Altered cytosol/membrane enzyme redistribution on interleukin-3 activation of protein kinase C

Abstract

Interleukin-3 (IL-3) is a member of a family of growth and differentiation peptides, collectively referred to as colony-stimulating factors, which regulate haematopoiesis. IL-3 has been highly purified from medium conditioned by WEHI-3B cells, and recently the molecular cloning of complementary DNA for murine IL-3 has been reported. IL-3 seems to stimulate a wide range of colony-forming cells derived from murine bone marrow and has consequently been studied under a variety of names, including burst-promoting activity, mast cell growth factor, P-cell stimulating factor and multi-colony-stimulating factor. Here we present evidence that IL-3-receptor interaction stimulates the rapid and transient redistribution of protein kinase C (PK-C) from cytosol to plasma membrane in FDC-P1 cells. Phorbol myristate acetate (PMA) is shown to have a similar effect in these IL-3-dependent FDC-P1 cells. Our data suggest that IL-3 and phorbol esters share a common feature of transmembrane signalling crucial for growth and differentiation.