TY - JOUR
T1 - Ultrastructural defects of collagen VI filaments in an Ullrich syndrome patient with loss of the α3(VI) N10-N7 domains
AU - Squarzoni, Stefano
AU - Sabatelli, Patrizia
AU - Bergamin, Natascha
AU - Guicheney, Pascale
AU - Demir, Ercan
AU - Merlini, Luciano
AU - Lattanzi, Giovanna
AU - Ognibene, Andrea
AU - Capanni, Cristina
AU - Mattioli, Elisabetta
AU - Columbaro, Marta
AU - Bonaldo, Paolo
AU - Maraldi, Nadir Mario
PY - 2006/1
Y1 - 2006/1
N2 - Ultrastructural alterations of collagen VI in cultured fibroblasts and reduced collagen VI immunostaining in the papillary dermis and endomysium were detected in a patient with a mild form of Ullrich congenital muscular dystrophy caused by a COL6A3 gene mutation. The patient had been previously demonstrated to express an α3(VI) chain shorter than normal due to skipping of the mutated exon. We show that collagen VI filaments are not organized in a normal network in the extracellular matrix secreted by patient's cultured fibroblasts. Moreover, we demonstrate that in this patient the α3(VI) chain is produced in lower amounts and it is almost exclusively represented by the shorter, alternatively spliced N6-C5 isoform. These results suggest that different α3(VI) chain isoforms, containing also domains of the N10-N7 region, are required for assembling a proper collagen VI network in the extracellular matrix.
AB - Ultrastructural alterations of collagen VI in cultured fibroblasts and reduced collagen VI immunostaining in the papillary dermis and endomysium were detected in a patient with a mild form of Ullrich congenital muscular dystrophy caused by a COL6A3 gene mutation. The patient had been previously demonstrated to express an α3(VI) chain shorter than normal due to skipping of the mutated exon. We show that collagen VI filaments are not organized in a normal network in the extracellular matrix secreted by patient's cultured fibroblasts. Moreover, we demonstrate that in this patient the α3(VI) chain is produced in lower amounts and it is almost exclusively represented by the shorter, alternatively spliced N6-C5 isoform. These results suggest that different α3(VI) chain isoforms, containing also domains of the N10-N7 region, are required for assembling a proper collagen VI network in the extracellular matrix.
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U2 - 10.1002/jcp.20443
DO - 10.1002/jcp.20443
M3 - Article
C2 - 15965965
AN - SCOPUS:28444496345
VL - 206
SP - 160
EP - 166
JO - Journal of cellular and comparative physiology
JF - Journal of cellular and comparative physiology
SN - 0021-9541
IS - 1
ER -