scholarly journals Soy isoflavones improves endometrial barrier through tight junction gene expression

Reproduction ◽  
2015 ◽  
Vol 149 (3) ◽  
pp. 269-280 ◽  
Author(s):  
Pongpat Kiatprasert ◽  
Chatsri Deachapunya ◽  
Chutamas Benjanirat ◽  
Sutthasinee Poonyachoti
Keyword(s):  
Tight Junction ◽  
Mrna Expression ◽  
Barrier Function ◽  
Soy Isoflavones ◽  
Gene Expressions ◽  
Epithelial Barrier Function ◽  
Gene Transcription Level ◽  
Ameliorative Effect ◽  
Zona Occludens ◽  
Endometrial Epithelial Cells

Contamination with bacterial endotoxin causes the disruption of the tight junction (TJ) barrier. We investigated the ameliorative effect of dietary flavonoids genistein (Ge) and daidzein (Di) in normal or lipopolysaccharide (LPS)-induced disruption of epithelial barrier function of the endometrium. Using the immortalized porcine glandular endometrial epithelial cells (PEG), transepithelial electrical resistance (TER) and FITC-dextran flux (FD-4) across the monolayer were measured. The mRNA expression of TJ proteins, zona occludens-1 (ZO1), and claudin-1, -3, -4, -7 and -8 was evaluated by real-time RT-PCR for coinciding effect of Ge or Di occurred at the gene transcription level. The results revealed that Ge and Di altered the TER, depending on times and concentrations. Low concentration (10−10 M) of both compounds decreased the TER, whereas higher concentrations (10−8and 10−6 M) increased the TER which was not related to the FD-4 flux. The increased TER by Ge or Di was parallel to the induction ofclaudin-3and-4or-8mRNA expression respectively. With LPS inoculation, all isoflavone treatments inhibited the decreased TER induced by LPS, but only Ge (10−8or 10−6 M) or Di (10−10or 10−6 M) was coincidence with the decreased FD-4 flux. Under this LPS-stimulated condition, some or all examined TJ gene expressions appeared to be promoted by specific concentration of Ge or Di respectively. Our findings suggest that the soy isoflavones treatment could promote and restore the impaired endometrial barrier function caused by LPS contamination.

scholarly journals JunD Represses Transcription and Translation of the Tight Junction Protein Zona Occludens-1 Modulating Intestinal Epithelial Barrier Function

2008 ◽  
Vol 19 (9) ◽  
pp. 3701-3712 ◽  
Author(s):  
Jie Chen ◽  
Lan Xiao ◽  
Jaladanki N. Rao ◽  
Tongtong Zou ◽  
Lan Liu ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Tight Junction ◽  
Barrier Function ◽  
Intestinal Epithelial Cells ◽  
Binding Protein ◽  
Mrna Translation ◽  
Epithelial Barrier ◽  
Intestinal Epithelial ◽  
Intestinal Epithelial Barrier ◽  
Epithelial Barrier Function

The AP-1 transcription factor JunD is highly expressed in intestinal epithelial cells, but its exact role in maintaining the integrity of intestinal epithelial barrier remains unknown. The tight junction (TJ) protein zonula occludens (ZO)-1 links the intracellular domain of TJ-transmembrane proteins occludin, claudins, and junctional adhesion molecules to many cytoplasmic proteins and the actin cytoskeleton and is crucial for assembly of the TJ complex. Here, we show that JunD negatively regulates expression of ZO-1 and is implicated in the regulation of intestinal epithelial barrier function. Increased JunD levels by ectopic overexpression of the junD gene or by depleting cellular polyamines repressed ZO-1 expression and increased epithelial paracellular permeability. JunD regulated ZO-1 expression at the levels of transcription and translation. Transcriptional repression of ZO-1 by JunD was mediated through cAMP response element-binding protein-binding site within its proximal region of the ZO-1-promoter, whereas induced JunD inhibited ZO-1 mRNA translation by enhancing the interaction of the ZO-1 3′-untranslated region with RNA-binding protein T cell-restricted intracellular antigen 1-related protein. These results indicate that JunD is a biological suppressor of ZO-1 expression in intestinal epithelial cells and plays a critical role in maintaining epithelial barrier function.

