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Mol. Hum. Reprod. Advance Access originally published online on August 1, 2006
Molecular Human Reproduction 2006 12(9):543-549; doi:10.1093/molehr/gal065
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© The Author 2006. Published by Oxford University Press on behalf of the European Society of Human Reproduction and Embryology. All rights reserved. For Permissions, please email: journals.permissions@oxfordjournals.org

Expression of endometrial glycogen synthase kinase-3ß protein throughout the menstrual cycle and its regulation by progesterone

Wael Salameh1,4, Jason P. Helliwell2, Guang Han2, Laron McPhaul3 and Omid Khorram2,5

1Department of Internal Medicine, 2Department of Obstetrics and Gynecology and 3Department of Pathology, Harbor-UCLA Medical Center, Torrance, CA, USA

4 Present address: Quest Diagnostics, San Juan Capistrano, CA, USA

5 To whom correspondence should be addressed at: Department of Obstetrics and Gynecology, Harbor-UCLA Medical Center, 1000 West Carson Street, Box 489, Torrance, CA, USA. E-mail: okhorram{at}obgyn.humc.edu

Glycogen synthase kinase-3ß (GSK-3ß) is a serine/threonine kinase that plays a role in glycogen synthesis by inhibiting glycogen synthase (GS) through phosphorylation. We hypothesized that GSK-3ß by virtue of its role in glycogen synthesis through the inhibition of GS will play a role in the preparation of the endometrium for blastocyst implantation. Immunohistochemical (IHC) analysis and Western blot analysis (WBA) detected GSK-3ß in the endometrium, myometrium, Fallopian tube and ovary. WBA showed more than 5-fold higher endometrial expression of the phosphorylated GSK-3ß (pGSK-3ß) isoform (inactive) in the secretory phase as compared with the proliferative phase (P < 0.001), whereas no differences in total GSK-3ß expression were detected. IHC analysis confirmed the WBA and showed marked expression of pGSK-3ß predominantly in glandular epithelial cells in early and mid secretory endometrium with scant expression during the proliferative phase. In in vitro experiments using human endometrial-derived epithelial cell line (HES), progesterone did not alter total GSK mRNA or protein expression. However, progesterone induced a dose-dependent increase in the expression of pGSK-3ß, which could be blocked by RU486. Cyclic expression of GSK-3ß’s active and inactive forms in the endometrium suggests that sex hormones regulate the expression of this enzyme. In vitro experiments demonstrate that progesterone through receptor-mediated mechanisms induces phosphorylation of endometrial GSK-3ß.

Key words: endometrium/glycogen synthase kinase-3ß/menstrual cycle/progesterone/RU486


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