Universität zu Köln

Tagliavini, F., Pellegrini, C., Sardone, F., Squarzoni, S., Paulsson, M., Wagener, R., Gualandi, F., Trabanelli, C., Ferlini, A., Merlini, L., Santi, S., Maraldi, N. M., Faldini, C. and Sabatelli, P. (2014). Defective collagen VI alpha 6 chain expression in the skeletal muscle of patients with collagen VI-related myopathies. Biochim. Biophys. Acta-Mol. Basis Dis., 1842 (9). S. 1604 - 1613. AMSTERDAM: ELSEVIER SCIENCE BV. ISSN 1879-260X

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Abstract

Collagen VI is a non-fibrillar collagen present in the extracellular matrix (ECM) as a complex polymer; the mainly expressed form is composed of alpha 1, alpha 2 and alpha 3 chains; mutations in genes encoding these chains cause myopathies known as Ullrich congenital muscular dystrophy (UCMD), Bethlem myopathy (BM) and myosclerosis myopathy (MM). The collagen VI alpha 6 chain is a recently identified component of the ECM of the human skeletal muscle. Here we report that the alpha 6 chain was dramatically reduced in skeletal muscle and muscle cell cultures of genetically characterized UCMD, BM and MM patients, independently of the clinical phenotype, the gene involved and the effect of the mutation on the expression of the classical alpha 1 alpha 2 alpha 3 heterotrimer. By contrast, the collagen VI alpha 6 chain was normally expressed or increased in the muscle of patients affected by other forms of muscular dystrophy, the overexpression matching with areas of increased fibrosis. In vitro treatment with TOE-beta 1, a potent collagen inducer, promoted the collagen VI a6 chain deposition in the ECM of normal muscle cells, whereas, in cultures derived from collagen VI-related myopathy patients, the collagen VI a6 chain failed to develop a network outside the cells and accumulated in the endoplasmic reticulum. The defect of the a6 chain points to a contribution to the pathogenesis of collagen VI-related disorders. (C) 2014 The Authors. Published by Elsevier B.V.

Item Type:	Journal Article
Creators:	Creators Email ORCID ORCID Put Code Tagliavini, F. UNSPECIFIED UNSPECIFIED UNSPECIFIED Pellegrini, C. UNSPECIFIED UNSPECIFIED UNSPECIFIED Sardone, F. UNSPECIFIED UNSPECIFIED UNSPECIFIED Squarzoni, S. UNSPECIFIED UNSPECIFIED UNSPECIFIED Paulsson, M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Wagener, R. UNSPECIFIED UNSPECIFIED UNSPECIFIED Gualandi, F. UNSPECIFIED UNSPECIFIED UNSPECIFIED Trabanelli, C. UNSPECIFIED UNSPECIFIED UNSPECIFIED Ferlini, A. UNSPECIFIED UNSPECIFIED UNSPECIFIED Merlini, L. UNSPECIFIED UNSPECIFIED UNSPECIFIED Santi, S. UNSPECIFIED UNSPECIFIED UNSPECIFIED Maraldi, N. M. UNSPECIFIED UNSPECIFIED UNSPECIFIED Faldini, C. UNSPECIFIED UNSPECIFIED UNSPECIFIED Sabatelli, P. UNSPECIFIED UNSPECIFIED UNSPECIFIED
URN:	urn:nbn:de:hbz:38-431039
DOI:	10.1016/j.bbadis.2014.05.033
Journal or Publication Title:	Biochim. Biophys. Acta-Mol. Basis Dis.
Volume:	1842
Number:	9
Page Range:	S. 1604 - 1613
Date:	2014
Publisher:	ELSEVIER SCIENCE BV
Place of Publication:	AMSTERDAM
ISSN:	1879-260X
Language:	English
Faculty:	Unspecified
Divisions:	Unspecified
Subjects:	no entry
Uncontrolled Keywords:	Keywords Language AUTOSOMAL-DOMINANT MYOPATHY; MUSCULAR-DYSTROPHY; BETHLEM MYOPATHY; MUTATIONS; AUTOPHAGY; MOUSE; MODEL; CONTRACTURES; STABILITY; FILAMENTS Multiple languages Biochemistry & Molecular Biology; Biophysics; Cell Biology Multiple languages
URI:	http://kups.ub.uni-koeln.de/id/eprint/43103