TGF-β1 differentially modulates the collagen VI α5 and α6 chains in human tendon cultures

P Sabatelli, F Sardone, F Traina, L Merlini, S Santi, R Wagener, C Faldini

Article ID: 6583
Vol 30, Issue 4S1, 2016
DOI: https://doi.org/10.54517/jbrha6583
Received: 8 January 2017; Accepted: 8 January 2017; Available online: 8 January 2017; Issue release: 8 January 2017

Abstract

Collagen VI is a microfibrillar collagen with a potential regulatory role in tendon repair mechanism. We studied the expression of collagen VI α5 and α6 chains in normal human tendon fibroblast cultures, both under basal condition and in response to TGF-β1, a potent regulator of tendon healing. Under basal condition, we found that the α5 chain was expressed, although to a lesser extent with respect to the α3 chain; in contrast, the α6 chain was absent. The treatment with TGFβ1 induced an opposite effect on the expression of the α5 and α6 chains; in fact, while the α5 chain was dramatically reduced, the α6 chain was induced and released in the culture medium. These data indicate that collagen VI α5 and α6 chains are differentially involved in tendon matrix homeostasis. The α6 chain may represent a new potential biomarker for monitoring TGFβ1-related events in tendon, as healing and fibrotic scar formation.


Keywords

collagen VI;transforming growth factor b1;endon;myotendinous junctions


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