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Secretory Phospholipase A₂ Receptor-Mediated Activation of Cytosolic Phospholipase A₂ in Murine Bone Marrow-Derived Mast Cells¹

Alfred N. Fonteh^2,*, Gen-ichi Atsumi, Tiffany LaPorte^* and Floyd H. Chilton^*,

^* Departments of Internal Medicine, Pulmonary and Critical Care Medicine, Infectious Diseases, and Physiology and Pharmacology, Wake Forest University School of Medicine, Medical Center Boulevard, Winston-Salem, NC 27157

The current study examined the signal transduction steps involved in the selective release of arachidonic acid (AA) induced by the addition of secretory phospholipase A₂ (sPLA₂) isotypes to bone marrow-derived mast cells (BMMC). Overexpression of sPLA₂ receptors caused a marked increase in AA and PGD₂ release after stimulation of BMMC, implicating sPLA₂ receptors in this process. The hypothesis that the release of AA by sPLA₂ involved activation of cytosolic PLA₂ (cPLA₂) was next tested. Addition of group IB PLA₂ to BMMC caused a transient increase in cPLA₂ activity and translocation of this activity to membrane fractions. Western analyses revealed that these changes in cPLA₂ were accompanied by a time-dependent gel shift of cPLA₂ induced by phosphorylation of cPLA₂ at various sites. A noncatalytic ligand of the sPLA₂ receptor, p-amino-phenyl--D-mannopyranoside BSA, also induced an increase in cPLA₂ activity in BMMC. sPLA₂ receptor ligands induced the phosphorylation of p44/p42 mitogen-activated protein kinase. Additionally, an inhibitor of p44/p42 mitogen-activated protein kinase (PD98059) significantly inhibited sPLA₂-induced cPLA₂ activation and AA release. sPLA₂ receptor ligands also increased Ras activation while an inhibitor of tyrosine phosphorylation (herbimycin) inhibited the increase in cPLA₂ activation and AA release. Addition of partially purified sPLA₂ from BMMC enhanced cPLA₂ activity and AA release. Similarly, overexpression of mouse groups IIA or V PLA₂ in BMMC induced an increase in AA release. These data suggest that sPLA₂ mediate the selective release of AA by binding to cell surface receptors and then inducing signal transduction events that lead to cPLA₂ activation.

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