Faculty Opinions recommendation of Impaired down-regulation of E-cadherin and beta-catenin protein expression in endometrial epithelial cells in the mid-secretory endometrium of infertile patients with endometriosis.

2010 ◽  
Author(s):  
Ali Akoum
Keyword(s):  
Epithelial Cells ◽  
Protein Expression ◽  
Beta Catenin ◽  
Down Regulation ◽  
Secretory Endometrium ◽  
Infertile Patients ◽  
Endometrial Epithelial Cells ◽  
E Cadherin

scholarly journals Impaired Down-Regulation of E-Cadherin and β-Catenin Protein Expression in Endometrial Epithelial Cells in the Mid-Secretory Endometrium of Infertile Patients with Endometriosis

2010 ◽  
Vol 95 (7) ◽  
pp. 3437-3445 ◽  
Author(s):  
Sachiko Matsuzaki ◽  
Claude Darcha ◽  
Elodie Maleysson ◽  
Michel Canis ◽  
Gérard Mage
Keyword(s):  
Epithelial Cells ◽  
Protein Expression ◽  
Molecular Mechanisms ◽  
Unexplained Infertility ◽  
Down Regulation ◽  
Pathway Activation ◽  
Laser Capture ◽  
Secretory Endometrium ◽  
Infertile Patients ◽  
E Cadherin

Context: Only a few, small, human studies on E-cadherin and β-catenin expression in normal cycling human endometrium have been reported. It remains unclear whether expression of these molecules might be altered in the endometrium of infertile patients with endometriosis. Objectives: The aim of the present study was to investigate E-cadherin and β-catenin expression in the endometrium of infertile patients with endometriosis, those with uterine fibromas, and patients with unexplained infertility. Design: Expression levels of E-cadherin and β-catenin mRNA and/or protein in the endometrium of infertile patients with endometriosis (n = 151), those with uterine fibromas (n = 41), patients with unexplained infertility (n = 9), as well as healthy fertile controls (n = 57) were measured. This study utilized laser capture microdissection, real-time RT-PCR, and immunohistochemistry. Results: No significant differences in E-cadherin or β-catenin mRNA expression in microdissected epithelial cells were observed among the different groups throughout the menstrual cycle. However, very low or no protein expression of E-cadherin, total β-catenin, or dephosphorylated β-catenin in luminal and glandular epithelial cells was detected in the mid-secretory endometrium of healthy fertile controls. E-cadherin, total β-catenin, and dephosphorylated β-catenin protein expression in the mid-secretory endometrium of infertile patients with endometriosis or unexplained infertility was significantly higher compared to that of healthy fertile controls in both luminal and glandular epithelial cells. Conclusions: These findings suggest that impaired down-regulation of E-cadherin and β-catenin protein expression, along with Wnt/β-catenin signaling pathway activation during the window of implantation, might be one of the potential molecular mechanisms of infertility in patients with endometriosis.

scholarly journals Oxytocin Receptor Down-Regulation Is Not Necessary for Reducing Oxytocin-Induced Prostaglandin F2α Accumulation by Interferon-τ in a Bovine Endometrial Epithelial Cell Line

Endocrinology ◽  
2009 ◽  
Vol 150 (2) ◽  
pp. 897-905 ◽  
Author(s):  
Narayanan Krishnaswamy ◽  
Ghislain Danyod ◽  
Pierre Chapdelaine ◽  
Michel A. Fortier
Keyword(s):  
Epithelial Cell ◽  
Epithelial Cells ◽  
Cell Line ◽  
Molecular Mechanisms ◽  
Prostaglandin F2α ◽  
Epithelial Cell Line ◽  
Dependent Manner ◽  
Down Regulation ◽  
Endometrial Epithelial Cell ◽  
Endometrial Epithelial Cells

