| First Author | Uozumi N | Year | 1997 |
| Journal | Nature | Volume | 390 |
| Issue | 6660 | Pages | 618-22 |
| PubMed ID | 9403692 | Mgi Jnum | J:39254 |
| Mgi Id | MGI:1100762 | Doi | 10.1038/37622 |
| Citation | Uozumi N, et al. (1997) Role of cytosolic phospholipase A2 in allergic response and parturition. Nature 390(6660):618-22 |
| abstractText | 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. |
