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This version published online on September 7, 2006
Endocrinology, doi:10.1210/en.2006-0723
A more recent version of this article appeared on December 1, 2006
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*Compound via MeSH
*Substance via MeSH

Submitted on May 31, 2006
Accepted on August 25, 2006

ROLE FOR PROSTAGLANDINS IN THE REGULATION OF TYPE 1 11{beta} HYDROXYSTEROID DEHYDROGENASE IN HUMAN GRANULOSA-LUTEIN CELLS

Kim C Jonas*, Christina Chandras, D Robert E Abayasekara, and Anthony E Michael

Department of Biochemistry and Molecular Biology, Royal Free and University College Medical School, University College London, Gower Street, London, WC1E 6BT, UK; Department of Veterinary Basic Science, Royal Veterinary College, Royal College Street, London, NW1 0TU, UK; Centre for Developmental and Endocrine Signalling, Academic Section of Obstetrics & Gynaecology, Division of Clinical Developmental Sciences, St.George's, University of London, Cranmer Terrace, London SW17 0RE, UK

* To whom correspondence should be addressed. E-mail: kjonas{at}rvc.ac.uk.

11{beta}-hydroxysteroid dehydrogenase (11{beta}HSD) enzymes regulate glucocorticoid availability in target tissues. 11{beta}HSD1 is the predominant isoenzyme expressed and active in human granulosa-lutein (hGL) cells. This study investigated the effects of pharmacological inhibitors of prostaglandin (PG) synthesis on 11{beta}HSD1 activities and expression in hGL cells. The consequences for 11{beta}HSD1 of increasing exposure of hGL cells to PGs, either by treatment with exogenous PGs or by challenging cells with interleukin-1{beta} (IL-1{beta}), were also assessed. Suppression of basal PG synthesis using 4 different inhibitors of prostaglandin H synthase enzymes (indomethacin, niflumic acid, meclofenamic acid (MA) and N-(2-cyclohexyloxy-4-nitorophenyl) methane sulfonamide (NS-398)) each resulted in significant decreases in both cortisol oxidation and cortisone reduction. Both activities of 11{beta}HSD1 were suppressed by up to 64 ± 6% (P < 0.05). Over 4 and 24 h, neither MA nor NS-398 affected the expression of 11{beta}HSD1 protein, suggesting enzyme regulation by PGs at the post-translational level. When cells were co-treated for 4 h with PGHS inhibitors plus 30 nM PGD2, PGF2{alpha} or PGE2, each PG overcame the suppression of cortisol oxidation by indomethacin or MA. Treatment of hGL cells with IL-1{beta} increased the concentrations of both PGE2 and PGF2{alpha}, accompanied by a 70 ± 25% increase in net cortisol oxidation. All 3 responses to IL-1{beta} were abolished when cells were co-treated with MA. These findings suggest a role for prostaglandins in the post-translational regulation of 11{beta}HSD1 activities in hGL cells.




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