Atypical expression of COX-2, StAR, CYP19A1 and apoptotic regulators in CD90 positive endometrial stromal cells from women with endometriosis

2013 ◽  
Vol 5 (2) ◽  
pp. 77-85
Author(s):  
Balamuthu Kadalmani ◽  
Hugh S. Taylor ◽  
Graciela Krikun ◽  
Kavitha Palanivel
Keyword(s):  
Stromal Cells ◽  
Endometrial Stromal Cells ◽  
Cox 2

Peritoneal fluid of patients with endometriosis promotes proliferation of endometrial stromal cells and induces COX-2 expression

2011 ◽  
Vol 95 (5) ◽  
pp. 1836-1838 ◽  
Author(s):  
Yuhuan Liu ◽  
Jingjing Hu ◽  
Wei Shen ◽  
Jiaqi Wang ◽  
Chao Chen ◽  
...  
Keyword(s):  
Stromal Cells ◽  
Peritoneal Fluid ◽  
Endometrial Stromal Cells ◽  
Cox 2

Effects of Celecoxib and Nimesulide on the Proliferation of Ectopic Endometrial Stromal Cells in vitro

2008 ◽  
Vol 36 (5) ◽  
pp. 1032-1038 ◽  
Author(s):  
B Kong ◽  
Y Tian ◽  
W Zhu ◽  
S Su ◽  
Y Kan
Keyword(s):  
Cell Cycle ◽  
Stromal Cells ◽  
Prostaglandin E ◽  
Apoptotic Cells ◽  
Dependent Manner ◽  
Selective Inhibitors ◽  
Endometrial Stromal Cells ◽  
Cox 2 ◽  
Dose Dependent

The effects of cyclooxygenase 2 (COX-2) selective inhibitors on the proliferation of ectopic endometrial stromal cells in vitro were investigated. Ectopic endometrial stromal cells were treated with either celecoxib or nimesulide for 24 and 48 h. The results showed that (i) both celecoxib and nimesulide inhibited the proliferation of ectopic endometrial stromal cells in vitro in a time- and dose-dependent manner; (ii) the expression of prostaglandin E2 was significantly inhibited by both celecoxib and nimesulide in a dose-dependent manner; (iii) the percentage of apoptotic cells was significantly higher for cells treated with celecoxib or nimesulide than for untreated cells; and (iv) the percentage of the cells in the G0/G1 phase increased after the cells were treated with either agent in a dose-dependent manner. These data suggest that celecoxib and nimesulide inhibited proliferation of ectopic endometrial stromal cells by inducing apoptosis and blocking the cell cycle at the G0/G1 phase.

scholarly journals Ubiquitin-Proteasomal Degradation of COX-2 in TGF-β Stimulated Human Endometrial Cells Is Mediated Through Endoplasmic Reticulum Mannosidase I

Endocrinology ◽  
2012 ◽  
Vol 153 (1) ◽  
pp. 426-437 ◽  
Author(s):  
Mohan Singh ◽  
Parvesh Chaudhry ◽  
Sophie Parent ◽  
Eric Asselin
Keyword(s):  
Endoplasmic Reticulum ◽  
Stromal Cells ◽  
Small Interfering Rna ◽  
Proteasomal Degradation ◽  
26S Proteasome ◽  
Dependent Manner ◽  
Endometrial Stromal Cells ◽  
Endometrial Cells ◽  
Cox 2 ◽  
Interfering Rna

