Rapid induction of polyadenylate binding protein and stimulation of translational initiation in pituitary tumor cells exposed to phorbol ester.

1. GH3 pituitary cells treated for 1-2 hr with phorbol myristate acetate exhibited accumulation of large polysomes and increased incorporation of amino acids into all discrete protein populations. 2. Preferential incorporation into a basic 74 kDa polypeptide preceded significant augmentation of protein synthesis. Cellular content of this polypeptide correlated directly with the increase in protein synthesis. 3. Stimulations of incorporation, of polysome accumulation, and of preferential synthesis of the 74 kDa protein were eliminated by inhibitors of transcription. 4. The rapidly induced protein was identical with the ubiquitous polyadenylate-binding protein on the bases of size, isoelectric point, distribution with polysomes, and association with poly(A) + mRNA.