Interferon-τ (IFNτ) is the embryonic signal responsible for pregnancy recognition in ruminants. The primary action of IFNτ is believed to be mediated through inhibition of prostaglandin F2α (PGF2α) released from the endometrial epithelial cells in response to oxytocin (OT). Our working hypothesis was that the antiluteolytic effect of IFNτ also involved modulation of PG production downstream of OT receptor (OTR) and/or cyclooxygenase 2 (COX2). There is currently no OT-sensitive endometrial cell line to study the molecular mechanisms underlying our hypotheses. Therefore, we established an immortalized bovine endometrial epithelial cell line (bEEL) exhibiting OT response. These cells were cytokeratin positive, expressed steroid receptors, and exhibited preferential accumulation of PGF2α over PGE2. The bEEL cells were highly sensitive to OT, showing time- and concentration-dependent increase in COX2 transcript and protein and PGF2α accumulation. Interestingly, IFNτ (20 ng/ml) significantly reduced OT-induced PGF2α accumulation, but surprisingly, the effect was not mediated through down-regulation of either OTR or COX2. Rather, IFNτ up-regulated COX2 in a time- and concentration-dependent manner while decreasing OT-induced PG accumulation. This suggests that COX2 is not a primary target for the antiluteolytic effect of IFNτ. Because IFNτ reduced OT-stimulated PGF2α accumulation within 3 h, the mechanism likely involves a direct interference at the level of the OT signaling or transcription in addition to the down-regulation of OTR observed in vivo. In summary, bEEL cells offer a unique in vitro model for investigating the cellular and molecular mechanisms underlying OT and IFNτ response in relation with luteolysis and recognition of pregnancy in the bovine. Interferon-τ acts as a competitive partial agonist, stimulating basal but inhibiting oxytocin- and phorbol myristate acetate-stimulated prostaglandin F2α production in immortalized bovine endometrial epithelial cells.

Down-regulation of MEK/ERK signaling by E-cadherin-dependent PI3K/Akt pathway in differentiating intestinal epithelial cells

2004 ◽  
Vol 199 (1) ◽  
pp. 32-39 ◽  
Author(s):  
Patrick Laprise ◽  
Marie-Jos�e Langlois ◽  
Marie-Jos�e Boucher ◽  
Christian Jobin ◽  
Nathalie Rivard
Keyword(s):  
Epithelial Cells ◽  
Intestinal Epithelial Cells ◽  
Erk Signaling ◽  
Akt Pathway ◽  
Intestinal Epithelial ◽  
Down Regulation ◽  
E Cadherin

scholarly journals AGR3 Regulates Airway Epithelial Junctions in Patients with Frequent Exacerbations of COPD

2021 ◽  
Vol 12 ◽  
Author(s):  
Rui Ye ◽  
Cuihong Wang ◽  
Pengbo Sun ◽  
Shuang Bai ◽  
Li Zhao
Keyword(s):  
Epithelial Cells ◽  
Protein Expression ◽  
Mrna Expression ◽  
Western Blotting ◽  
Human Lung ◽  
Airway Epithelial Cells ◽  
Copd Exacerbation ◽  
Airway Epithelial ◽  
Copd Exacerbations ◽  
E Cadherin

