scholarly journals Analyzing Beneficial Effects of Nutritional Supplements on Intestinal Epithelial Barrier Functions During Experimental Colitis

10.3791/55095 ◽  
2017 ◽  
Author(s):  
Hilda Vargas Robles ◽  
Karla Fabiola Castro Ochoa ◽  
Porfirio Nava ◽  
Angélica Silva Olivares ◽  
Mineko Shibayama ◽  
...  
Keyword(s):  
Nutritional Supplements ◽  
Experimental Colitis ◽  
Epithelial Barrier ◽  
Intestinal Epithelial ◽  
Intestinal Epithelial Barrier ◽  
Barrier Functions ◽  
Beneficial Effects

Intestinal epithelial barrier functions in ageing

2019 ◽  
Vol 54 ◽  
pp. 100938 ◽  
Author(s):  
Jacopo J.V. Branca ◽  
Massimo Gulisano ◽  
Claudio Nicoletti
Keyword(s):  
Epithelial Barrier ◽  
Intestinal Epithelial ◽  
Intestinal Epithelial Barrier ◽  
Barrier Functions

scholarly journals The Arp2/3 Inhibitory Protein Arpin Is Required for Intestinal Epithelial Barrier Integrity

2021 ◽  
Vol 9 ◽  
Author(s):  
Sandra Chánez-Paredes ◽  
Armando Montoya-García ◽  
Karla F. Castro-Ochoa ◽  
Julio García-Cordero ◽  
Leticia Cedillo-Barrón ◽  
...  
Keyword(s):  
Protein Complexes ◽  
Experimental Colitis ◽  
Epithelial Barrier ◽  
Intestinal Epithelial ◽  
Intestinal Epithelial Barrier ◽  
Colon Tissue ◽  
Inhibitory Protein ◽  
Α Subunit ◽  
Epithelial Monolayers ◽  
Tnf Α

The intestinal epithelial barrier (IEB) depends on stable interepithelial protein complexes such as tight junctions (TJ), adherens junctions (AJ), and the actin cytoskeleton. During inflammation, the IEB is compromised due to TJ protein internalization and actin remodeling. An important actin regulator is the actin-related protein 2/3 (Arp2/3) complex, which induces actin branching. Activation of Arp2/3 by nucleation-promoting factors is required for the formation of epithelial monolayers, but little is known about the relevance of Arp2/3 inhibition and endogenous Arp2/3 inhibitory proteins for IEB regulation. We found that the recently identified Arp2/3 inhibitory protein arpin was strongly expressed in intestinal epithelial cells. Arpin expression decreased in response to tumor necrosis factor (TNF)α and interferon (IFN)γ treatment, whereas the expression of gadkin and protein interacting with protein C-kinase α-subunit 1 (PICK1), other Arp2/3 inhibitors, remained unchanged. Of note, arpin coprecipitated with the TJ proteins occludin and claudin-1 and the AJ protein E-cadherin. Arpin depletion altered the architecture of both AJ and TJ, increased actin filament content and actomyosin contractility, and significantly increased epithelial permeability, demonstrating that arpin is indeed required for maintaining IEB integrity. During experimental colitis in mice, arpin expression was also decreased. Analyzing colon tissues from ulcerative colitis patients by Western blot, we found different arpin levels with overall no significant changes. However, in acutely inflamed areas, arpin was significantly reduced compared to non-inflamed areas. Importantly, patients receiving mesalazine had significantly higher arpin levels than untreated patients. As arpin depletion (theoretically meaning more active Arp2/3) increased permeability, we wanted to know whether Arp2/3 inhibition would show the opposite. Indeed, the specific Arp2/3 inhibitor CK666 ameliorated TNFα/IFNγ-induced permeability in established Caco-2 monolayers by preventing TJ disruption. CK666 treatment also attenuated colitis development, colon tissue damage, TJ disruption, and permeability in dextran sulphate sodium (DSS)-treated mice. Our results demonstrate that loss of arpin triggers IEB dysfunction during inflammation and that low arpin levels can be considered a novel hallmark of acute inflammation.

