Phosphatidic acid induces decidualization by stimulating Akt-PP2A binding in human endometrial stromal cellsopen access
- Authors
- Lee, So Young; Lee, Yun Young; Choi, Joong Sub; Yoon, Mee-Sup; Han, Joong-Soo
- Issue Date
- Nov-2016
- Publisher
- WILEY
- Keywords
- decidualization; human endometrial stromal cells; infertility; phosphatidic acid; phospholipase D1
- Citation
- FEBS JOURNAL, v.283, no.22, pp.4163 - 4175
- Indexed
- SCIE
SCOPUS
- Journal Title
- FEBS JOURNAL
- Volume
- 283
- Number
- 22
- Start Page
- 4163
- End Page
- 4175
- URI
- https://scholarworks.bwise.kr/hanyang/handle/2021.sw.hanyang/153635
- DOI
- 10.1111/febs.13914
- ISSN
- 1742-464X
- Abstract
- Decidualization of human endometrial stromal cells (hESCs) is crucial for successful uterine implantation and maintaining pregnancy. We previously reported that phospholipase D1 (PLD1) is required for cAMP-induced decidualization of hESCs. However, the mechanism by which phosphatidic acid (PA), the product of PLD1 action, might regulate decidualization is not known. We confirmed that PA induced decidualization of hESCs by observing morphological changes and measuring increased levels of decidualization markers such as IGFBP1 and prolactin transcripts (P < 0.05). Treatment with PA reduced phosphorylation of Akt and consequently that of FoxO1, which led to the increased IGFBP1 and prolactin mRNA levels (P < 0.05). Conversely, PLD1 knockdown rescued Akt phosphorylation. Binding of PP2A and Akt increased in response to cAMP or PA, suggesting that their binding is directly responsible for the inactivation of Akt during decidualization. Consistent with this observation, treatment with okadaic acid, a PP2A inhibitor, also inhibited cAMP-induced decidualization by blocking Akt dephosphorylation.
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Collections - 서울 의과대학 > 서울 생화학·분자생물학교실 > 1. Journal Articles
- 서울 의과대학 > 서울 산부인과학교실 > 1. Journal Articles
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