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J Biol Chem, Vol. 275, Issue 17, 12416-12423, April 28, 2000

The Requirement of Both Extracellular Regulated Kinase and p38 Mitogen-activated Protein Kinase for Stimulation of Cytosolic Phospholipase A2 Activity by Either Fcgamma RIIA or Fcgamma RIIIB in Human Neutrophils
A POSSIBLE ROLE FOR Pyk2 BUT NOT FOR THE Grb2-Sos-Shc COMPLEX*

Inbal Hazan-HalevyDagger , Rony Seger§, and Rachel LevyDagger

From the Dagger  Laboratory of Infectious Diseases, Department of Clinical Biochemistry, Faculty of Health Sciences, Ben-Gurion University of the Negev and Soroka Medical Center, Beer Sheva 84105, Israel and the § Department of Biological Regulation, The Weizmann Institute of Science, Rehovot 76100 Israel

The signal transduction pathways initiated by opsonized zymosan (OZ) leading to activation of cytosolic phospholipase A2 (cPLA2) in human neutrophils remain obscure. In a previous study, we showed that the activation of cPLA2 by OZ is tyrosine kinase-dependent. The present study demonstrates that the signals initiated by OZ involve activation of tyrosine kinase Pyk2 but not the formation of the adhesion protein complex, Shc-Grb2-Sos. Stimulation of cPLA2 activity by OZ is mediated by Fc gamma  receptors (Fcgamma Rs) and not by complement receptors for the C3b protein. Cross-linking of Fcgamma RIIA or Fcgamma RIIIB induces p38 mitogen-activated protein (MAP) kinase and extracellular regulated kinase (ERK) phosphorylation. The kinetics of cPLA2 activity stimulated by either of the Fcgamma Rs or by both is similar to that of p38 MAP kinase and was detected as early as 15 s after stimulation, maintained a plateau for 10 min, and decreased thereafter. ERK activation was detected also within 15 s but decreased significantly 5 min after stimulation. The MEK inhibitor, PD-098059, or the p38 MAP kinase inhibitor, SB-203580, caused a partial inhibition during the time course of cPLA2 activity, whereas their combination caused a total inhibition. Thus, although ERK activation is significantly shorter than that of p38 MAP kinase, it is equally required for activation and maintenance of cPLA2 activity by occupancy of a single receptor, Fcgamma RIIA or Fcgamma RIIIB.

* This work was supported by a grant from the Ministry of Health, Israel.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.

To whom correspondence should be addressed: Dept. of Clinical Biochemistry, Faculty of Health Sciences, Ben-Gurion University of the Negev, Beer Sheva 84105, Israel. Tel.: 972-7-6403186; Fax: 972-7-6467477; E-mail: ral@bgumail.bgu.ac.il.

Copyright © 2000 by The American Society for Biochemistry and Molecular Biology, Inc.
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