Reversible disassembly of an intestinal epithelial monolayer by prolonged exposure to phorbol ester

1994 ◽  
Vol 266 (2) ◽  
pp. G214-G221 ◽  
Author(s):  
G. Hecht ◽  
B. Robinson ◽  
A. Koutsouris
Keyword(s):  
Tight Junction ◽  
Phorbol Ester ◽  
Barrier Function ◽  
Prolonged Exposure ◽  
Morphological Changes ◽  
Cell Types ◽  
Intestinal Epithelial ◽  
Epithelial Monolayer ◽  
Epithelial Barrier Function ◽  
Functional Changes

This article describes a model of reversible disassembly of a cultured human intestinal epithelial monolayer by prolonged exposure to the phorbol ester 12-O-tetradecanoylphorbol 13-acetate (TPA). Prolonged phorbol ester exposure reduces protein kinase C (PKC) levels in numerous cell types including T84, as shown here. Under PKC-downregulated conditions, T84 monolayers, which simulate the highly organized structure of native intestinal crypt cells, become disassembled into 2 or 3 layers of rounded cells. Proliferation does not account for these morphological changes as assessed by thymidine incorporation studies. The effects of structural disorganization on epithelial barrier function was also examined. The permeability of disassembled monolayers was significantly greater than that of controls. Flux studies localized the permeability defect to the tight junction. PKC-associated alterations in the perijunctional ring of actin and myosin, one of the putative regulators of flow across the tight junction, were found to correlate with the observed functional changes. Most interesting was the fact that monolayer reassembly to the original columnar epithelial phenotype and reestablishment of barrier function occurred upon normalization of PKC levels. This model of reversible monolayer disassembly will allow investigation into the relationship between epithelial structure and function and examination of factors that govern monolayer formation.

scholarly journals Acidic Bile Salt Modulates the Squamous Epithelial Barrier Function by Modulating Tight Junction Protein

2011 ◽  
Vol 140 (5) ◽  
pp. S-619-S-620
Author(s):  
Xin Chen ◽  
Tadayuki Oshima ◽  
Toshihiko Tomita ◽  
Hirokazu Fukui ◽  
Jiro Watari ◽  
...  
Keyword(s):  
Tight Junction ◽  
Bile Salt ◽  
Barrier Function ◽  
Tight Junction Protein ◽  
Epithelial Barrier ◽  
Epithelial Barrier Function ◽  
Junction Protein

scholarly journals The HIF target ATG9A is essential for epithelial barrier function and tight junction biogenesis

2020 ◽  
Vol 31 (20) ◽  
pp. 2249-2258
Author(s):  
Alexander S. Dowdell ◽  
Ian M. Cartwright ◽  
Matthew S. Goldberg ◽  
Rachael Kostelecky ◽  
Tyler Ross ◽  
...  
Keyword(s):  
Transcription Factor ◽  
Tight Junction ◽  
Barrier Function ◽  
Intestinal Epithelial Cells ◽  
Hypoxia Inducible Factor ◽  
Epithelial Barrier ◽  
Adaptation To Hypoxia ◽  
Intestinal Epithelial ◽  
Hypoxia Response ◽  
Epithelial Barrier Function

The transcription factor hypoxia-inducible factor (HIF) mediates adaptation to hypoxia. We found that HIF regulates the autophagy protein ATG9A in intestinal epithelial cells. Subsequent knockdown of ATG9A resulted in tight junction mislocalization and cytoskeletal defects. These results suggest a link among the hypoxia response, autophagy, and junctional biogenesis.

PGE2promotes Ca2+-mediated epithelial barrier disruption through EP1and EP4receptors in Caco-2 cell monolayers

2010 ◽  
Vol 299 (2) ◽  
pp. C324-C334 ◽  
Author(s):  
M. José Rodríguez-Lagunas ◽  
Raquel Martín-Venegas ◽  
Juan José Moreno ◽  
Ruth Ferrer
Keyword(s):  
Signaling Pathways ◽  
Barrier Function ◽  
Epithelial Barrier ◽  
Intestinal Epithelial ◽  
Epithelial Barrier Function ◽  
Cell Monolayers ◽  
Intracellular Ca ◽  
Inflammatory Processes ◽  
Zona Occludens

