Thrombin-induced protein phosphorylation in resting platelets and fibroblasts: evidence for common post-receptor molecular events.

We have investigated the thrombin-stimulated protein phosphorylation associated with the activation of two cellular processes: 1) reinitiation of DNA synthesis in G0-arrested hamster fibroblasts and 2) stimulation of serotonin release in platelets. We found a rapid 4- to 6-fold increased phosphorylation of a peptide with apparent Mr = 27,000 in SDS-PAGE. In both cell systems, the 27,000 dalton phosphopeptide is cytosolic, is resolved by isoelectric focusing as multiple variants (pHi 5 to 6), and thrombin stimulation generates the most acidic phosphorylated forms. This result and the fact that the 27,000 dalton peptide is also stimulated by a variety of growth factors in fibroblasts, strongly suggests that thrombin action in platelets and growth factor-induced mitogenesis, share common post-receptor molecular events.