The promotion of endothelial cell attachment and spreading using FNIII10 fused 
to VEGF-A165

Traub, S.; Morgner, J.; Martino, M. M.; Honing, S.; Swartz, M. A.; Wickström, S. A.; Hubbell, J. A.; Eming, S. A.

doi:10.1016/j.biomaterials.2013.04.050

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The promotion of endothelial cell attachment and spreading using FNIII10 fused to VEGF-A165

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Wickström, S. A.
Wickström – Skin Homeostasis and Ageing, Max Planck Research Groups, Max Planck Institute for Biology of Ageing, Max Planck Society;

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http://www.ncbi.nlm.nih.gov/pubmed/23683723
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引用

Traub, S., Morgner, J., Martino, M. M., Honing, S., Swartz, M. A., Wickström, S. A., Hubbell, J. A., & Eming, S. A. (2013). The promotion of endothelial cell attachment and spreading using FNIII10 fused to VEGF-A165. Biomaterials, 34(24), 5958-68. doi:10.1016/j.biomaterials.2013.04.050.

引用: https://hdl.handle.net/21.11116/0000-000B-6E3D-7

要旨

Synergy in the downstream signaling pathways of the vascular endothelial growth factor receptor-2 (VEGFR-2) and the integrin alphavbeta3 is critical for blood vessel formation. Thus, agents that activate both receptors could possess efficient pro-angiogenic potential. Here, we created a fibrin-binding bi-functional protein (FNIII10-VEGF) consisting of the 10th type III domain of fibronectin (FNIII10) fused to a plasmin-resistant VEGF-A165 mutant (VEGF) that potentiated angiogenic processes when compared to the effect of the separate molecules. FNIII10-VEGF was able to bind both VEGFR-2 and integrin alphavbeta3. Intriguingly, cell attachment and spreading to immobilized FNIII10-VEGF was significantly enhanced compared to individual FNIII10 or VEGF proteins. Delivery of immobilized FNIII10-VEGF by covalent linkage to a fibrin matrix significantly enhanced the angiogenic response in an in vivo wound healing assay compared to soluble VEGF. Unexpectedly, the angiogenic response to fibrin-immobilized FNIII10-VEGF was reduced in comparison to the pro-angiogenic effect of fibrin-immobilized VEGF. Collectively, findings of this study corroborate a critical role for a subtle balance of the integrin-VEGF interplay in angiogenesis and provide insight in how engineered growth factors in concert with biomaterial matrices may offer a potent molecular/material approach to harness these interactions for therapeutic angiogenesis.