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Originally published In Press as doi:10.1074/jbc.M109764200 on November 30, 2001

J. Biol. Chem., Vol. 277, Issue 6, 4069-4078, February 8, 2002
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Regulation of Cytosolic Phospholipase A2 Activity in Macrophages Stimulated with Receptor-recognized Forms of alpha 2-Macroglobulin
ROLE IN MITOGENESIS AND CELL PROLIFERATION*

Uma Kant Misra and Salvatore Vincent PizzoDagger

From the Department of Pathology, Duke University Medical Center, Durham, North Carolina 27710

Macrophages exposed to receptor-recognized forms of alpha 2-macroglobulin (alpha 2M*) demonstrate increased DNA synthesis and cell division. In the current study, we have probed the role of cytosolic phospholipase A2 (cPLA2) activity in the cellular response to alpha 2M*. Ligation of the alpha 2M* signaling receptor by alpha 2M*, or its receptor binding fragment, increased cPLA2 activity 2-3-fold in a concentration and time-dependent manner. This activation required a pertussis toxin-insensitive G protein. Cellular binding of alpha 2M* also induced transient translocation of cPLA2 activity to nuclei and membrane fractions. Inhibition of protein kinase C activity or chelation of Ca2+ inhibited alpha 2M*-induced increased cPLA2 activity. Binding of alpha 2M* to macrophages, moreover, increased phosphorylation of MEK 1/2, ERK 1/2, p38 MAPK, and JNK. Incubation of macrophages with inhibitors of MEK 1/2 or p38 MAPK before stimulation with alpha 2M* profoundly decreased phosphorylation of MAPKs, blocking cPLA2 activation. alpha 2M*-induced increase in [3H]thymidine uptake and cell proliferation was completely abolished if activation of cPLA2 was prevented. The response of macrophages to alpha 2M* requires transcription factors nuclear factor kappa B, and cAMP-responsive element-binding protein as well as expression of the proto-oncogenes c-fos and c-myc. These studies indicate that the activation of cPLA2 plays a crucial role in alpha 2M*-induced mitogenesis and cell proliferation.

* 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: Dept. of Pathology, Box 3712, Duke University Medical Center, Durham, NC 27710. Tel.: 919-684-3528; Fax: 919-684-8689; E-mail: pizzo001@mc.duke.edu.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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Copyright © 2002 by the American Society for Biochemistry and Molecular Biology.