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J. Biol. Chem., Vol. 276, Issue 31, 28976-28983, August 3, 2001

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Phosphorylation of p42/44^MAPK by Various Signal Transduction Pathways Activates Cytosolic Phospholipase A₂ to Variable Degrees^*

Gerda S. A. T. van Rossum^§, Rinse Klooster, Henk van den Bosch^¶, Arie J. Verkleij, and Johannes Boonstra

From the  Department of Molecular Cell Biology and ^¶ Centre for Biomembranes and Lipid Enzymology, Institute of Biomembranes, Utrecht University, Utrecht 3584 CH, The Netherlands

Arachidonic acid has been implicated to play a role in physiological and pathophysiological processes and is selectively released by the 85-kDa cytosolic phospholipase A₂ (cPLA₂). The activity of cPLA₂ is regulated by calcium, translocating the enzyme to its substrate, and by phosphorylation by a mitogen-activated protein kinase (MAPK) family member and a MAPK-activated protein kinase. In this study, the signal transduction pathways in growth factor-induced phosphorylation of p42/44^MAPK and cPLA₂ activation were investigated in Her14 fibroblasts. p42/44^MAPK in response to epidermal growth factor was not only phosphorylated via the Raf-MEK pathway but mainly through protein kinase C (PKC) or a related or unrelated kinase in which the phosphorylated p42/44^MAPK corresponded with cPLA₂ activity. Serum-induced phosphorylation of p42/44^MAPK also corresponded with cPLA₂ activity but is predominantly mediated via Raf-MEK and partly through PKC or a related or unrelated kinase. In contrast, activation of PKC by phorbol ester did not result in increased cPLA₂ activity, while p42/44^MAPK is phosphorylated, mainly via Raf-MEK and through MEK. Moreover, p42/44^MAPK phosphorylation is present in quiescent and proliferating cells, and p42/44^MAPK is entirely phosphorylated via Raf-MEK, but it only corresponds to cPLA₂ activity in the former cells. Collectively, these data show that p42/44^MAPK in proliferating, quiescent, and stimulated cells is phosphorylated by various signal transduction pathways, suggesting the activation of different populations of p42/44^MAPK and cPLA₂.

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