Interleukin-1β Stimulates Ovarian Phospholipase A2(PLA2) Expression and Activity: Up-Regulation of Both Secretory and Cytosolic PLA21
Author(s) -
Shahar Kol,
Izhar BenShlomo,
Motomu Ando,
Donna W. Payne,
Eli Y. Adashi
Publication year - 1997
Publication title -
endocrinology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.674
H-Index - 257
eISSN - 1945-7170
pISSN - 0013-7227
DOI - 10.1210/endo.138.1.4898
Subject(s) - medicine , endocrinology , phospholipase a2 , arachidonic acid , biology , prostaglandin , phosphatidylethanolamine , phosphatidylcholine , ovary , receptor , cytosol , phospholipase , receptor antagonist , phospholipase a , prostanoid , biochemistry , antagonist , enzyme , phospholipid , membrane
Interleukin (IL)-1 beta has been shown to stimulate ovarian prostaglandin biosynthesis. We hypothesized that this effect entails the induction of phospholipase A2 (PLA2). Treatment of cultured whole ovarian dispersates of immature rat origin with IL-1 beta produced significant increases in [3H]arachidonic acid (AA) release and [3H]prostanoid accumulation as well as increases in cellular PLA2 activity and in secretory PLA2 and cytosolic PLA2 transcripts. Cotreatment with IL-1 receptor antagonist reversed IL-mediated (and basal) release of [3H]labeled AA and prostaglandin products, as well as cellular PLA2 activity. Treatment with IL-1 beta also promoted a significant decrease in the cellular content of [3H]phospholipids (apparently phosphatidylethanolamine but not phosphatidylcholine). These observations establish the ovary as a site of IL-1-dependent sPLA2 and cPLA2 gene expression, document the presence of a possible phosphatidylethanolamine-dependent PLA2 activity in cultured whole ovarian dispersates, reveal the up-regulatory, receptor-mediated action of IL-1 beta in this regard and suggest the existence of endogenous PLA2-stimulating/ IL-1-like bioactivity.
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