Prostaglandin F2α (PGF2α), a mitogen for resting Swiss 3T3 cells, rapidly stimulates phosphorylation of an 80 kDa protein (80 K). 1-Oleoyl-2-acetylglycerol (OAG) and 12-O-tetradecanoyl phorbol-13-acetate (TPA) both protein kinase C (PKC) activators, also elicit 80 K phosphorylation. In contrast PGE1, PGE2 or PGF2β, which are non-mitogenic in these cells, had tittle or no action on this event. However PGE1 and PGE2 potentiate the PGF2α proliferative effect but do not enhance its action on 80 K phosphorylation. These results suggest that PGF2α mitogenic induction involves PKC signalling pathway activation while its enhancement by PGE1 or PGE2 occurs through a different mechanism(s).