
Evidence and characterization of the receptor to eye-derived growth factor I, the retinal form of basic fibroblast growth factor, on bovine epithelial lens cells.
Author(s) -
Michel Moenner,
Bruno Chevallier,
Josette Badet,
Denis Barritault
Publication year - 1986
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.83.14.5024
Subject(s) - receptor , growth factor , fibroblast growth factor , fibroblast growth factor receptor 3 , insulin like growth factor 2 receptor , retinal , biology , biophysics , cell surface receptor , fibroblast growth factor receptor , basic fibroblast growth factor , biochemistry , chemistry , insulin like growth factor 1 receptor
Eye-derived growth factor I (EDGF-I), the retinal form of the basic fibroblast growth factor, has been purified to homogeneity from bovine retina by heparin-Sepharose chromatography. The radioiodinated EDGF-I retained full mitogenic activity and was used to study the interaction of the growth factor with bovine epithelial lens cells. We showed that 125I-labeled EDGF-I bound in a saturable and reversible manner to a specific cellular receptor. Scatchard analysis of the equilibrium binding gave a Kd of 53 X 10(-12) M with approximately equal to 20,000 binding sites per cell. Crosslinking experiments using two homobifunctional reagents induced the formation of a specific major complex with a Mr of approximately equal to 145,000, as determined by NaDodSO4/PAGE, and independent of reducing conditions. These data establish the existence of a receptor for the basic growth factor derived from neural tissues and give an estimation of the size of this receptor at Mr 130,000.