&lt;i&gt;Streptococcus pyogenes&lt;/i&gt; translocates across an epithelial barrier

Sumitomo, Tomoko

doi:10.3412/jsb.72.213

Cited by 2 publications

(1 citation statement)

References 19 publications

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“…CLDN2 is a member of the claudin family. Claudin proteins play important roles in the formation and maintenance of tight junctions among cells ( 28 ). Tight junctions divide the epithelial plasma membrane into apical and basal sides, resulting in cell polarity, but have selective permeability to different types of molecules and ions ( 29 ).…”

Section: Discussionmentioning

confidence: 99%

miR-331 inhibits CLDN2 expression and may alleviate the vascular endothelial injury induced by sepsis

Kong

2020

Exp Ther Med

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Section: Discussionmentioning

confidence: 99%

miR-331 inhibits CLDN2 expression and may alleviate the vascular endothelial injury induced by sepsis

Kong

2020

Exp Ther Med

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Faecal Proteases from Pouchitis Patients Activate Protease Activating Receptor-2 to Disrupt the Epithelial Barrier

Hoffman

Cohen

Carroll

et al. 2019

Journal of Crohn's and Colitis

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Background and Aims The pathogenesis of pouch inflammation may involve epithelial barrier disruption. We investigated whether faecal proteolytic activity is increased during pouchitis and results in epithelial barrier dysfunction through protease activating receptor [PAR] activation, and assessed whether the intestinal microbiome may be the source of the proteases. Methods Faecal samples were measured for protease activity using a fluorescein isothiocyanate [FITC]-casein florescence assay. Caco-2 cell monolayers were exposed to faecal supernatants to assess permeability to FITC-dextran. Tight junction protein integrity and PAR activation were assessed by immunoblot and immunofluorescence. A truncated PAR2 protein in Caco-2 cells was achieved by stable transfection using CRISPR/Cas9 plasmid. PAR2 activation in pouch biopsies was examined using antibodies directed to the N-terminus of the protein. Microbial composition was analysed based on 16S rRNA gene sequence analysis. Results Ten pouchitis patients, six normal pouch [NP] patients and nine healthy controls [HC] were recruited. The pouchitis patients exhibited a 5.19- and 5.35-fold higher faecal protease [FP] activity [p ≤ 0.05] compared to the NP and HC participants, respectively. The genus Haemophilus was positively associated with FP activity [R = 0.718, false discovery rate < 0.1]. Faecal supernatants from pouchitis patients activated PAR2 on Caco-2 monolayers, disrupted tight junction proteins and increased epithelial permeability. PAR2 truncation in Caco-2 abrogated faecal protease-mediated permeability. Pouch biopsies obtained from pouchitis patients, but not from NP patients, displayed PAR2 activation. Conclusions Protease-producing bacteria may increase faecal proteolytic activity that results in pouch inflammation through disruption of tight junction proteins and increased epithelial permeability in a PAR2-dependent manner. This mechanism may initiate or propagate pouch inflammation.

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<i>Streptococcus pyogenes</i> translocates across an epithelial barrier

Cited by 2 publications

References 19 publications

miR-331 inhibits CLDN2 expression and may alleviate the vascular endothelial injury induced by sepsis

miR-331 inhibits CLDN2 expression and may alleviate the vascular endothelial injury induced by sepsis

Faecal Proteases from Pouchitis Patients Activate Protease Activating Receptor-2 to Disrupt the Epithelial Barrier

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