Cyclooxygenase (COX)-2 is a key regulatory enzyme in the production of prostaglandins (PG) during various physiological processes. Mechanisms of COX-2 regulation in human endometrial stromal cells (human endometrial stromal cells) are not fully understood. In this study, we investigate the role of TGF-β in the regulation of COX-2 in human uterine stromal cells. Each TGF-β isoform decreases COX-2 protein level in human uterine stromal cells in Smad2/3-dependent manner. The decrease in COX-2 is accompanied by a decrease in PG synthesis. Knockdown of Smad4 using specific small interfering RNA prevents the decrease in COX-2 protein, confirming that Smad pathway is implicated in the regulation of COX-2 expression in human endometrial stromal cells. Pretreatment with 26S proteasome inhibitor, MG132, significantly restores COX-2 protein and PG synthesis, indicating that COX-2 undergoes proteasomal degradation in the presence of TGF-β. In addition, each TGF-β isoform up-regulates endoplasmic reticulum (ER)-mannosidase I (ERManI) implying that COX-2 degradation is mediated through ER-associated degradation pathway in these cells. Furthermore, inhibition of ERManI activity using the mannosidase inhibitor (kifunensine), or small interfering RNA-mediated knockdown of ERManI, prevents TGF-β-induced COX-2 degradation. Taken together, these studies suggest that TGF-β promotes COX-2 degradation in a Smad-dependent manner by up-regulating the expression of ERManI and thereby enhancing ER-associated degradation and proteasomal degradation pathways.

Omega 3 Fatty Acids Counteract IL-8 and Prostaglandin E2 Secretion Induced by TNF-α in Cultured Endometrial Stromal Cells

2011 ◽  
Vol 3 (1) ◽  
pp. 34-39
Author(s):  
Romina Novembri ◽  
Stefano Luisi ◽  
Patrizia Carrarelli ◽  
Valentina Ciani ◽  
Flavio de Pascalis ◽  
...  
Keyword(s):  
Fatty Acids ◽  
Inflammatory Mediators ◽  
Stromal Cells ◽  
Inhibitory Effect ◽  
Omega 3 Fatty Acids ◽  
Omega 3 ◽  
Endometrial Stromal Cells ◽  
Tnf Α ◽  
Key Enzyme ◽  
Cox 2

Background Inflammation is part of the normal host response to infection and injury and excess inflammation may lead to acute or chronic diseases. Endometriosis is a common gynecologic disease characterized by increased endometrial production of inflammatory mediators such as cytokines, reactive oxygen species, and prostaglandins. Omega-3 polyunsaturated fatty acids play a role in the inflammatory process and a therapeutic effect has been suggested. Methods On this basis, this study aimed to assess in human cultured endometrial stromal cells the effect of two omega-3 fatty acids (DHA and EPA), on i) TNF-α induced IL-8 and PGE2 release and on ii) cyclooxygenase-2 (Cox-2) mRNA expression a key enzyme for prostaglandin production. Results DHA or EPA significantly reduced LPS-induced IL-8 (P<0.01) and PGE2 (P<0.01) release decreasing the expression of Cox-2 (P<0.01). Conclusions In conclusion, our study revealed an inhibitory effect of omega-3 fatty acids on inflammatory mediators secretion and suggests a potential benefit for the treatment of pelvic pain in patients with dysmenorrhea and/or endometriosis.

Hexachlorobenzene exposure enhances COX-2 expression and metalloprotease activities in human endometrial stromal cells

2014 ◽  
Vol 229 ◽  
pp. S78-S79
Author(s):  
Florencia Chiappini ◽  
Juan Ignacio Bastón ◽  
Agustina Vaccarezza ◽  
Jose Javier Singla ◽  
Carolina Pontillo ◽  
...  
Keyword(s):  
Stromal Cells ◽  
Endometrial Stromal Cells ◽  
Cox 2

scholarly journals Inhibition of TPPP3 attenuates β-catenin/NF-κB/COX-2 signaling in endometrial stromal cells and impairs decidualization

2019 ◽  
Vol 240 (3) ◽  
pp. 417-429 ◽  
Author(s):  
Vinay Shukla ◽  
Jyoti Bala Kaushal ◽  
Pushplata Sankhwar ◽  
Murli Manohar ◽  
Anila Dwivedi
Keyword(s):  
Stromal Cells ◽  
Embryo Implantation ◽  
Nuclear Accumulation ◽  
Decidual Cell ◽  
Endometrial Stromal Cells ◽  
Cox 2 ◽  
Sirna Knockdown

