Laminin heparin-binding peptides bind to several growth factors and enhance diabetic wound healing
Ishihara J., Ishihara A., Fukunaga K., Sasaki K., White M.J.V., Briquez P.S., Hubbell J.A.Nature Communications, 2018
In this article, the authors show that multiple laminin isoforms promiscuously bind to growth factors with high affinity, through their heparin-binding domains located in the α chain laminin-type G (LG) domains. These domains also bind to syndecan cell-surface receptors, promoting attachment of fibroblasts and endothelial cells. The authors explore the application of these multifunctional laminin HBDs in wound healing in the type-2 diabetic mouse and demonstrate that covalent incorporation of laminin HBDs into fibrin matrices improve retention of GFs and significantly enhances the efficacy of vascular endothelial cell growth factor (VEGF-A165) and platelet-derived growth factor (PDGF-BB) in promoting wound healing in vivo, under conditions where the GFs alone in fibrin are inefficacious.
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