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. 1997 Dec 11;390(6660):618-22.
doi: 10.1038/37622.

Role of cytosolic phospholipase A2 in allergic response and parturition

N Uozumi  1 , K Kume, T Nagase, N Nakatani, S Ishii, F Tashiro, Y Komagata, K Maki, K Ikuta, Y Ouchi, J Miyazaki, T Shimizu
Affiliations

Role of cytosolic phospholipase A2 in allergic response and parturition

N Uozumi et al. Nature. .

Abstract

Phospholipase A2 (PLA2) comprises a superfamily of enzymes that hydrolyse the ester bond of phospholipids at the sn-2 position. Among the members of this superfamily, cytosolic PLA2 has attracted attention because it preferentially hydrolyses arachidonoyl phospholipids and is activated by submicromolar concentrations of Ca2+ ions and by phosphorylation by mitogen-activated protein kinases (MAP kinases). Here we investigate the function of cytosolic PLA2 in vivo by using homologous recombination to generate mice deficient in this enzyme. These mice showed a marked decrease in their production of eicosanoids and platelet-activating factor in peritoneal macrophages. Their ovalbumin-induced anaphylactic responses were significantly reduced, as was their bronchial reactivity to methacholine. Female mutant mice failed to deliver offspring, but these could be rescued by administration of a progesterone-receptor antagonist to the mother at term. Considered together with previous findings, our results indicate that cytosolic PLA2 plays a non-redundant role in allergic responses and reproductive physiology.

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