Background: The mechanisms underlying differences in the susceptibility to chronic obstructive pulmonary disease (COPD) exacerbations between patients are not well understood. Recent studies have shown that the patients with frequent COPD exacerbations is related to specific protein expression in lung tissue. Anterior gradient 3 (AGR3) is expressed in airway epithelial cells in the lung and proteomic analysis revealed that its expression is decreased in patients with frequent COPD exacerbations. Moreover, the loss of epithelial integrity might facilitate trans-epithelial permeability of pathogens in such patients. This study was performed to determine that AGR3 protein play a role in COPD frequency exacerbators.Methods: Human lung tissues were collected from current-smoking patients (Control; n = 15) as well as patients with infrequent COPD exacerbations (IFCOPD; n = 18) and frequent COPD exacerbations (FCOPD; n = 8). While AGR3 protein expression was measured by immunohistochemistry and western blotting, AGR mRNA expression was determined by real time quantitative polymerase chain reaction (RT-qPCR). Furthermore, adherent junctions (AJs) and tight junctions (TJs) protein expression in human lung tissues were measured by immunohistochemistry. The effects of cigarette smoke extract (CSE) on AJ and TJ protein and mRNA expression in BEAS-2B cells were assessed by western blotting and RT-qPCR. In addition, the effect of AGR3 overexpression and knockdown on AJ and TJ protein expression was determined.Results: AGR3 was mainly expressed in the airway epithelium and AGR3-positive products were localized in the cytoplasm. Western blotting and RT-qPCR results showed that AGR3 protein (p = 0.009) and mRNA (p = 0.04) expression in the FCOPD group was significantly lower than that in the IFCOPD group. Moreover, E-cadherin, occludin, and zonula occludens-1 (ZO-1) expression was lower in the FCOPD group than in the IFCOPD group. The protein and mRNA expression of E-cadherin, occludin, and ZO-1 was decreased within 24 h post-CSE exposure. AGR3 overexpression rescued CSE-induced downregulation of E-cadherin, occludin, and ZO-1.Conclusion: Difference in AGR3 expression in the lung tissue might be correlated with increased susceptibility to COPD exacerbation. AGR3 can prevent CSE-induced downregulation of E-cadherin, occludin, and ZO-1 in airway epithelial cells. Loss of AGR3 might promote viral and bacterial infection and induce immune inflammation to increase COPD exacerbation.

scholarly journals Brain Metastases from Lung Cancer Show Increased Expression of DVL1, DVL3 and Beta-Catenin and Down-Regulation of E-Cadherin

2014 ◽  
Vol 15 (6) ◽  
pp. 10635-10651 ◽  
Author(s):  
Anja Kafka ◽  
Davor Tomas ◽  
Vili Beroš ◽  
Hrvoje Pećina ◽  
Martina Zeljko ◽  
...  
Keyword(s):  
Lung Cancer ◽  
Brain Metastases ◽  
Beta Catenin ◽  
Down Regulation ◽  
E Cadherin

scholarly journals Defining interactions and distributions of cadherin and catenin complexes in polarized epithelial cells.

1994 ◽  
Vol 125 (6) ◽  
pp. 1341-1352 ◽  
Author(s):  
I S Näthke ◽  
L Hinck ◽  
J R Swedlow ◽  
J Papkoff ◽  
W J Nelson
Keyword(s):  
Epithelial Cells ◽  
Functional Organization ◽  
Insoluble Fraction ◽  
Junctional Complex ◽  
Beta Catenin ◽  
Lateral Membrane ◽  
Apical Junctional Complex ◽  
Polarized Epithelial Cells ◽  
Triton X ◽  
E Cadherin

The cadherin/catenin complex plays important roles in cell adhesion, signal transduction, as well as the initiation and maintenance of structural and functional organization of cells and tissues. In the preceding study, we showed that the assembly of the cadherin/catenin complex is temporally regulated, and that novel combinations of catenin and cadherin complexes are formed in both Triton X-100-soluble and -insoluble fractions; we proposed a model in which pools of catenins are important in regulating assembly of E-cadherin/catenin and catenin complexes. Here, we sought to determine the spatial distributions of E-cadherin, alpha-catenin, beta-catenin, and plakoglobin, and whether different complexes of these proteins accumulate at steady state in polarized Madin-Darby canine kidney cells. Protein distributions were visualized by wide field, optical sectioning, and double immunofluorescence microscopy, followed by reconstruction of three-dimensional images. In cells that were extracted with Triton X-100 and then fixed (Triton X-100-insoluble fraction), more E-cadherin was concentrated at the apical junction relative to other areas of the lateral membrane. alpha-Catenin and beta-catenin colocalize with E-cadherin at the apical junctional complex. There is some overlap in the distribution of these proteins in the lateral membrane, but there are also areas where the distributions are distinct. Plakoglobin is excluded from the apical junctional complex, and its distribution in the lateral membrane is different from that of E-cadherin. Cells were also fixed and then permeabilized to reveal the total cellular pool of each protein (Triton X-100-soluble and -insoluble fractions). This analysis showed lateral membrane localization of alpha-catenin, beta-catenin, and plakoglobin, and it also revealed that they are distributed throughout the cell. Chemical cross-linking of proteins and analysis with specific antibodies confirmed the presence at steady state of E-cadherin/catenin complexes containing either beta-catenin or plakoglobin, and catenin complexes devoid of E-cadherin. Complexes containing E-cadherin/beta-catenin and E-cadherin/alpha-catenin are present in both the Triton X-100-soluble and -insoluble fractions, but E-cadherin/plakoglobin complexes are not detected in the Triton X-100-insoluble fraction. Taken together, these results show that different complexes of cadherin and catenins accumulate in fully polarized epithelial cells, and that they distribute to different sites. We suggest that cadherin/catenin and catenin complexes at different sites have specialized roles in establishing and maintaining the structural and functional organization of polarized epithelial cells.

