Growth stimulatory factor originally isolated from bovine brain and pituitary and found to stimulate DNA synthesis in cultured fibroblast cells. Isoln: D. Gospodarowicz, Nature 249, 123 (1974). Mitogenic effect on cultured cell lines and induction of amphibian limb regeneration in vivo: D. Gospodarowicz et al., Adv. Metab. Disord. 8, 301 (1975). Two closely related forms have been identified, known as basic (bFGF) and acidic (aFGF) fibroblast growth factors, having a total amino acid sequence homology of 55%. Both induce the proliferation and differentiation of a wide variety of cell types, including corneal and vascular endothelial cells, myoblasts, chondrocytes, osteoblasts and glial cells. FGF has neurotrophic and angiogenic activity and may play an important role in the wound healing process. Purification of bFGF from pituitary: D. Gospodarowicz, J. Biol. Chem. 250, 2515 (1975); from brain: D. Gospodarowicz et al., ibid. 253, 3736 (1978). Identification of aFGF from bovine brain: K. A. Thomas et al., ibid. 255, 5517 (1980). Comparison of fibroblast growth factors: S. K. Lemmon et al., J. Cell Biol. 95, 162 (1982). Purification and characterization of aFGF: K. A. Thomas et al., Proc. Natl. Acad. Sci. USA 81, 357 (1984). Identity of bFGF from brain and pituitary: D. Gospodarowicz et al., ibid. 6963. Amino acid sequence of bFGF: F. Esch et al., ibid. 82, 6507 (1985); of aFGF: G. Gimenez-Gallego et al., Science 230, 1385 (1985); F. Esch et al., Biochem. Biophys. Res. Commun. 133, 554 (1985). Possible identity of aFGF with endothelial cell growth factor (ECGF) and eye-derived growth factor-II (EDGF-II): A. B. Schreiber et al., J. Cell Biol. 101, 1623 (1985); of bFGF with macrophage-derived growth factor (MDGF): A. Baird et al., Biochem. Biophys. Res. Commun. 126, 358 (1985); of FGFs with retina-derived endothelial cell growth factors: A. Baird et al., Biochemistry 24, 7855 (1985). Cloning of cDNA for bovine bFGF: J. A. Abraham et al., Science 233, 545 (1986); for human bFGF: T. Kurokawa et al., FEBS Lett. 213, 189 (1987); M. Iwane et al., Biochem. Biophys. Res. Commun. 146, 470 (1987). Expression of a chemically synthesized gene for bioactive bovine aFGF: D. L. Linemeyer et al., Biotechnology 5, 960 (1987). Receptor binding study: G. Neufeld, D. Gospodarowicz: J. Biol. Chem. 261, 5631 (1986). FGF-like factors have been isolated from several human tumor cell lines: R. R. Lobb et al., Biochem. Biophys. Res. Commun. 139, 861 (1986); M. Klagsbrun et al., Proc. Natl. Acad. Sci. USA 83, 2448 (1986); D. Moscatelli et al., J. Cell. Physiol. 129, 273 (1986). FGF has also been shown to be structurally homologous to the protein products of several oncogenes: C. Dickson, G. Peters, Nature 326, 833 (1987); M. Taira et al., Proc. Natl. Acad. Sci. USA 84, 2980 (1987); P. Delli Bovi et al., Cell 50, 729 (1987). Review of tissue distribution and bioactivity of bFGF: A. Baird et al., Recent Prog. Horm. Res. 42, 143-205 (1986). Review of structural characterization and biological functions: D. Gospodarowicz et al., Endocr. Rev. 8, 95-114 (1987). Potential role in the control of pituitary and gonad development: D. Gospodarowicz, N. Ferrara, J. Steroid Biochem. 32, 183-191 (1989). Reviews: K. A. Thomas, G. Gimenez-Gallego, Trends Biochem. Sci. 11, 81-84 (1986); D. Gospodarowicz et al., Mol. Cell. Endocrinol. 46, 187-204 (1986); K. A. Thomas, FASEB J. 1, 434-440 (1987).