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Originally published In Press as doi:10.1074/jbc.M105264200 on July 9, 2001

J. Biol. Chem., Vol. 276, Issue 38, 35344-35351, September 21, 2001
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Atypical lambda /iota PKC Conveys 5-Lipoxygenase/Leukotriene B4-mediated Cross-talk between Phospholipase A2s Regulating NF-kappa B Activation in Response to Tumor Necrosis Factor-alpha and Interleukin-1beta *

Marit W. AnthonsenDagger , Sonja Andersen, Anita Solhaug, and Berit Johansen

From the UNIGEN Center for Molecular Biology, Faculty of Chemistry and Biology, Norwegian University of Science and Technology, N-7491 Trondheim, Norway

The transcription factor nuclear factor kappa B (NF-kappa B) plays crucial roles in a wide variety of biological functions such as inflammation, stress, and immune responses. We have shown previously that secretory nonpancreatic (snp) and cytosolic (c) phospholipase A2 (PLA2) regulate NF-kappa B activation in response to tumor necrosis factor (TNF)-alpha or interleukin (IL)-1beta activation and that a functional coupling mediated by the 5-lipoxygenase (5-LO) metabolite leukotriene B4 (LTB4) exists between snpPLA2 and cPLA2 in human keratinocytes. In this study, we have further investigated the mechanisms of PLA2-modulated NF-kappa B activation with respect to specific kinases involved in TNF-alpha /IL-1beta -stimulated cPLA2 phosphorylation and NF-kappa B activation. The protein kinase C (PKC) inhibitors RO 31-8220, Gö 6976, and a pseudosubstrate peptide inhibitor of atypical PKCs attenuated arachidonic acid release, cPLA2 phosphorylation, and NF-kappa B activation induced by TNF-alpha or IL-1beta , thus indicating atypical PKCs in cPLA2 regulation and transcription factor activation. Transfection of a kinase-inactive mutant of lambda /iota PKC in NIH-3T3 fibroblasts completely abolished TNF-alpha /IL-1beta -stimulated cellular arachidonic acid release and cPLA2 activation assayed in vitro, confirming the role of lambda /iota PKC in cPLA2 regulation. Furthermore, lambda /iota PKC and cPLA2 phosphorylation was attenuated by phosphatidyinositol 3-kinase (PI3-kinase) inhibitors, which also reduced NF-kappa B activation in response to TNF-alpha and IL-1beta , indicating a role for PI3-kinase in these processes in human keratinocytes. TNF-alpha - and IL-1beta -induced phosphorylation of lambda /iota PKC was attenuated by inhibitors toward snpPLA2 and 5-LO and by an LTB4 receptor antagonist, suggesting lambda /iota PKC as a downstream effector of snpPLA2 and 5-LO/LTB4 the LTB4 receptor. Hence, lambda /iota PKC regulates snpPLA2/LTB4-mediated cPLA2 activation, cellular arachidonic acid release, and NF-kappa B activation induced by TNF-alpha and IL-1beta . In addition, our results demonstrate that PI3-kinase and lambda /iota PKC are involved in cytokine-induced cPLA2 and NF-kappa B activation, thus identifying lambda /iota PKC as a novel regulator of cPLA2.

* This work was supported by grants from the University of Trondheim (to M. W. A.), the Norwegian Research Council Grants 135802/310 (to M. W. A.) and 102264/310 (to B. J.), and the Norwegian Cancer Society Grants A00038/003 (to M. W. A.) and A98086/003 (to B. J.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

Dagger To whom correspondence should be addressed. Tel.: 47 73 551278; Fax: 47 73 596100.

Copyright © 2001 by The American Society for Biochemistry and Molecular Biology, Inc.
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