Phosphorylation and lipocortin-like activity of a 34-kD surface protein in lens epithelial cells: relation to mitogenesis induced by basic fibroblast growth factor.

In order to elucidate the molecular mechanism whereby basic fibroblast growth factor (bFGF) exerts its action on cell proliferation, we investigated the possible relationship between the mitogenic response to bFGF of bovine lens epithelial cells and the phosphorylation and phospholipase A2 (PLA2) activity of a 34-kD protein (p34) present in the basal plasma membrane of these cells. When p34 was obtained from the peripheral epithelial cells which were not capable of being stimulated with bFGF, pretreatment with bFGF led to decreased phosphorylation and PLA2 activity of p34. In contrast, both an increased phosphorylation of p34 and a strong activation of PLA2 occurred when p34 was derived from the central epithelium which was induced to proliferate in the presence of bFGF. It is hypothesized that p34 might play a key role as part of signal transduction of bFGF in controlling DNA synthesis of bovine lens epithelial cells.