Prostaglandin F2 alpha inhibits epidermal growth factor binding to cellular receptors on adipocyte precursors in primary culture.

Prostaglandin F2 alpha (PGF2 alpha) and epidermal growth factor (EGF) are potent differentiation inhibitors of adipocyte precursors in primary culture. We show here that PGF2 alpha specifically inhibited EGF binding to adipocyte precursors in a dose dependent fashion. Scatchard analysis indicates that PGF2 alpha causes a 50% decrease in the number of available EGF cell surface receptors without change in receptor affinity. Comparison of EGF binding at different temperatures and on fixed cells indicates that PGF2 alpha increases internalization of EGF-receptor complexes in adipocyte precursors. Phorbol myristate acetate (PMA) also inhibited EGF binding in adipocyte precursors. PGF2 alpha effect was abolished in cells exposed to prolonged treatment with PMA indicating that PGF2 alpha effect on EGF binding is mediated by protein kinase C. These results would suggest that in adipocyte precursors PGF2 alpha may be the physiological mediator of phorbol ester effect on EGF receptor properties.