Ultrastructural defects of collagen VI filaments in an Ullrich syndrome patient with loss of the alpha 3(VI) N10-N7 domains


Squarzoni S., Sabatelli P., Bergamin N., Guicheney P., Demir E., Merlini L., ...More

JOURNAL OF CELLULAR PHYSIOLOGY, vol.206, no.1, pp.160-166, 2006 (SCI-Expanded) identifier identifier identifier

  • Publication Type: Article / Article
  • Volume: 206 Issue: 1
  • Publication Date: 2006
  • Doi Number: 10.1002/jcp.20443
  • Journal Name: JOURNAL OF CELLULAR PHYSIOLOGY
  • Journal Indexes: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Page Numbers: pp.160-166
  • Gazi University Affiliated: Yes

Abstract

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 alpha 3(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 alpha 3(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 alpha 3(VI) chain isoforms, containing also domains of the N10-N7 region, are required for assembling a proper collagen VI network in the extracellular matrix. J. Cell. Physiol. 206: 160-166, 2006. (c) 2005 Wiley-Liss, Inc.