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., ...Daha Fazla

JOURNAL OF CELLULAR PHYSIOLOGY, cilt.206, sa.1, ss.160-166, 2006 (SCI-Expanded) identifier identifier identifier

  • Yayın Türü: Makale / Tam Makale
  • Cilt numarası: 206 Sayı: 1
  • Basım Tarihi: 2006
  • Doi Numarası: 10.1002/jcp.20443
  • Dergi Adı: JOURNAL OF CELLULAR PHYSIOLOGY
  • Derginin Tarandığı İndeksler: Science Citation Index Expanded (SCI-EXPANDED), Scopus
  • Sayfa Sayıları: ss.160-166
  • Gazi Üniversitesi Adresli: Evet

Özet

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.