Regulation of tight junction formation in intestinal epithelial cells by the IL-15 ligand-receptor system

1998 ◽  
Vol 114 ◽  
pp. A898
Author(s):  
R. Nishiyama ◽  
D.K. Podolsky ◽  
H.C. Reinecker
Keyword(s):  
Epithelial Cells ◽  
Tight Junction ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial ◽  
Receptor System ◽  
Tight Junction Formation ◽  
Junction Formation

scholarly journals The 220-kD protein colocalizing with cadherins in non-epithelial cells is identical to ZO-1, a tight junction-associated protein in epithelial cells: cDNA cloning and immunoelectron microscopy.

1993 ◽  
Vol 121 (3) ◽  
pp. 491-502 ◽  
Author(s):  
M Itoh ◽  
A Nagafuchi ◽  
S Yonemura ◽  
T Kitani-Yasuda ◽  
S Tsukita ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Tight Junction ◽  
Tight Junctions ◽  
Immunoelectron Microscopy ◽  
Intestinal Epithelial Cells ◽  
Microscopic Level ◽  
Junction Zone ◽  
Intestinal Epithelial ◽  
Tight Junction Formation ◽  
Junction Formation

We previously identified a 220-kD constitutive protein of the plasma membrane undercoat which colocalizes at the immunofluorescence microscopic level with cadherins and occurs not only in epithelial M., S. Yonemura, A. Nagafuchi, Sa. Tsukita, and Sh. Tsukita. 1991. J. Cell Biol. 115:1449-1462). To clarify the nature and possible functions of this protein, we cloned its full-length cDNA and sequenced it. Unexpectedly, we found mouse 220-kD protein to be highly homologous to rat protein ZO-1, only a part of which had been already sequenced. This relationship was confirmed by immunoblotting with anti-ZO-1 antibody. As protein ZO-1 was originally identified as a component exclusively underlying tight junctions in epithelial cells, where cadherins are not believed to be localized, we analyzed the distribution of cadherins and the 220-kD protein by ultrathin cryosection immunoelectron microscopy. We found that in non-epithelial cells lacking tight junctions cadherins and the 220-kD protein colocalize, whereas in epithelial cells (e.g., intestinal epithelial cells) bearing well-developed tight junctions cadherins and the 220-kD protein are clearly segregated into adherens and tight junctions, respectively. Interestingly, in epithelial cells such as hepatocytes, which tight junctions are not so well developed, the 220-kD protein is detected not only in the tight junction zone but also at adherens junctions. Furthermore, we show in mouse L cells transfected with cDNAs encoding N-, P-, E-cadherins that cadherins interact directly or indirectly with the 220-kD protein. Possible functions of the 220-kD protein (ZO-1) are discussed with special reference to the molecular mechanism for adherens and tight junction formation.

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.

scholarly journals Laminaria japonica Extract Enhances Intestinal Barrier Function by Altering Inflammatory Response and Tight Junction-Related Protein in Lipopolysaccharide-Stimulated Caco-2 Cells

Nutrients ◽  
2019 ◽  
Vol 11 (5) ◽  
pp. 1001 ◽  
Author(s):  
Hyo-Seon Yang ◽  
Fawaz G Haj ◽  
Myoungsook Lee ◽  
Inhae Kang ◽  
Guiguo Zhang ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Tight Junction ◽  
Intestinal Epithelial Cells ◽  
Physiological State ◽  
Water Extract ◽  
Laminaria Japonica ◽  
Intestinal Barrier Function ◽  
Intestinal Epithelial ◽  
Water Extracts ◽  
Human Intestinal Epithelial Cells

