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*
Department of Health Chemistry, Showa University School of Pharmaceutical Sciences, Hatanodai, Shinagawa-ku, Tokyo, Japan;
Departments of Chemistry and Biochemistry, University of Washington, Seattle, WA 98195; and
Institut de Pharmacologie Moleculaire et Cellulaire, Centre National de la Recherche Scientifique-Unité Propre de Recherche 411, Sophia Antipolis, Valbonne, France
We herein demonstrate that mast cells express all known
members of the group II subfamily of secretory phospholipase
A2 (sPLA2) isozymes, and those having heparin
affinity markedly enhance the exocytotic response. Rat mastocytoma
RBL-2H3 cells transfected with heparin-binding (sPLA2-IIA,
-V, and -IID), but not heparin-nonbinding (sPLA2-IIC),
enzymes released more granule-associated markers (ß-hexosaminidase
and histamine) than mock- or cytosolic PLA2
(cPLA2)-transfected cells after stimulation with IgE and
Ag. Site-directed mutagenesis of sPLA2-IIA and -V revealed
that both the catalytic and heparin-binding domains are essential for
this function. Confocal laser and electron microscopic analyses
revealed that sPLA2-IIA, which was stored in secretory
granules in unstimulated cells, accumulated on the membranous sites
where fusion between the plasma membrane and granule membranes occurred
in activated cells. These results suggest that the heparin-binding
sPLA2s bind to the perigranular membranes through their
heparin-binding domain, and lysophospholipids produced in situ by their
enzymatic action may facilitate the ongoing membrane fusion. In
contrast to the redundant role of sPLA2-IIA, -IID, and -V
in the regulation of degranulation, only sPLA2-V had the
ability to markedly augment IgE/Ag-stimulated immediate
PGD2 production, which reached a level comparable to that
elicited by cPLA2. The latter observation reveals an
unexplored functional segregation among the three related isozymes
expressed in the same cell population.
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