membrana y de citoesqueleto. El estudio de caracterización molecular y funcional de estas proteínas ha inducido múltiples avances en el diagnóstico y tratamiento de las distrofias musculares; de igual manera, ha contribuido al conocimiento de los mecanismos celulares y moleculares que intervienen en el origen de estas enfermedades.
REFERENCIAS (EN ESTE ARTÍCULO)
Koenig M, Monaco AP, Kunkel LM. The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 1988;53(2):219-228.
Monaco AP, Bertelson CJ, Colletti-Feener C, Kunkel LM. Localization and cloning of Xp21 deletion breakpoints involved in muscular dystrophy. Hum Genet 1987;75(3):221-227.
Ray PN, Belfall B, Duff C, Logan C, et al. Cloning of the breakpoint of an X;21 translocation associated with Duchenne muscular dystrophy. Nature 1985;318(6047):672-675.
Thompson MW, Ray PN, Belfall B, Duff C, et al. Linkage analysis of polymorphisms within the DNA fragment XJ cloned from the breakpoint of an X;21 translocation associated with X linked muscular dystrophy. J Med Genet 1986;23(6):548-555.
Worton RG, Duff C, Sylvester JE, Schmickel RD, Willard HF. Duchenne muscular dystrophy involving translocation of the dmd gene next to ribosomal RNA genes. Science 1984;224(4656):1447-1449.
Cox GA, Phelps SF, Chapman VM, Chamberlain JS. New mdx mutation disrupts expression of muscle and nonmuscle isoforms of dystrophin. Nat Genet 1993;4(1):87-93.
Der Dunnen JT, Bakker E, Breteler EG, Pearson PL, van Ommen GJ. Direct detection of more than 50% of the Duchenne muscular dystrophy mutations by field inversion gels. Nature 1987;329(6140):640-642.
Koenig M, Hoffman EP, Bertelson CJ, Monaco AP, et al. Complete cloning of the Duchenne muscular dystrophy (DMD) cDNA and preliminary genomic organization of the DMD gene in normal and affected individuals. Cell 1987;50(3):509-517.
Kunkel LM, Monaco AP, Middlesworth W, Ochs HD, Latt SA. Specific cloning of DNA fragments absent from the DNA of a male patient with an X chromosome deletion. Proc Natl Acad Sci USA 1985;82(14):4778-4782.
Campbell KP. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 1995;80(5):675-679.
Ervasti JM, Ohlendieck K, Kahl SD, Gaver MG, Campbell KP. Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle. Nature 1990;345(6273):315-319.
Ibraghimov-Beskrovnaya O, Ervasti JM, Leveille CJ, Slaughter CA, Sernett SW, Campbell KP. Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature 1992;355(6362):696-702.
Ettinger AJ, Feng G, Sanes JR. epsilon-Sarcoglycan, a broadly expressed homologue of the gene mutated in limb-girdle muscular dystrophy 2D. J Biol Chem 1997;272(51):32534-32538.
Straub V, Ettinger AJ, Durbeej M, Venzke DP, et al. epsilonsarcoglycan replaces alpha-sarcoglycan in smooth muscle to form a unique dystrophin-glycoprotein complex. J Biol Chem 1999;274(39):27989-27996.
Crosbie RH, Heighway J, Venzke DP, Lee JC, Campbell KP. Sarcospan, the 25-kDa transmembrane component of the dystrophin-glycoprotein complex. J Biol Chem 1997;272(50):31221-31224.
Forrest SM, Cross GS, Speer A, Gardner-Medwin D, et al. Preferential deletion of exons in Duchenne and Becker muscular dystrophies. Nature 1987;329(6140):638-640.
Wapennar MC, Klevits T, Hart KA. A deletion hot spot in the Duchenne muscular dystrophy gene. Genomics 1988;2(2):10-18.
Chamberlain JS, Gibbs RA, Ranier JE, Nguyen PN, Caskey CT. Deletion screening of the Duchenne muscular dystrophy locus via multiplex DNA amplification. Nucleic Acids Res 1988;16(23):11141-11156.
Beggs AH, Hoffman EP, Snyder JR, Arahata K, et al. Exploring the molecular basis for variability among patients with Becker muscular dystrophy: dystrophin gene and protein studies. Am J Hum Genet 1991;49(1):54-67.
Coral-Vazquez R, Arenas D, Cisneros B, Peñaloza L, et al. Pattern of deletions of the dystrophin gene in Mexican Duchenne/Becker muscular dystrophy patients: the use of new designed primers for the analysis of the major deletion "hot spot" region. Am J Med Genet 1997;70(3):240-246.
Coral-Vazquez R, Arenas D, Cisneros B, Peñaloza L, et al. Analysis of dystrophin gene deletions in patients from the Mexican population with Duchenne/Becker muscular dystrophy. Arch Med Res 1993;24(1):1-6.
Lalic T, Vossen RH, Coffa J, Schouten JP, et al. Deletion and duplication screening in the DMD gene using MLPA. Eur J Hum Genet 2005;13(11):1231-1234.
López-Hernández LB, van Heusden D, Soriano-Ursúa MA, Figuera-Villanueva L, et al. Genotype-phenotype discordance in Duchenne muscular dystrophy patient due to a novel mutation: insights on to the shock absorber function of dystrophin. J Appl Genetics 2010 (enviado).
Monaco AP, Bertelson CJ, Liechti-Gallati S, Moser H, Kunkel LM. An explanation for the phenotypic differences between patients bearing partial deletions of the DMD locus. Genomics 1988;2(1):90-95.
Aartsma-Rus A, van Deutekom JC, Fokkema IF, van Ommen GJ, den Dunnen JT. Entries in the Leiden Duchenne muscular dystrophy mutation database: an overview of mutation types and paradoxical cases that confirm the reading-frame rule. Muscle Nerve 2006;34(2):135-144.
Muntoni F, Torelli S, Ferlini A. Dystrophin and mutations: one gene, several proteins, multiple phenotypes. Lancet Neurol 2003;2(12):731-740.
Coral-Vazquez RM, Rosas-Vargas H, Meza-Espinosa P, Mendoza I, et al. Severe congenital muscular dystrophy in a Mexican family with a new nonsense mutation (R2578X) in the laminin alpha-2 gene. J Hum Genet 2003;48(2):91-95.
Schwartz M, Hertz JM, Sveen ML, Vissing J. LGMD2I presenting with a characteristic Duchenne or Becker muscular dystrophy phenotype. Neurology 2005;64(9):1635-1637.