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From the * Harvard Thorndike Laboratory and Charles A. Dana Research Institute, The specific intracellular sites at which enzymes act to generate arachidonate-derived
eicosanoid mediators of inflammation are uncertain. We evaluated the formation and function
of cytoplasmic lipid bodies. Lipid body formation in eosinophils was a rapidly (<1 h) inducible
response which was platelet-activating factor (PAF) receptor-mediated, involved signaling
through protein kinase C, and required new protein synthesis. In intact and enucleated eosinophils, the PAF-induced increases in lipid body numbers correlated with enhanced production
of both lipoxygenase- and cyclooxygenase-derived eicosanoids. All principal eosinophil eicosanoid-forming enzymes, 5-lipoxygenase, leukotriene C4 synthase, and cyclooxygenase, were immunolocalized to native as well as newly induced lipid bodies in intact and enucleated eosinophils.
Thus, lipid bodies are structurally distinct, inducible, nonnuclear sites for enhanced synthesis of paracrine eicosanoid mediators of inflammation.
Department of
Medicine and § Department of Pathology, Beth Israel Deaconess Medical Center, and Department of
Medicine, Brigham and Women's Hospital and Harvard Medical School, Boston, Massachusetts
02215
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