Selection of Peptide Ligands Binding to Fibroblast Growth Factor Receptor 1

Selection of peptide ligands binding to fibroblast growth factor receptor 1.

Inappropriate expression of fibroblast growth factors (FGFs) or activation of FGF receptors (FGFRs) could contribute to several human angiogenic pathologies. In an attempt to design antagonists of FGF, we developed a screening procedure for identifying peptide ligands binding to FGFR1. To retain the natural conformation of FGFR1 during screening, we expressed recombinant FGFR1 on the surface of...

Structural interactions of fibroblast growth factor receptor with its ligands.

Fibroblast growth factors (FGFs) effect cellular responses by binding to FGF receptors (FGFRs). FGF bound to extracellular domains on the FGFR in the presence of heparin activates the cytoplasmic receptor tyrosine kinase through autophosphorylation. We have crystallized a complex between human FGF1 and a two-domain extracellular fragment of human FGFR2. The crystal structure, determined by mult...

identification of new peptide ligands for epidermal growth factor receptor using phage display technology

Fibroblast Growth Factor-1 vs. Fibroblast Growth Factor-2 in Ischemic Skin Flap Survival in a Rat Animal Model

BACKGROUND One of the main challenges in skin flap surgery is tissue ischemia and following necrosis. The present study compares the effects of fibroblast growth factors 1 and 2 on increasing cutaneous vasculature, improving ischemia, and preventing distal necrosis in ischemic skin flaps in rat model. METHODS Thirty rats were allocated into 3 groups (n=10) and 2×8 cm dorsal rando...

N-glycosylation of fibroblast growth factor receptor 1 regulates ligand and heparan sulfate co-receptor binding.

The regulation of cell function by fibroblast growth factors (FGF) occurs through a dual receptor system consisting of a receptor-tyrosine kinase, FGFR and the glycosaminoglycan heparan sulfate (HS). Mutations of some potential N-glycosylation sites in human fgfr lead to phenotypes characteristic of receptor overactivation. To establish how N-glycosylation may affect FGFR function, soluble- and...