We recently demonstrated that PGE2induces the disruption of the intestinal epithelial barrier function. In the present study, our objectives were to study the role of PGE2receptors (EP1–EP4) and the signaling pathways involved in this event. Paracellular permeability (PP) was assessed in differentiated Caco-2 cell cultures from d-mannitol fluxes and transepithelial electrical resistance (TER) in the presence of different PGE2receptor agonists (carbacyclin, sulprostone, butaprost, ONO-AE1-259, ONO-AE-248, GR63799, and ONO-AE1-329) and antagonists (ONO-8711, SC-19220, AH-6809, ONO-AE3-240, ONO-AE3-208, and AH-23848). The results indicate that EP1and EP4but not EP2and EP3might be involved in PP regulation. These effects were mediated through PLC-inositol trisphosphate (IP3)-Ca2+and cAMP-PKA signaling pathways, respectively. We also observed an increase in intracellular Ca2+concentration ([Ca2+]i) strengthened by cAMP formation indicating a cross talk interaction of these two pathways. Moreover, the participation of a conventional PKC isoform was shown. The results also indicate that the increase in PP may be correlated with the redistribution of occludin, zona occludens 1 (ZO-1), and the perijunctional actin ring together with an increase in myosin light chain kinase activity. Although the disruption of epithelial barrier function observed in inflammatory bowel disease (IBD) patients has been traditionally attributed to cytokines, the present study focused on the role of PGE2in PP regulation, as mucosal levels of this eicosanoid are also increased in these inflammatory processes.

scholarly journals Differential effects of claudin-3 and claudin-4 on alveolar epithelial barrier function

2011 ◽  
Vol 301 (1) ◽  
pp. L40-L49 ◽  
Author(s):  
Leslie A. Mitchell ◽  
Christian E. Overgaard ◽  
Christina Ward ◽  
Susan S. Margulies ◽  
Michael Koval
Keyword(s):  
Epithelial Cells ◽  
Tight Junction ◽  
Barrier Function ◽  
Alveolar Epithelium ◽  
Alveolar Epithelial Cells ◽  
Epithelial Barrier ◽  
Tight Junction Proteins ◽  
Epithelial Barrier Function ◽  
Alveolar Epithelial ◽  
Junction Proteins

Alveolar barrier function depends critically on the claudin family tight junction proteins. Of the major claudins expressed by alveolar epithelial cells, claudin (Cldn)-3 and Cldn-4 are the most closely related by amino acid homology, yet they differ dramatically in the pattern of expression. Previously published reports have shown that Cldn-3 is predominantly expressed by type II alveolar epithelial cells; Cldn-4 is expressed throughout the alveolar epithelium and is specifically upregulated in response to acute lung injury. Using primary rat alveolar epithelial cells transduced with yellow fluorescent protein-tagged claudin constructs, we have identified roles for Cldn-3 and Cldn-4 in alveolar epithelial barrier function. Surprisingly, increasing expression of Cldn-3 decreased alveolar epithelial barrier function, as assessed by transepithelial resistance and dye flux measurements. Conversely, increasing Cldn-4 expression improved alveolar epithelial transepithelial resistance compared with control cells. Other alveolar epithelial tight junction proteins were largely unaffected by increased expression of Cldn-3 and Cldn-4. Taken together, these results demonstrate that, in the context of the alveolar epithelium, Cldn-3 and Cldn-4 have different effects on paracellular permeability, despite significant homology in their extracellular loop domains.

Altered tight junction structure contributes to the impaired epithelial barrier function in ulcerative colitis

1999 ◽  
Vol 116 (2) ◽  
pp. 301-309 ◽  
Author(s):  
Heinz Schmitz ◽  
Christian Barmeyer ◽  
MichaeL Fromm ◽  
Norbert Runkel ◽  
Hans-Dieter Foss ◽  
...  
Keyword(s):  
Ulcerative Colitis ◽  
Tight Junction ◽  
Barrier Function ◽  
Epithelial Barrier ◽  
Epithelial Barrier Function ◽  
Junction Structure

scholarly journals Diesel Exhaust Particle Exposure Reduces Expression of the Epithelial Tight Junction Protein Tricellulin

2020 ◽  
Author(s):  
Timothy Smyth ◽  
Janelle Veazey ◽  
Sophia Eliseeva ◽  
David Chalupa ◽  
Alison Elder ◽  
...  
Keyword(s):  
Tight Junction ◽  
Diesel Exhaust ◽  
Barrier Function ◽  
Diesel Exhaust Particles ◽  
Tight Junction Protein ◽  
Epithelial Barrier ◽  
Airway Epithelial ◽  
Epithelial Barrier Function ◽  
Barrier Integrity ◽  
Junction Protein

