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CLDN2 may have a role regulating tissue-specific physiological properties in tight junctions in UC.
the accumulation of DXR (show DXR Proteins) into spheroids was enhanced by claudin-2 knockdown, resulting in a reduction in cell viability. We suggest that claudin-2 may be a novel therapeutic target in lung adenocarcinoma, because claudin-2 knockdown increased the accumulation of anticancer agents in cancer cells and spheroids.
integration of claudin-2, occludin (show OCLN Proteins) and ZO-1 (show TJP1 Proteins) is necessary for maintaining the function of the proximal tubular epithelium.
these findings provide a novel mechanism by which microbial-derived butyrate promotes barrier through IL-10RA (show IL10RA Proteins)-dependent repression of claudin-2
Low CLDN2 expression is associated with Lung Cancer metastasis.
results reveal that IL-22 (show IL22 Proteins) increases intestinal epithelial permeability by upregulating Claudin-2 expression through the JAK (show JAK3 Proteins)/STAT (show STAT1 Proteins) pathway
In summary, we demonstrate that TCPTP (show PTPN2 Proteins) protects the intestinal epithelial barrier by restricting STAT (show STAT1 Proteins)-induced claudin-2 expression.
The cation channel (show TRPV1 Proteins)-forming tight junction protein (show OCLN Proteins) claudin-2 was shown to permit the paracellular passage of water through its pore.
suggest that epigenetic inhibitors suppress the abnormal proliferation of lung adenocarcinoma cells highly expressing claudin-2
Data show that alterations in myosin light chain kinase (show MYLK Proteins) activity, claudin-15 (show CLDN15 Proteins) and claudin-2 expression are associated with gluten-induced symptomatology and intestinal permeability changes in diarrhea-predominant irritable bowel syndrome (IBS-D).
claudin-2-null mice conserve sodium to the same extent as WT mice, even during profound dietary sodium depletion, as a result of the upregulation of transcellular Na-K-2Cl transport activity in the thick ascending limb of Henle
The tight junction patch clamp technique indicated mouse claudin-2 ion channel opening events in MDCK cells
The current study reveals an important and novel mechanism for VDR by regulation of epithelial barriers.
findings reveal a critical albeit complex role of claudin-2 in intestinal homeostasis by regulating epithelial permeability, inflammation and proliferation
Based on studies of Cldn2(-/-) mice, claudin 2 regulates paracellular ion and water flow required for proper regulation of bile composition and flow.
IL-6 (show IL6 Proteins) modulation of intestinal TJ permeability was regulated by JNK (show MAPK8 Proteins) activation of AP-1 (show JUN Proteins) and AP-1 (show JUN Proteins) activation of claudin-2 gene
this study set out to map out all the pore-lining residues of claudin-2 by comprehensive cysteine-scanning mutagenesis of the entire first extracellular loop (ECL1).
The capacity of non-AQP1 (show AQP1 Proteins)-dependent transcellular proximal fluid reabsorption (PFR) is sufficient to be maintained in AQP1 (show AQP1 Proteins)- and claudin-2-doubly deficient knockout mice.
These results suggest that the ERK (show EPHB2 Proteins) pathway positively regulates claudin-2 protein expression and claudin-2 is involved in lowering TER (show TECR Proteins) in CMT93-II cells.
This gene product belongs to the claudin protein family whose members have been identified as major integral membrane proteins localized exclusively at tight junctions. Claudins are expressed in an organ-specific manner and regulate tissue-specific physiologic properties of tight junctions. This protein is expressed in the intestine. Alternatively spliced transcript variants with different 5' untranslated region have been found for this gene.
, integral membrane protein claudin-2