Modulation of barrier function during Fas-mediated apoptosis in human intestinal epithelial cells

Abreu, María T.; Palladino, Andrew A.; Arnold, Elizabeth T.; Kwon, Richard S.; McRoberts, James A.

doi:10.1053/gast.2000.20232

Cited by 121 publications

(106 citation statements)

References 39 publications

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“…This suggests that, depending on their claudin patterns, epithelial cells may specifically respond to apoptotic stimuli. Moreover, the reduction of the pore-inducing claudin-2 and the up-regulation of the tightening claudin-1 may represent a physiological compensatory mechanism when single apoptotic cells are removed from an epithelial cell layer to maintain at least a limited barrier function until the neighboring cells have reestablished new cell-cell contacts (Abreu et al, 2000).…”

Section: Discussionmentioning

confidence: 99%

“…Especially when apoptotic cells lose their contacts to neighboring cells and detach, it is critical that the remaining cells establish new contacts to maintain barrier function (Abreu et al, 2000) to avoid infiltration of noxious agents or allergens. Impairment of epithelial barrier function is a typical phenomenon observed in the intestinal mucosa of inflammatory bowel disease (IBD) patients.…”

Section: Discussionmentioning

confidence: 99%

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The specific fates of tight junction proteins in apoptotic epithelial cells

Bojarski

Weiske

Schöneberg³

et al. 2004

Journal of Cell Science

154

129

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The polarized morphology of epithelial cells depends on the establishment and maintenance of characteristic intercellular junctions. The dramatic morphological changes observed in apoptotic epithelial cells were ascribed at least in part to the specific fragmentation of components of adherens junctions and desmosomes. Little, however, is known about tight junctions during apoptosis. We have found that after induction of apoptosis in epithelial cells, tight junction proteins undergo proteolytic cleavage in a distinctive manner correlated with a disruption of tight junctions. The transmembrane protein occludin and, likewise, the cytoplasmic adaptor proteins ZO-1 and ZO-2 are fragmented by caspase cleavage. In addition, occludin is cleaved at an extracellular site by a metalloproteinase. The caspase cleavage site in occludin was mapped C-terminally to Asp320 within the C-terminal cytoplasmic domain. Mutagenesis of this site efficiently blocked fragmentation. In the presence of caspase and/or metalloproteinase inhibitors, fragmentation of occludin, ZO-1 and ZO-2 was blocked and cellular morphology was almost fully preserved. Interestingly, two members of the claudin family of transmembrane tight junction proteins exhibited a different behavior. While the amount of claudin-2 protein was reduced similarly to occludin, ZO-1 and ZO-2, claudin-1 was either fully preserved or was even increased in apoptotic cells.

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Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

The specific fates of tight junction proteins in apoptotic epithelial cells

Bojarski

Weiske

Schöneberg³

et al. 2004

Journal of Cell Science

154

129

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“…T84 were cultured on 12-mm Transwell polycarbonate membranes (no. 3041; Costar, Cambridge, MA) and maintained in DMEM/F12 (Invitrogen Life Technologies, Gaithersburg, MD) with 5% penicillin/streptomycin (Pen/ Strep), 5% L-glutamine, supplemented with 5% FBS as previously described (35). T84 cells were used between passages 16 and 35 (35,36).…”

Section: Cells and Reagentsmentioning

confidence: 99%

“…3041; Costar, Cambridge, MA) and maintained in DMEM/F12 (Invitrogen Life Technologies, Gaithersburg, MD) with 5% penicillin/streptomycin (Pen/ Strep), 5% L-glutamine, supplemented with 5% FBS as previously described (35). T84 cells were used between passages 16 and 35 (35,36). Caco-2 were maintained in MEM (Invitrogen Life Technologies) supplemented with 10% FBS, 2 mM L-glutamine, 0.1 mM nonessential amino acids, 1 mM sodium pyruvate, and 5% Pen/Strep.…”

Section: Cells and Reagentsmentioning

confidence: 99%

β-Defensin-2 Expression Is Regulated by TLR Signaling in Intestinal Epithelial Cells

Vora¹,

Youdim²,

Thomas³

et al. 2004

The Journal of Immunology

Self Cite

320

225

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The intestinal epithelium serves as a barrier to the intestinal flora. In response to pathogens, intestinal epithelial cells (IEC) secrete proinflammatory cytokines. To aid in defense against bacteria, IEC also secrete antimicrobial peptides, termed defensins. The aim of our studies was to understand the role of TLR signaling in regulation of β-defensin expression by IEC. The effect of LPS and peptidoglycan on β-defensin-2 expression was examined in IEC lines constitutively or transgenically expressing TLRs. Regulation of β-defensin-2 was assessed using promoter-reporter constructs of the human β-defensin-2 gene. LPS and peptidoglycan stimulated β-defensin-2 promoter activation in a TLR4- and TLR2-dependent manner, respectively. A mutation in the NF-κB or AP-1 site within the β-defensin-2 promoter abrogated this response. In addition, inhibition of Jun kinase prevents up-regulation of β-defensin-2 protein expression in response to LPS. IEC respond to pathogen-associated molecular patterns with expression of the antimicrobial peptide β-defensin-2. This mechanism may protect the intestinal epithelium from pathogen invasion and from potential invaders among the commensal flora.

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“…While a primary barrier defect may be present in IBD kindreds 12-14 , it is also clear that epithelial barrier defects can be induced by inflammatory cytokines [15][16][17][18][19][20][21][22][23][24] . Recent work has demonstrated that barrier dysfunction induced by inflammatory processes can be due to epithelial damage as well as non-apoptotic regulation of tight junction permeability 19,22,[25][26][27][28] . In vitro and in vivo studies have shown that TNF signals directly to intestinal epithelia to regulate barrier function via myosin light chain kinase (MLCK) activation 20, 29-33 .…”

Section: Introductionmentioning

confidence: 99%

LIGHT Signals Directly to Intestinal Epithelia to Cause Barrier Dysfunction via Cytoskeletal and Endocytic Mechanisms

et al. 2007

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BACKGROUND & AIMS-LIGHT (lymphotoxin-like inducible protein that competes with glycoprotein D for herpes virus entry on T cells) is a TNF core family member that regulates T cell activation and causes experimental inflammatory bowel disease. Additional data suggest that LIGHT may be involved in the pathogenesis of human inflammatory bowel disease. The aim of this study was to determine if LIGHT was capable of signaling directly to intestinal epithelia and to define the mechanisms and consequences of such signaling.

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Modulation of barrier function during Fas-mediated apoptosis in human intestinal epithelial cells

Cited by 121 publications

References 39 publications

The specific fates of tight junction proteins in apoptotic epithelial cells

The specific fates of tight junction proteins in apoptotic epithelial cells

β-Defensin-2 Expression Is Regulated by TLR Signaling in Intestinal Epithelial Cells

LIGHT Signals Directly to Intestinal Epithelia to Cause Barrier Dysfunction via Cytoskeletal and Endocytic Mechanisms

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