scholarly journals Activation of SGK1 in Endometrial Epithelial Cells in Response to PI3K/AKT Inhibition Impairs Embryo Implantation

2016 ◽  
Vol 39 (5) ◽  
pp. 2077-2087 ◽  
Author(s):  
Madhuri S. Salker ◽  
Jennifer H. Steel ◽  
Zohreh Hosseinzadeh ◽  
Jaya Nautiyal ◽  
Zoe Webster ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Embryo Implantation ◽  
Transport Processes ◽  
Akt Inhibitor ◽  
Down Regulation ◽  
Uterine Lumen ◽  
Akt Activation ◽  
A Cell ◽  
Phosphoinositide 3 Kinase ◽  
Endometrial Epithelial Cells

Background: Serum & Glucocorticoid Regulated Kinase 1 (SGK1) plays a fundamental role in ion and solute transport processes in epithelia. In the endometrium, down-regulation of SGK1 during the window of receptivity facilitates embryo implantation whereas expression of a constitutively active mutant in the murine uterus blocks implantation. Methods/Results: Here, we report that treatment of endometrial epithelial cells with specific inhibitors of the phosphoinositide 3-kinase (PI3K)/AKT activity pathway results in reciprocal activation of SGK1. Flushing of the uterine lumen of mice with a cell permeable, substrate competitive phosphatidylinositol analogue that inhibits AKT activation (AKT inhibitor III) resulted in Sgk1 phosphorylation, down-regulation of the E3 ubiquitin-protein ligase Nedd4-2, and increased expression of epithelial Na+ channels (ENaC). Furthermore, exposure of the uterine lumen to AKT inhibitor III prior to embryo transfer induced a spectrum of early pregnancy defects, ranging from implantation failure to aberrant spacing of implantation sites. Conclusion: Taken together, our data indicate that the balanced activities of two related serine/threonine kinases, AKT and SGK1, critically govern the implantation process.

scholarly journals miR-543 Inhibits the Occurrence and Development of Intrauterine Adhesion by Inhibiting the Proliferation, Migration, and Invasion of Endometrial Cells

2021 ◽  
Vol 2021 ◽  
pp. 1-9
Author(s):  
Xin Liu ◽  
Qian Xu ◽  
Chao Chen ◽  
Hua Duan
Keyword(s):  
Epithelial Cells ◽  
Protein Expression ◽  
Endometrial Adenocarcinoma ◽  
Luciferase Reporter ◽  
Control Group ◽  
Intrauterine Adhesions ◽  
Endometrial Cells ◽  
Intrauterine Adhesion ◽  
Adenocarcinoma Cells ◽  
Endometrial Epithelial Cells

