Akt as a possible intracellular mediator for decidualization in human endometrial stromal cells

Osamu Yoshino, Yutaka Osuga, Yasushi Hirota, Kaori Koga, Tetsu Yano, Osamu Tsutsumi, Yuji Taketani
Molecular human reproduction · 2003 · vol. 9(5) , pp. 265–269 · doi:10.1093/molehr/gag035 · PMID:12728019 · W2159373438
Lab / animal OA: closed CC0 ⤵ 10 in-corpus citations
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This study investigated Akt in human endometrial stromal cells and found that its phosphorylation, potentially regulated by the cAMP/PKA pathway, decreases during progesterone-induced decidualization.

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Abstract

To gain an insight into intracellular mechanisms involved in differentiation of human endometrial cells into decidual cells, we examined the presence of Akt, an emerging intracellular mediator in human endometrial stromal cells (ESC). We explored the mechanisms regulating Akt phosphorylation during the process of progesterone-induced decidualization using a primary cell culture system of ESC. Both Akt and phosphorylated Akt (phospho-Akt) were present in ESC. The total Akt level in ESC cultured for 12 days in the absence of ovarian hormones was similar to ESC treated with estradiol (E(2)) at 10 ng/ml, progesterone at 100 ng/ml or E(2) plus progesterone (E(2)progesterone), whereas the levels of phospho-Akt were markedly decreased with progesterone or E(2) progesterone, compared to control cells. Notably, phospho-Akt levels increased during 12 days of culture in parallel with an increase in total Akt in untreated cells. An increase of phospho-Akt in the E(2) progesterone-treated cells was marginal. The level of phospho-Akt in E(2) progesterone-treated cells was markedly reduced compared to control cells at all time points examined. Treatment of the cells with 8-bromo-cAMP decreased the amount of phospho-Akt in ESC in as short a period as 15 min, while no discernible change was observed in the untreated cells. Conversely, H89, an inhibitor of protein kinase A (PKA), significantly increased the amount of phospho-Akt. The addition of H-89 reversed the decrease in the level of phospho-Akt seen in the cells treated with E(2) progesterone. Thus, we demonstrated the presence of Akt and its phosphorylated form in human ESC. We further suggest that Akt phosphorylation through the cAMP/PKA signal transduction pathway may regulate cellular functions coupled with decidualization.

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MeSH descriptors

Decidua Protein Serine-Threonine Kinases Proto-Oncogene Proteins 8-Bromo Cyclic Adenosine Monophosphate 8-Bromo Cyclic Adenosine Monophosphate Cyclic AMP-Dependent Protein Kinases Cyclic AMP-Dependent Protein Kinases Decidua Decidua Decidua Female Humans Phosphorylation Progesterone Progesterone Proto-Oncogene Proteins Proto-Oncogene Proteins Proto-Oncogene Proteins c-akt Stromal Cells Stromal Cells

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