Journal
MATRIX BIOLOGY
Volume 27, Issue 3, Pages 201-210Publisher
ELSEVIER
DOI: 10.1016/j.matbio.2007.10.003
Keywords
matrix assembly; TSG-6; fibronectin; CUB domains
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Funding
- Arthritis Research UK Funding Source: Medline
- Intramural NIH HHS [Z01 SC009172-03] Funding Source: Medline
- Wellcome Trust Funding Source: Medline
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Human plasma fibronectin binds with high affinity to the inflammation-induced secreted protein TSG-6. Fibronectin binds to the CUB-C domain of TSG-6 but not to its Link module. TSG-6 can thus act as a bridging molecule to facilitate fibronectin association with the TSG-6 Link module ligand thrombospondin-1. Fibronectin binding to TSG-6 is divalent cation-independent and is conserved in cellular fibronectins. Based on competition binding studies using recombinant and proteolytic fragments of ftbronectin, TSG-6 binding localizes to type III repeats 9-14 of fibronectin. This region of fibronectin contains the Arg-Gly-Asp sequence recognized by alpha 5 beta 1 integrin, but deletion of that sequence does not prevent TSG-6 binding, and TSG-6 does not inhibit cell adhesion on fibronectin substrates mediated by this integrin. This region of fibronectin is also involved in fibronectin matrix assembly, and addition of TSG-6 enhances exogenous and endogenous fibronectin matrix assembly by human fibroblasts. Therefore, TSG-6 is a high affinity ligand that can mediate fibronectin interactions with other matrix components and modulate some interactions of fibronectin with cells. (C) Published by Elsevier B.V./International Society of Matrix Biology.
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