Objective. To explore the function of miR-543 in endometrial cells and the possible mechanism of regulating the occurrence and development of intrauterine adhesion. Method. Endometrial epithelial cells and endometrial adenocarcinoma cells were transfected with miR-543 mimics and miR-543 inhibitor as the experimental group and were tested with the control group, using the CCK-8 method, scratch test, and Transwell assay, and flow cytometry was used to detect the proliferation, migration, invasion, and apoptosis of cells. RT-qPCR and Western blot were used to detect the expression of corresponding mRNA and protein. Results. After the overexpression of miR-543, endometrial epithelial cells and endometrial adenocarcinoma cells have reduced migratory, proliferative, and invasive capabilities, while the apoptosis rate has increased significantly. The mRNA expression of CDH2, COL16A1, vimentin, α-SMA and fibronectin decreased, and the protein expression of CDH2, vimentin, and α-SMA also decreased, while the mRNA and protein expression of CDH1 increased. The result after interfering with miR-543 is opposite, and luciferase reporter gene confirms that CDH2 is the target gene of miR-543. Conclusion. During the formation of intrauterine adhesions, the expression of CDH2, COL16A1, vimentin, and α-SMA may be inhibited by the high expression of miR-543, which may affect the degree of fibrosis and collagen content in the intrauterine adhesions, thereby inhibiting the occurrence and development of intrauterine adhesions.

159 CHANGES IN PROTEIN EXPRESSION PROFILES IN BOVINE ENDOMETRIAL EPITHELIAL CELLS (bEEC) FOLLOWING E. COLI LIPOPOLYSACCHARIDE CHALLENGE

2015 ◽  
Vol 27 (1) ◽  
pp. 170 ◽  
Author(s):  
Y. Z. Guo ◽  
C. Piras ◽  
A. Soggiu ◽  
M. Chanrot ◽  
R. Båge ◽  
...  
Keyword(s):  
Cell Proliferation ◽  
Epithelial Cells ◽  
Protein Expression ◽  
Expression Profiles ◽  
Time Of Flight ◽  
Cell Number ◽  
Differentially Expressed ◽  
E Coli ◽  
Maldi Tof ◽  
Endometrial Epithelial Cells

E. coli is one of the most frequent bacteria involved in uterine diseases. Lipopolysaccharide (LPS) is a component of the outer membrane of Gram-negative bacteria involved in the pathogenic processes leading to postpartum metritis and endometritis in cattle. It also causes inflammation of the endometrium. Increase of cell proliferation by LPS is part of the inflammatory process and has been reported in human epithelial and immune cells (Martin et al. 2000 J. Immunol. 165, 139–147) and from bovine endometrial epithelial cells (bEEC) (Guo et al. 2014 Reprod. Fertil. Dev. 26, 165–166). The aim of this study was to investigate possible changes in protein expression in relation with the proliferative response of bEEC after challenge with E. coli-LPS. In vitro culture of bEEC was performed from 3 cows. On passage 5, bEEC from each individual were exposed to 0, 8, and 16 µg mL–1 LPS for 72 h. At time 0 and 72 h later, attached cells were counted and for each time and LPS dosage, cells were frozen for proteomic analyses. The variation of cells number over time was analysed by ANOVA (SAS 9.1, proc GLM; SAS Institute, Inc., Cary, NC, USA). All samples were analysed (every sample run in triplicate) by 2-D gel electrophoresis coupled to matrix-assisted laser desorption/ionization-time-of-flight (MALDI-TOF)/time-of-flight (TOF) mass spectrometry (MS) and shotgun nLC-MS/MS analysis. As reported before, a significant increase in cell number was observed for cells treated with 8 µg mL–1 LPS (P ≤ 0.001), whereas changes in cell number were highly variable and nonsignificant for 16 µg mL–1 LPS. From each sample, ~800 proteins were visualised. Results from 2-D gel coupled to MALDI-TOF/TOF were very reproducible (same responses between individual cows) and revealed changes in protein profiles very much related (from P < 0.05 to P < 0.01) to proliferative phenotypes for seven proteins. From shotgun analysis, 27 proteins were found significantly differentially expressed (P < 0.05 to P < 0.01) following exposure to LPS (21 up-regulated and 6 down-regulated). Among the 21 found as up-regulated, 20 were differentially expressed both for the 8 and 16 µg mL–1 LPS, whereas 5 out of 6 were down-regulated for both dosages. Differentially expressed proteins were associated to cell proliferation, apoptosis, oxidative stress, regulation of histones, allergy, and general cell metabolism pathways. Candidate proteins need to be confirmed from larger series of individuals and relevant pathways further studied. Research was partially funded by RMUSTV.

Sign in / Sign up

Export Citation Format

Share Document