The DOI matches its Crossref record; 36 of the 36 references it cites were found in a registry or an index.
The 12th–14th type III repeats of fibronectin function as a highly promiscuous growth factor-binding domain
Open accessAbstract
It has recently been shown that some growth factors (GFs) have strong interactions with nonproteoglycan extracellular matrix proteins. Relevant here, the 12th-14th type three repeats of fibronectin (FN III12-14) have been shown to bind insulin-like growth factor binding-protein-3, fibroblast growth factor (FGF)-2, and vascular endothelial growth factor (VEGF)-A with high affinity. Since FN III12-14 is known to bind GFs from different families, we hypothesized that this domain could be highly promiscuous in its GF-binding capacity. We used biochemical approaches and surface plasmon resonance to investigate such interactions with recombinant FN III12-14. We found that FN III12-14 binds most of the GFs from the platelet-derived growth factor (PDGF)/VEGF and FGF families and some GFs from the transforming growth factor-β and neurotrophin families, with K(D) values in the nanomolar range, without inhibiting GF activity. Overall, 25 new binding interactions were identified. In a clinically relevant fibrin matrix, a fibrin-binding variant of FN III12-14 was highly effective as a GF delivery system. For instance, in matrices functionalized with FN III12-14, PDGF-BB-induced sprouting of human smooth muscle cell spheroids was greatly enhanced. We show that FN III12-14 is a highly promiscuous ligand for GFs and also holds great potential in clinical healing applications.
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Metadata
- Authors
- Martino, M. M., & Hubbell, J. A.
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2010-12
- Volume
- 24
- Issue
- 12
- Pages
- 4711-4721
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2151810131
- Cited by
- 316
- References
- 36
- FWCI
- 10.32
- Type
- journal article
- Language
- en
- Open access
- green
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