Display options
Share it on

Biochemistry. 1990 Feb 06;29(5):1245-54. doi: 10.1021/bi00457a021.

Structural and functional features of the alpha 3 chain indicate a bridging role for chicken collagen VI in connective tissues.

Biochemistry

P Bonaldo, V Russo, F Bucciotti, R Doliana, A Colombatti

Affiliations

  1. Divisione di Oncologia Sperimentale 2, Centro di Riferimento Oncologico, Aviano, Italy.

PMID: 2322559 DOI: 10.1021/bi00457a021

Abstract

Type VI collagen is a component of 100 nm long periodic filaments with a widespread distribution around collagen fibers and on the surface of cells. It is an unusual collagen constituted by three distinct chains, one of which (alpha 3) is much larger than the others and is encoded by a 9-kb mRNA. The amino acid sequence of the alpha 3(VI) deduced from the present cDNA clones specifies for a multidomain protein of at least 2648 residues made of a short collagenous sequence (336 residues), flanked at the N-terminus by nine 200 residue long repeating motifs and at the C-terminus by two similar motifs that share extensive identities with the collagen-binding type A repeats of von Willebrand factor. Type VI collagen and alpha 3(VI) fusion proteins bound to insolubilized type I collagen in a specific, time-dependent, and saturable manner. The alpha 3(VI) chain has three Arg-Gly-Asp sequences in the collagenous domain, and cell attachment was stimulated by the triple helix of type VI collagen and by alpha 3(VI) fusion proteins containing Arg-Gly-Asp sequences. This function was specifically inhibited by the Arg-Gly-Asp-Ser synthetic peptide. The type I collagen-binding and the cell-attachment properties of the alpha 3(VI) chain provide direct information for the role of type VI collagen in connective tissues.

Similar articles

Cited by

Giusti B, Pepe G.
Front Aging Neurosci. 2016 Oct 20;8:237. doi: 10.3389/fnagi.2016.00237. eCollection 2016.
PMID: 27812333

Substances

MeSH terms

Publication Types

LinkOut - more resources