199 TNF-α Induced Expression of Enteric Neuronal Neuropeptide Y (NPY) Influences Intestinal Epithelial Barrier Functions

2010 ◽  
Vol 138 (5) ◽  
pp. S-37
Author(s):  
Bindu P. Chandrasekharan ◽  
Denise D. Belsham ◽  
Simon M. Mwangi ◽  
Asma Nusrat ◽  
Shanthi V. Sitaraman ◽  
...  
Keyword(s):  
Neuropeptide Y ◽  
Epithelial Barrier ◽  
Intestinal Epithelial ◽  
Intestinal Epithelial Barrier ◽  
Barrier Functions ◽  
Induced Expression ◽  
Tnf Α

scholarly journals Nonmuscle Myosin IIA Regulates Intestinal Epithelial Barrier in vivo and Plays a Protective Role During Experimental Colitis

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Nayden G. Naydenov ◽  
Alex Feygin ◽  
Dongdong Wang ◽  
John F. Kuemmerle ◽  
Gianni Harris ◽  
...  
Keyword(s):  
Experimental Colitis ◽  
Protective Role ◽  
Epithelial Barrier ◽  
Intestinal Epithelial ◽  
Nonmuscle Myosin ◽  
Intestinal Epithelial Barrier ◽  
Myosin Iia

Desmoglein 2-mediated adhesion is required for intestinal epithelial barrier integrity

2010 ◽  
Vol 298 (5) ◽  
pp. G774-G783 ◽  
Author(s):  
Nicolas Schlegel ◽  
Michael Meir ◽  
Wolfgang-Moritz Heupel ◽  
Bastian Holthöfer ◽  
Rudolf E. Leube ◽  
...  
Keyword(s):  
Tight Junction ◽  
Intestinal Barrier ◽  
Intercellular Junctions ◽  
Barrier Properties ◽  
Epithelial Barrier ◽  
Intestinal Epithelial ◽  
Intestinal Epithelial Barrier ◽  
Barrier Functions ◽  
Epithelial Monolayers

The integrity of intercellular junctions that form the “terminal bar” in intestinal epithelium is crucial for sealing the intestinal barrier. Whereas specific roles of tight and adherens junctions are well known, the contribution of desmosomal adhesion for maintaining the intestinal epithelial barrier has not been specifically addressed. For the present study, we generated a desmoglein 2 antibody directed against the extracellular domain (Dsg2 ED) to test whether impaired Dsg2-mediated adhesion affects intestinal epithelial barrier functions in vitro. This antibody was able to specifically block Dsg2 interaction in cell-free atomic-force microscopy experiments. For in vitro studies of the intestinal barrier we used Caco2 cells following differentiation into tight enterocyte-like epithelial monolayers. Application of Dsg2 ED to Caco2 monolayers resulted in increased cell dissociation compared with controls in a dispase-based enterocyte dissociation assay. Under similar conditions, Dsg2 antibody significantly decreased transepithelial electrical resistance and increased FITC-dextran flux, indicating that Dsg2 interaction is critically involved in the maintenance of epithelial intestinal barrier functions. As revealed by immunostaining, this was due to Dsg2 ED antibody-induced rupture of tight junctions because tight junction proteins claudins 1, 4, and 5, occludin, and tight junction-associated protein zonula occludens-1 were partially removed from cell borders by Dsg2 ED treatment. Similar results were obtained by application of a commercial monoclonal antibody directed against the ED of Dsg2. Antibody-induced effects were blocked by absorption experiments using Dsg2-Fc-coated beads. Our data indicate that Dsg2-mediated adhesion affects tight junction integrity and is required to maintain intestinal epithelial barrier properties.

scholarly journals Regulation of intestinal epithelial cells transcriptome by enteric glial cells: impact on intestinal epithelial barrier functions

BMC Genomics ◽  
2009 ◽  
Vol 10 (1) ◽  
pp. 507 ◽  
Author(s):  
Laurianne Van Landeghem ◽  
Maxime M Mahé ◽  
Raluca Teusan ◽  
Jean Léger ◽  
Isabelle Guisle ◽  
...  
Keyword(s):  
Epithelial Cells ◽  
Glial Cells ◽  
Intestinal Epithelial Cells ◽  
Epithelial Barrier ◽  
Intestinal Epithelial ◽  
Intestinal Epithelial Barrier ◽  
Barrier Functions ◽  
Enteric Glial Cells
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