In the normal physiological state, intestinal epithelial cells act as a defensive frontline of host mucosal immunity to tolerate constant exposure to external stimuli. In this study, we investigated the potential anti-inflammatory and gut permeability protective effects of Laminaria japonica (LJ) water extract (LJE) and three types of fermented Laminaria japonica water extracts (LJE-F1, LJE-F2, and LJE-F3) in lipopolysaccharide (LPS)-stimulated Caco-2, human intestinal epithelial cells. All four extracts significantly decreased the production of nitric oxide and interleukin-6 induced by LPS stimulus. In addition, LJE and the three types of LJE-Fs also inhibited LPS-induced loss of monolayer permeability, as assessed by changes in transepithelial electrical resistance. All four LJ extracts significantly prevented the inhibition of the protein levels of occludin, whereas LJE, LJE-F1, and LJE-F3 significantly attenuated the reduction in phosphorylation of adenosine monophosphate-activated protein kinase compared with the LPS-treated group in Caco-2 cells. In conclusion, LJE and its fermented water extracts appear to have potential gut health-promoting effects by reducing inflammation and partially regulating the tight junction-related proteins in human intestinal epithelial cells. Thus, additional studies are warranted to evaluate Laminaria japonica as a therapeutic agent for inflammatory bowel diseases.

scholarly journals In VitroPrevention ofSalmonellaLipopolysaccharide-Induced Damages in Epithelial Barrier Function by VariousLactobacillusStrains

2013 ◽  
Vol 2013 ◽  
pp. 1-6 ◽  
Author(s):  
Chun-Yan Yeung ◽  
Jen-Shiu Chiang Chiau ◽  
Wai-Tao Chan ◽  
Chun-Bin Jiang ◽  
Mei-Lien Cheng ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Tight Junction ◽  
Mononuclear Cells ◽  
Intestinal Epithelial Cells ◽  
Barrier Properties ◽  
Bacterial Invasion ◽  
Epithelial Barrier ◽  
Intestinal Epithelial ◽  
Peripheral Blood Mononuclear

Background.Lactobacillusshows beneficial anti-inflammatory effects onSalmonellainfection. The maintenance of the tight junction (TJ) integrity plays an importance role in avoiding bacterial invasion. WhetherLactobacilluscould be used to regulate the TJ protein expression and distribution in inflamed intestinal epithelial cells was determined.Methods. Using the transwell coculture model,Salmonellalipopolysaccharide (LPS) was apically added to polarized Caco-2 cells cocultured with peripheral blood mononuclear cells in the basolateral compartment. LPS-stimulated Caco-2 cells were incubated with variousLactobacillusstrains. TJ integrity was determined by measuring transepithelial electrical resistance across Caco-2 monolayer. Expression and localization of TJ proteins (zonula-occludens- (ZO-) 1) were determined by Western blot and immunofluorescence microscopy.Results. Various strains ofLactobacilluswere responsible for the different modulations of cell layer integrity. LPS was specifically able to disrupt epithelial barrier and change the location of ZO-1. Our data demonstrate thatLactobacilluscould attenuate the barrier disruption of intestinal epithelial cells caused bySalmonellaLPS administration. We showed thatLactobacillusstrains are associated with the maintenance of the tight junction integrity and appearance.Conclusion. In this study we provide insight that live probiotics could improve epithelial barrier properties and this may explain the potential mechanism behind their beneficial effectin vivo.

828 Glucocorticoids Stimulate Tight Junction Sealing in Intestinal Epithelial Cells By Modulating Expression of Claudin-2 and Claudin-4

2008 ◽  
Vol 134 (4) ◽  
pp. A-118-A-119
Author(s):  
A FISCHER ◽  
M GLUTH ◽  
U PAPE ◽  
B WIEDENMANN ◽  
D BAUMGART ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Tight Junction ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial

T1927 Legume Lectin Rapidly Enters Intestinal Epithelial Cells and Disrupts Tight Junction Localization of ZO-1

2010 ◽  
Vol 138 (5) ◽  
pp. S-608
Author(s):  
Karol Dokladny ◽  
Balamurugan Ramadass ◽  
Henry C. Lin ◽  
Pope Moseley
Keyword(s):  
Epithelial Cells ◽  
Tight Junction ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial ◽  
Legume Lectin
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