Embryo implantation and decidualization are critical events that occur during early pregnancy. Decidualization is synchronized by the crosstalk of progesterone and the cAMP signaling pathway. Previously, we confirmed the role of TPPP3 during embryo implantation in mice, but the underlying role and mechanism of TPPP3 in decidualization has not yet been understood. The current study was aimed to investigate the role of TPPP3 in decidualization in vivo and in vitro. For in vivo experiments, decidual reaction was artificially induced in the uteri of BALB/c mice. TPPP3 was found to be highly expressed during decidualization, whereas in the uteri receiving TPPP3 siRNA, decidualization was suppressed and the expression of β-catenin and decidual marker prolactin was reduced. In human endometrium, TPPP3 protein was found to be predominantly expressed in the mid-secretory phase (LH+7). In the primary culture of human endometrial stromal cells (hESCs), TPPP3 siRNA knockdown inhibited stromal-to-decidual cell transition and decreased the expression of the decidualization markers prolactin and IGFBP-1. Immunofluorescence and immunoblotting experiments revealed that TPPP3 siRNA knockdown suppressed the expression of β-catenin, NF-κB and COX-2 in hESCs during decidualization. TPPP3 inhibition also decreased NF-kB nuclear accumulation in hESCs and suppressed NF-κB transcriptional promoter activity. COX-2 expression was significantly decreased in the presence of a selective NF-kB inhibitor (QNZ) implicating that NF-kB is involved in COX-2 expression in hESCs undergoing decidualization. TUNEL assay and FACS analysis revealed that TPPP3 knockdown induced apoptosis and caused loss of mitochondrial membrane potential in hESCs. The study suggested that TPPP3 plays a significant role in decidualization and its inhibition leads to the suppression of β-catenin/NF-κB/COX-2 signaling along with the induction of mitochondria-dependent apoptosis.

A positive COX-2/IL-1β loop promotes decidualization by up-regulating CD82

Reproduction ◽  
2021 ◽  
Author(s):  
Qiu-Chan Qu ◽  
Hui-Hui Shen ◽  
Cheng-Jie Wang ◽  
Xinyan Zhang ◽  
Jiang-Nan Wu ◽  
...  
Keyword(s):  
Stromal Cells ◽  
Feedback Loop ◽  
Neutralizing Antibody ◽  
Trophoblast Invasion ◽  
Metastasis Suppressor ◽  
Mrna Levels ◽  
Endometrial Stromal Cells ◽  
Immunohistochemistry Staining ◽  
Cox 2 ◽  
High Level

A successful pregnancy requires sufficient decidualization of endometrial stromal cells (ESCs). CD82, a metastasis suppressor, is a critical regulator for trophoblast invasion but the effect in decidualization was largely unknown. Here we reported that there was a high level of CD82 in DSC by the immunohistochemistry staining and flow cytometer analysis. Stimulation with prostaglandin E2 (PGE2) elevated the expression of CD82 in ESCs. In contrast, celecoxib, a selective COX-2 inhibitor, significantly down-regulated the expression of CD82 in decidual stromal cells (DSCs). Bioinformatics analysis and further research showed that recombinant human interleukin (IL)-1β protein (rhIL-1β) up-regulated CD82 in ESCs. Of note, blocking IL-1β signaling with anti-human IL-1β neutralizing antibody could reverse the stimulatory effect of PGE2 on CD82 in ESCs. Silencing CD82 resulted in the decease of the decidualization markers PRL and IGFBP1 mRNA levels in DSCs. More importantly, we observed rhIL-1β also up-regulated the expression of COX-2, and the up-regulation of PRL and IGFBP1 induced by rhIL-1β could be abolished by celecoxib in ESCs or CD82 deficiency in DSCs. This study suggests that CD82 should be a novel promotor for decidualization under a positive regulation of the COX-2/PGE2/IL-1β positive feedback loop.

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