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Papers In Press, published online ahead of print November 30, 2001
Department of Pathology, Duke University Medical Center, Durham, NC 27710
Corresponding Author: Pizzo001{at}mc.duke.edu
Macrophages exposed to receptor-recognized forms of
J. Biol. Chem, 10.1074/jbc.M109764200
Submitted on October 9, 2001
Revised on November 30, 2001
Accepted on November 29, 2001
Regulation of cytosolic phospholipase A2 activity in macrophages stimulated with receptor-recognized forms of
2-macroglobulin: Role in mitogenesis and cell proliferation
2-macroglobulin (2M*) demonstrate increased DNA synthesis and cell division. In the current study, we have probed the role of cytosolic phospholipase A22 (cPLA2) activity in the cellular response to 2M*. Ligation of the 2M* signaling receptor by 2M*, or its receptor binding fragment, increased cPLA2 activity two-threefold in a concentration and time-dependent manner. This activation required a pertussis toxin-insensitive G protein. Cellular binding of 2M* also induced transient translocation of cPLA2 activity to nuclei and membrane fractions. Inhibition of protein kinase C activity or chelation of Ca2+ inhibited 2M*-induced increased cPLA2 activity. Binding of 2M* to macrophages, moreover, increased phosphorylation of MEK 1/2, ERK 1/2, p38MAPK, and JNK. Incubation of macrophages with inhibitors of MEK 1/2 or p38MAPK before stimulation with 22M* profoundly decreased phosphorylation of MAPKs, blocking cPLA2 activation. 2M*-induced increase in [3H]thymidine uptake and cell proliferation was completely abolished if activation of cPLA2 was prevented. The response of macrophages to 2M* requires transcription factors NF
B, and CREB 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 2M*-induced mitogenesis and cell proliferation.
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