Tenascin C promiscuously binds growth factors via its fifth fibronectin type III-like domain.

Tenascin C (TNC) is an extracellular matrix protein that is upregulated during development as well as tissue remodeling. TNC is comprised of multiple independent folding domains, including 15 fibronectin type III-like (TNCIII) domains. The fifth TNCIII domain (TNCIII5) has previously been shown to b...

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Autores principales:	Laura De Laporte, Jeffrey J Rice, Federico Tortelli, Jeffrey A Hubbell
Formato:	article
Lenguaje:	EN
Publicado:	Public Library of Science (PLoS) 2013
Materias:	Medicine R Science Q
Acceso en línea:	https://doaj.org/article/0d11729b46f74c659bd939bb767b6f8f
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spelling	oai:doaj.org-article:0d11729b46f74c659bd939bb767b6f8f2021-11-18T07:48:50ZTenascin C promiscuously binds growth factors via its fifth fibronectin type III-like domain.1932-620310.1371/journal.pone.0062076https://doaj.org/article/0d11729b46f74c659bd939bb767b6f8f2013-01-01T00:00:00Zhttps://www.ncbi.nlm.nih.gov/pmc/articles/pmid/23637968/?tool=EBIhttps://doaj.org/toc/1932-6203Tenascin C (TNC) is an extracellular matrix protein that is upregulated during development as well as tissue remodeling. TNC is comprised of multiple independent folding domains, including 15 fibronectin type III-like (TNCIII) domains. The fifth TNCIII domain (TNCIII5) has previously been shown to bind heparin. Our group has shown that the heparin-binding fibronectin type III domains of fibronectin (FNIII), specifically FNIII12-14, possess affinity towards a large number of growth factors. Here, we show that TNCIII5 binds growth factors promiscuously and with high affinity. We produced recombinant fragments of TNC representing the first five TNCIII repeats (TNCIII1-5), as well as subdomains, including TNCIII5, to study interactions with various growth factors. Multiple growth factors of the platelet-derived growth factor (PDGF) family, the fibroblast growth factor (FGF) family, the transforming growth factor beta (TGF-β) superfamily, the insulin-like growth factor binding proteins (IGF-BPs), and neurotrophins were found to bind with high affinity to this region of TNC, specifically to TNCIII5. Surface plasmon resonance was performed to analyze the kinetics of binding of TNCIII1-5 with TGF-β1, PDGF-BB, NT-3, and FGF-2. The promiscuous yet high affinity of TNC for a wide array of growth factors, mediated mainly by TNCIII5, may play a role in multiple physiological and pathological processes involving TNC.Laura De LaporteJeffrey J RiceFederico TortelliJeffrey A HubbellPublic Library of Science (PLoS)articleMedicineRScienceQENPLoS ONE, Vol 8, Iss 4, p e62076 (2013)
institution	DOAJ
collection	DOAJ
language	EN
topic	Medicine R Science Q
spellingShingle	Medicine R Science Q Laura De Laporte Jeffrey J Rice Federico Tortelli Jeffrey A Hubbell Tenascin C promiscuously binds growth factors via its fifth fibronectin type III-like domain.
description	Tenascin C (TNC) is an extracellular matrix protein that is upregulated during development as well as tissue remodeling. TNC is comprised of multiple independent folding domains, including 15 fibronectin type III-like (TNCIII) domains. The fifth TNCIII domain (TNCIII5) has previously been shown to bind heparin. Our group has shown that the heparin-binding fibronectin type III domains of fibronectin (FNIII), specifically FNIII12-14, possess affinity towards a large number of growth factors. Here, we show that TNCIII5 binds growth factors promiscuously and with high affinity. We produced recombinant fragments of TNC representing the first five TNCIII repeats (TNCIII1-5), as well as subdomains, including TNCIII5, to study interactions with various growth factors. Multiple growth factors of the platelet-derived growth factor (PDGF) family, the fibroblast growth factor (FGF) family, the transforming growth factor beta (TGF-β) superfamily, the insulin-like growth factor binding proteins (IGF-BPs), and neurotrophins were found to bind with high affinity to this region of TNC, specifically to TNCIII5. Surface plasmon resonance was performed to analyze the kinetics of binding of TNCIII1-5 with TGF-β1, PDGF-BB, NT-3, and FGF-2. The promiscuous yet high affinity of TNC for a wide array of growth factors, mediated mainly by TNCIII5, may play a role in multiple physiological and pathological processes involving TNC.
format	article
author	Laura De Laporte Jeffrey J Rice Federico Tortelli Jeffrey A Hubbell
author_facet	Laura De Laporte Jeffrey J Rice Federico Tortelli Jeffrey A Hubbell
author_sort	Laura De Laporte
title	Tenascin C promiscuously binds growth factors via its fifth fibronectin type III-like domain.
title_short	Tenascin C promiscuously binds growth factors via its fifth fibronectin type III-like domain.
title_full	Tenascin C promiscuously binds growth factors via its fifth fibronectin type III-like domain.
title_fullStr	Tenascin C promiscuously binds growth factors via its fifth fibronectin type III-like domain.
title_full_unstemmed	Tenascin C promiscuously binds growth factors via its fifth fibronectin type III-like domain.
title_sort	tenascin c promiscuously binds growth factors via its fifth fibronectin type iii-like domain.
publisher	Public Library of Science (PLoS)
publishDate	2013
url	https://doaj.org/article/0d11729b46f74c659bd939bb767b6f8f
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Tenascin C promiscuously binds growth factors via its fifth fibronectin type III-like domain.

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