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Collagen VI glycine mutations: perturbed assembly and a spectrum of clinical severity.
Pace, Rishika A; Peat, Rachel A; Baker, Naomi L; Zamurs, Laura; Mörgelin, Matthias; Irving, Melita; Adams, Naomi E; Bateman, John F; Mowat, David; Smith, Nicholas J C; Lamont, Phillipa J; Moore, Steven A; Mathews, Katherine D; North, Kathryn N; Lamandé, Shireen R.
Afiliación
  • Pace RA; Murdoch Childrens Research Institute and Department of Paediatrics, University of Melbourne, Royal Children's Hospital, Victoria, Australia.
Ann Neurol ; 64(3): 294-303, 2008 Sep.
Article en En | MEDLINE | ID: mdl-18825676
OBJECTIVE: The collagen VI muscular dystrophies, Bethlem myopathy and Ullrich congenital muscular dystrophy, form a continuum of clinical phenotypes. Glycine mutations in the triple helix have been identified in both Bethlem and Ullrich congenital muscular dystrophy, but it is not known why they cause these different phenotypes. METHODS: We studied eight new patients who presented with a spectrum of clinical severity, screened the three collagen VI messenger RNA for mutations, and examined collagen VI biosynthesis and the assembly pathway. RESULTS: All eight patients had heterozygous glycine mutations toward the N-terminal end of the triple helix. The mutations produced two assembly phenotypes. In the first patient group, collagen VI dimers accumulated in the cell but not the medium, microfibril formation in the medium was moderately reduced, and the amount of collagen VI in the extracellular matrix was not significantly altered. The second group had more severe assembly defects: some secreted collagen VI tetramers were not disulfide bonded, microfibril formation in the medium was severely compromised, and collagen VI in the extracellular matrix was reduced. INTERPRETATION: These data indicate that collagen VI glycine mutations impair the assembly pathway in different ways and disease severity correlates with the assembly abnormality. In mildly affected patients, normal amounts of collagen VI were deposited in the fibroblast matrix, whereas in patients with moderate-to-severe disability, assembly defects led to a reduced collagen VI fibroblast matrix. This study thus provides an explanation for how different glycine mutations produce a spectrum of clinical severity.
Asunto(s)

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Enfermedades del Colágeno / Predisposición Genética a la Enfermedad / Colágeno Tipo VI / Glicina / Distrofias Musculares / Mutación Límite: Humans / Male Idioma: En Revista: Ann Neurol Año: 2008 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Estados Unidos

Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Enfermedades del Colágeno / Predisposición Genética a la Enfermedad / Colágeno Tipo VI / Glicina / Distrofias Musculares / Mutación Límite: Humans / Male Idioma: En Revista: Ann Neurol Año: 2008 Tipo del documento: Article País de afiliación: Australia Pais de publicación: Estados Unidos