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Progesterone-dependent induction of phospholipase C-related catalytically inactive protein 1 (PRIP-1) in decidualizing human endometrial stromal cells

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Muter, Joanne, Brighton, Paul, Lucas, Emma S., Lacey, Lauren, Shmygol, Anatoly, Quenby, Siobhan, Blanks, Andrew M. and Brosens, Jan J. (2016) Progesterone-dependent induction of phospholipase C-related catalytically inactive protein 1 (PRIP-1) in decidualizing human endometrial stromal cells. Endocrinology, 157 (7). pp. 2883-2893. doi:10.1210/en.2015-1914

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Official URL: http://dx.doi.org/10.1210/en.2015-1914

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Abstract

Decidualization denotes the transformation of endometrial stromal cells into specialized decidual cells. In pregnancy, decidual cells form a protective matrix around the implanting embryo, enabling coordinated trophoblast invasion and formation of a functional placenta. Continuous progesterone (P4) signaling renders decidual cells resistant to various environmental stressors, whereas withdrawal inevitably triggers tissue breakdown and menstruation or miscarriage. Here, we show that PLCL1, coding phospholipase C (PLC)-related catalytically inactive protein 1 (PRIP-1), is highly induced in response to P4 signaling in decidualizing human endometrial stromal cells (HESCs). Knockdown experiments in undifferentiated HESCs revealed that PRIP-1 maintains basal phosphoinositide 3-kinase/Protein kinase B activity, which in turn prevents illicit nuclear translocation of the transcription factor forkhead box protein O1 and induction of the apoptotic activator BIM. By contrast, loss of this scaffold protein did not compromise survival of decidual cells. PRIP-1 knockdown did also not interfere with the responsiveness of HESCs to deciduogenic cues, although the overall expression of differentiation markers, such as PRL, IGFBP1, and WNT4, was blunted. Finally, we show that PRIP-1 in decidual cells uncouples PLC activation from intracellular Ca2+ release by attenuating inositol 1,4,5-trisphosphate signaling. In summary, PRIP-1 is a multifaceted P4-inducible scaffold protein that gates the activity of major signal transduction pathways in the endometrium. It prevents apoptosis of proliferating stromal cells and contributes to the relative autonomy of decidual cells by silencing PLC signaling downstream of Gq protein-coupled receptors.

Item Type: Journal Article
Subjects: Q Science > QP Physiology
Divisions: Faculty of Medicine > Warwick Medical School > Biomedical Sciences > Cell & Developmental Biology
Faculty of Medicine > Warwick Medical School > Biomedical Sciences
Faculty of Medicine > Warwick Medical School
Library of Congress Subject Headings (LCSH): Endometrium, Decidua, Progesterone, Phospholipase C
Journal or Publication Title: Endocrinology
Publisher: Endocrine Society
ISSN: 0013-7227
Official Date: 1 July 2016
Dates:
DateEvent
1 July 2016Published
3 May 2016Accepted
Volume: 157
Number: 7
Page Range: pp. 2883-2893
DOI: 10.1210/en.2015-1914
Status: Peer Reviewed
Publication Status: Published
Publisher Statement: This is a pre-copyedited, author-produced version of an article accepted for publication in Endocrinology following peer review. The version of record Joanne Muter, Paul J. Brighton, Emma S. Lucas, Lauren Lacey, Anatoly Shmygol, Siobhan Quenby, Andrew M. Blanks, Jan J. Brosens, Progesterone-Dependent Induction of Phospholipase C-Related Catalytically Inactive Protein 1 (PRIP-1) in Decidualizing Human Endometrial Stromal Cells, Endocrinology, Volume 157, Issue 7, 1 July 2016, Pages 2883–2893, is available online at: http://dx.doi.org/10.1210/en.2015-1914
Access rights to Published version: Restricted or Subscription Access
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RIOXX Funder/Project Grant:
Project/Grant IDRIOXX Funder NameFunder ID
UNSPECIFIEDWarwick Medical Schoolhttp://dx.doi.org/10.13039/501100004443
UNSPECIFIEDUniversity Hospitals Coventry and Warwickshire NHS Trusthttp://viaf.org/viaf/152707181
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