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Published online before print December 5, 2005

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© by The Society for Leukocyte Biology
Journal of Leukocyte Biology, doi:10.1189/jlb.0805438

Received for publication August 5, 2005.
Revised August 24, 2005.
Accepted for publication October 17, 2005.

Article

Role of PKC isoforms in the FcR-mediated inhibition of LPS-stimulated IL-12 secretion by macrophages

Van Fronhofer ^*, Michelle R. Lennartz , and Daniel J. Loegering ^*@

Centers for *Cardiovascular Sciences and Cell Biology and Cancer Research, Albany Medical College, New York

^@ To whom correspondence should be addressed. E-mail: loegerd{at}mail.amc.edu.

	Abstract

Ligation of Fc receptors for immunoglobulin G (FcRs) inhibits lipopolysaccharide (LPS)-stimulated secretion of interleukin (IL)-12 by macrophages. FcR activation of protein kinase C (PKC) contributes to several functions of this receptor including phagocytosis, activation of the reduced nicotinamide adenine dinucleotide phosphate oxidase, and secretion of certain cytokines. Therefore, we tested the hypothesis that PKC mediates the FcR inhibition of IL-12 secretion by macrophages. In murine macrophages, FcR ligation augmented LPS-stimulated activation of PKC- and PKC- but reduced IL-12p40 secretion. Similarly, activation of PKC with phorbol 12-myristate 13-acetate (PMA) depressed LPS-stimulated IL-12p40 secretion, and depletion of PKC augmented LPS-stimulated IL-12p40 secretion. Antisense down-regulation of PKC- increased LPS-stimulated IL-12p40 secretion and fully prevented the effects of FcR ligation or PMA on IL-12p40 secretion. In contrast, down-regulation of PKC- blocked LPS-stimulated secretion of IL-12p40. Down-regulation of PKC- had no effect on LPS-stimulated IL-12p40 secretion. The results suggest a negative role for PKC- and a positive role for PKC- in the regulation of LPS-stimulated IL-12p40 secretion.

Key Words: cytokines • signal transduction

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