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 haematopoiesis1–3. 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 reported4,5. 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 activity6, mast cell growth factor7, P-cell stimulating factor8 and multi-colony-stimulating factor3,9. 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.
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Farrar, W., Thomas, T. & Anderson, W. Altered cytosol/membrane enzyme redistribution on interleukin-3 activation of protein kinase C. Nature 315, 235–237 (1985). https://doi.org/10.1038/315235a0
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DOI: https://doi.org/10.1038/315235a0
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