ABSTRACT
Eye derived growth factor II (EDGF II), the retinal form of acidic fibroblast growth factor (aFGF) is present in rod outer segments (ROS) purified in the dark, which display higher EDGF specific activity than all other parts of the retina. EDGF binds to ROS disc membranes upon illumination. This binding is not reversible in the dark. ATP, but not GTP, readily releases EDGF from either dark-adapted or previously bleached ROS. The release of EDGF activity from ROS membranes would require a phosphorylation mechanism since AMP-PNP, an ATP analogue, is not efficient. ROS membranes compete with cellular EDGF receptors of retinal pigment epithelial cells in vitro for the binding of labelled EDGF II, suggesting that they also possess specific binding sites. These data suggest that EDGF II is involved in photoreceptor cell biology.
