Tenascin C Promiscuously Binds Growth Factors via Its Fifth Fibronectin Type III-Like DomainReportar como inadecuado




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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.



Autor: Laura De Laporte , Jeffrey J. Rice , Federico Tortelli, Jeffrey A. Hubbell

Fuente: http://plos.srce.hr/



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