Abstract Background: While exposure to diesel exhaust particles has been linked to aberrant immune responses in allergic diseases such as asthma, little attention has been paid to their effects on the airway epithelium. In this study, we sought to determine the effect of diesel exhaust exposure on airway epithelial barrier function and composition using in vitro and in vivo model systems. Methods: 16HBE14o- human bronchial epithelial cells were grown on collagen coated Transwell inserts and exposed to 5 to 50 µg/cm2 SRM 2975 diesel particulate matter (DEP) suspended in cell culture medium or vehicle controls. Changes in barrier function were assessed by measuring transepithelial electrical resistance (TEER) and permeability to 4 kDa FITC Dextran. Neonatal BALB/c mice were exposed to aerosolized DEP (255 ± 89 µg/m3; 2 hours per day for 5 days) and changes in the tight junction protein Tricellulin were assessed two weeks post exposure. Results: A six-hour incubation of epithelial cells with diesel exhaust particles caused a significant concentration-dependent reduction in epithelial barrier integrity as measured by decreased TEER and increased permeability to 4 kDa FITC-Dextran. This reduction in epithelial barrier integrity corresponded to a significant reduction in expression of the tight junction protein Tricellulin. siRNA mediated knockdown of Tricellulin recapitulated changes in barrier function caused by DEP exposure. Neonatal exposure to aerosolized DEP caused a significant reduction in lung Tricellulin two weeks post exposure at both the protein and mRNA level. Conclusion: Short term exposure to DEP causes a significant reduction in epithelial barrier integrity through a reduction in the tight junction protein Tricellulin. Neonatal exposure to aerosolized DEP caused a significant and sustained reduction in Tricellulin protein and mRNA in the lung, suggesting that early life exposure to inhaled DEP may cause lasting changes in airway epithelial barrier function.

scholarly journals Diesel Exhaust Particle Exposure Reduces Expression of the Epithelial Tight Junction Protein Tricellulin

2020 ◽  
Author(s):  
Timothy Smyth ◽  
Janelle Veazey ◽  
Sophia Eliseeva ◽  
David Chalupa ◽  
Alison Elder ◽  
...  
Keyword(s):  
Tight Junction ◽  
Diesel Exhaust ◽  
Barrier Function ◽  
Diesel Exhaust Particles ◽  
Tight Junction Protein ◽  
Epithelial Barrier ◽  
Airway Epithelial ◽  
Epithelial Barrier Function ◽  
Barrier Integrity ◽  
Junction Protein

Abstract Background While exposure to diesel exhaust particles has been linked to aberrant immune responses in allergic diseases such as asthma, little attention has been payed to their effects on the airway epithelium. In this study, we sought to determine the effect of diesel exhaust exposure on airway epithelial barrier function and composition using in vitro and in vivo model systems. 16HBE14o- human bronchial epithelial cells were grown on collagen coated Transwell inserts and exposed to 5 to 50 µg/cm2 SRM 2975 diesel particulate matter (DEP) suspended in cell culture medium or vehicle controls. Changes in barrier function were assessed by measuring transepithelial electrical resistance (TEER) and permeability to 4 kDa FITC Dextran. Neonatal BALB/c mice were exposed to aerosolized DEP (255 ± 89 µg/m3; 2 hours per day for 5 days) and changes in the tight junction protein Tricellulin were assessed two weeks post exposure. Results A six-hour incubation of epithelial cells with diesel exhaust particles caused a significant concentration-dependent reduction in epithelial barrier integrity as measured by decreased TEER and increased permeability to 4 kDa FITC-Dextran. This reduction in epithelial barrier integrity corresponded to a significant reduction in expression of the tight junction protein Tricellulin. siRNA mediated knockdown of Tricellulin recapitulated changes in barrier function caused by DEP exposure. Neonatal exposure to aerosolized DEP caused a significant reduction in lung Tricellulin two weeks post exposure at both the protein and mRNA level. Conclusion Short term exposure to DEP causes a significant reduction in epithelial barrier integrity through a reduction in the tight junction protein Tricellulin. Neonatal exposure to aerosolized DEP caused a significant and sustained reduction in Tricellulin protein and mRNA in the lung, suggesting that early life exposure to inhaled DEP may cause lasting changes in airway epithelial barrier function.

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