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Cytosolic Phospholipase A₂-Mediated Regulation of Phospholipase D2 in Leukocyte Cell Lines¹

Jae Ho Kim^*,, Byoung Dae Lee, Yong Kim, Sang Do Lee, Pann-Ghill Suh and Sung Ho Ryu^2,

^* National Creative Research Initiative Center for Calcium and Learning, Department of Life Science and School of Environmental Engineering, Pohang University of Science and Technology, Pohang, South Korea

Phospholipase D (PLD) has been implicated in a variety of cellular processes, including inflammation, secretion, and respiratory burst. Two distinct PLD isoforms, designated PLD₁ and PLD₂, have been cloned; however, the regulatory mechanism for each PLD isoform is not clear. In our present study we investigated how PLD₂ activity is regulated in mouse lymphocytic leukemia L1210 cells, which mainly contain PLD₂ , and in PLD₂ -transfected COS-7 cells. Intriguingly, A23187, a calcium ionophore that induces calcium influx, potently stimulates PLD activity in these two cell lines, suggesting that Ca²⁺ might be implicated in the regulation of the PLD₂ activity. In addition to the A23187-induced PLD₂ activation, A23187 also increases PLA₂-mediated arachidonic acid release, and the A23187-stimulated PLD₂ and PLA₂ activities could be blocked by pretreatment of the cells with cytosolic calcium-dependent PLA₂ (cPLA₂) inhibitors, such as arachidonyl trifluoromethyl ketone and methyl arachidonyl fluorophosphonate in these two cell lines. Moreover, the A23187-induced PLD₂ and PLA₂ activities could be inhibited by cotransfection with antisense cPLA₂ oligonucleotide. These results suggest a role for cPLA₂ in the regulation of PLD₂ activity in vivo. The inhibitory effect of arachidonyl trifluoromethyl ketone on the A23187-induced PLD₂ activity could be recovered by addition of exogenous lysophosphatidylcholine. This study is the first to demonstrate that PLD₂ activity is up-regulated by Ca²⁺ influx and that cPLA₂ may play a key role in the Ca²⁺-dependent regulation of PLD₂ through generation of lysophosphatidylcholine.

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