Open AccessReceptor- and heparin-binding domains of basic fibroblast growth factor.
Author(s) -
Andrew Baird,
David Schubert,
Nicholas Ling,
Roger Guillemin
Publication year - 1988
Publication title -
proceedings of the national academy of sciences of the united states of america
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 5.011
H-Index - 771
eISSN - 1091-6490
pISSN - 0027-8424
DOI - 10.1073/pnas.85.7.2324
Subject(s) - fibroblast growth factor , fibroblast growth factor receptor 3 , fibroblast growth factor receptor 4 , epidermal growth factor , fibroblast growth factor receptor 2 , fibroblast growth factor receptor , microbiology and biotechnology , dna synthesis , receptor , fibronectin , growth factor , biology , growth factor receptor inhibitor , biological activity , basic fibroblast growth factor , 3t3 cells , biochemistry , chemistry , cell , in vitro , transfection , gene
Two functional domains in the primary structure of basic fibroblast growth factor (FGF) have been identified on the basis of their ability to interact with the FGF receptor, bind radiolabeled heparin, and modulate the cellular response to FGF. Peptides derived from these two functional domains can act as partial agonists and antagonists in biological assays of FGF activity. Peptides related to the sequences of FGF-(24-68)-NH2 and FGF-(106-115)-NH2 inhibit thymidine incorporation into 3T3 fibroblasts when they are stimulated by FGF but have no effect when the cells are treated with either platelet-derived growth factor or epidermal growth factor. They also possess partial agonist activity and can stimulate DNA synthesis when tested in the absence of exogenous FGF. The active peptides have no effect on the binding of epidermal growth factor to its receptor on A431 cells and they can modulate the effects of FGF, but not fibronectin, on endothelial cell adhesion. The results suggest the possibility of designing specific analogs of FGF that are capable of inhibiting the biological effects of FGF.