title: Purification of an active receptor for acidic and basic fibroblast growth factor from bovine retina.
abstract: Acidic and basic fibroblast growth factors (FGFs) influence cell division and differentiation in retina cells. Their effects are thought to be mainly mediated through stimulation of a specific membrane receptor and subsequent generation of an intracellular signal pathway. In this study, we purified a FGF receptor of 130 kDa from bovine neural retina using wheat germ agglutinin affinity chromatography followed by FGF-affinity chromatography. The isolated receptor showed ligand binding activity with dissociation constants of 0.8 nM and 2 nM for aFGF and bFGF, respectively. Furthermore, binding of aFGF and bFGF to purified receptor resulted in self-phosphorylation, demonstrating that the isolated receptor had an unaltered intrinsic kinase activity.
authors.affiliation: Unité de Recherches Gérontologiques, INSERM U118, Paris, France.
authors.forename: A
authors.initials: A
authors.lastname: Torriglia
authors.forename: P R
authors.initials: PR
authors.lastname: Blanquet
mesh_terms: D000818:Animals; D002417:Cattle; D004789:Enzyme Activation; D016220:Fibroblast Growth Factor 1 / Q000378:metabolism*; D016222:Fibroblast Growth Factor 2 / Q000378:metabolism*; D011494:Protein Kinases / Q000378:metabolism; D017468:Receptors, Fibroblast Growth Factor / Q000302:isolation & purification* / Q000378:metabolism; D012160:Retina / Q000378:metabolism*
chemical_list: D017468:Receptors, Fibroblast Growth Factor; D016222:Fibroblast Growth Factor 2; D016220:Fibroblast Growth Factor 1; D011494:Protein Kinases