Influence of fibroblast growth factor on phosphorylation and activity of a 34 kDa lipocortin-like protein in bovine epithelial lens cells

We examined the effect of basic fibroblast growth factor (FGF) on phosphorylation and lipocortin-like activity of the 34 kDa protein present in the basal membrane of epithelial peripheral cells which initiate growth and differentiation in the bovine lens. We found that: (i) the 34 kDa protein possesses anti-phospholipase A2 (PLA2) activity of lipocortin; (ii) in response to FGF, the anti-PLA2 activity of this protein is enhanced whereas its phosphorylation is markedly decreased. It is suggested that the 34 kDa protein might represent an important biological activity in controlling FGF induction of growth and differentiation in the adult eye lens.