TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly.
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 thrombosp...
| Main Authors: | , , , , , , , , , |
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| Format: | Journal article |
| Language: | English |
| Published: |
2008
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| _version_ | 1826259551706415104 |
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| author | Kuznetsova, SA Mahoney, D Martin-Manso, G Ali, T Nentwich, H Sipes, J Zeng, B Vogel, T Day, A Roberts, D |
| author_facet | Kuznetsova, SA Mahoney, D Martin-Manso, G Ali, T Nentwich, H Sipes, J Zeng, B Vogel, T Day, A Roberts, D |
| author_sort | Kuznetsova, SA |
| collection | OXFORD |
| description | 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 fibronectin, TSG-6 binding localizes to type III repeats 9-14 of fibronectin. This region of fibronectin contains the Arg-Gly-Asp sequence recognized by alpha5beta1 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. |
| first_indexed | 2024-03-06T18:51:41Z |
| format | Journal article |
| id | oxford-uuid:1072a439-fe1e-41df-9c42-d0136277c639 |
| institution | University of Oxford |
| language | English |
| last_indexed | 2024-03-06T18:51:41Z |
| publishDate | 2008 |
| record_format | dspace |
| spelling | oxford-uuid:1072a439-fe1e-41df-9c42-d0136277c6392022-03-26T09:56:32ZTSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly.Journal articlehttp://purl.org/coar/resource_type/c_dcae04bcuuid:1072a439-fe1e-41df-9c42-d0136277c639EnglishSymplectic Elements at Oxford2008Kuznetsova, SAMahoney, DMartin-Manso, GAli, TNentwich, HSipes, JZeng, BVogel, TDay, ARoberts, DHuman 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 fibronectin, TSG-6 binding localizes to type III repeats 9-14 of fibronectin. This region of fibronectin contains the Arg-Gly-Asp sequence recognized by alpha5beta1 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. |
| spellingShingle | Kuznetsova, SA Mahoney, D Martin-Manso, G Ali, T Nentwich, H Sipes, J Zeng, B Vogel, T Day, A Roberts, D TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly. |
| title | TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly. |
| title_full | TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly. |
| title_fullStr | TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly. |
| title_full_unstemmed | TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly. |
| title_short | TSG-6 binds via its CUB_C domain to the cell-binding domain of fibronectin and increases fibronectin matrix assembly. |
| title_sort | tsg 6 binds via its cub c domain to the cell binding domain of fibronectin and increases fibronectin matrix assembly |
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