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Claudin 2

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.[provided by RefSeq, Jan 2010] (from NCBI)
Top mentioned proteins: Occludin, claudin-1, ZO-1, claudin-4, claudin-3
Papers on claudin-2
Segmental Differences in Radiation-Induced Alterations of Tight Junction-Related Proteins in Non-Human Primate Jejunum, Ileum and Colon.
Hauer-Jensen et al., Québec, Canada. In Radiat Res, Jan 2016
Western blot analysis revealed increased levels of claudin-2 on day 4 and of JAM-1 on day 7 postirradiation in all three gut segments.
Increased urothelial paracellular transport promotes cystitis.
Carattino et al., Pittsburgh, United States. In Am J Physiol Renal Physiol, Jan 2016
To determine whether urothelial barrier dysfunction is sufficient to promote cystitis, we employed in situ adenoviral transduction to selectively overexpress the pore-forming tight junction-associated protein claudin-2 (CLDN-2).
Claudin-2-dependent paracellular channels are dynamically gated.
Turner et al., Chicago, United States. In Elife, Dec 2015
We report a novel trans-tight junction patch clamp technique that detects flux across individual claudin-2 channels within the tight junction of cultured canine renal tubule or human intestinal epithelial monolayers.
Resveratrol induces chemosensitization to 5-fluorouracil through up-regulation of intercellular junctions, Epithelial-to-mesenchymal transition and apoptosis in colorectal cancer.
Shakibaei et al., München, Germany. In Biochem Pharmacol, Dec 2015
Interestingly, resveratrol induced a transition from 5-FU-induced formation of microvilli to a planar cell surface, which was concomitant with up-regulation of desmosomes, gap- and tight junctions (claudin-2) and adhesion molecules (E-cadherin) expression in HCT116 and HCT116R cells.
Structural and Functional Changes in the Tight Junctions of Asymptomatic and Serology-negative First-degree Relatives of Patients With Celiac Disease.
Makharia et al., New Delhi, India. In J Clin Gastroenterol, Dec 2015
The ultrastructure of tight junctions using transmission electron microscopy, and the expression of key tight junction proteins (claudin-2, claudin-3, occludin, JAM-A, and ZO-1) and zonulin using real-time PCR and immunohistochemistry were assessed in anti-tTG Ab-negative, HLA-DQ2/-DQ8-positive FDRs having normal villi and in disease controls.
Necrotizing enterocolitis in a mouse model leads to widespread renal inflammation, acute kidney injury, and disruption of renal tight junction proteins.
Chen et al., Cleveland, United States. In Pediatr Res, Nov 2015
The membrane localization of claudin-2 was altered in the NEC kidneys and its immunostaining signal at TJ was disrupted.
Vitamin D receptor knockout mice exhibit elongated intestinal microvilli and increased ezrin expression.
Stangl et al., Halle, Germany. In Nutr Res, Nov 2015
We further observed a decrease in the messenger RNA and protein expression of the calcium-transporting tight junction protein claudin-2 in the VDR-KO mice compared with the WT mice (P < .05).
Curcumin prevents cisplatin-induced decrease in the tight and adherens junctions: relation to oxidative stress.
Pedraza-Chaverri et al., Mexico. In Food Funct, Nov 2015
The present study explored whether curcumin is able to prevent the cisplatin-induced fibrosis and decreased expression of the TJ and adherens junction (AJ) proteins occludin, claudin-2 and E-cadherin in cisplatin-induced nephrotoxicity.
Urinary Claudin-2 Measurements as a Predictor of Necrotizing Enterocolitis: A Pilot Study.
J Hunter M D et al., Chicago, United States. In J Neonatal Surg, Oct 2015
Immunofluorescence analysis of claudin-2 was performed on the intestinal tissue.
Tight junction, selective permeability, and related diseases.
Fromm et al., Berlin, Germany. In Semin Cell Dev Biol, 2014
All channel formers exhibit at least one of the three types of selectivity: for cations (claudin-2, -10b, -15), for anions (claudin-10a, -17) or for water (claudin-2).
Potentiometric-scanning ion conductance microscopy for measurement at tight junctions.
Hou et al., Bloomington, United States. In Tissue Barriers, 2013
This review summarizes recent advances in paracellular conductance recording with an emphasis on the P-SICM based approach, which is applied to detect claudin-2 mediated permeability changes at the tight junction.
Molecular mechanisms of vitamin D action.
Jurutka et al., Phoenix, United States. In Calcif Tissue Int, 2013
Thus, vitamin D action in a particular cell depends upon the metabolic production or delivery of sufficient concentrations of the 1,25D ligand, expression of adequate VDR and RXR coreceptor proteins, and cell-specific programming of transcriptional responses to regulate select genes that encode proteins that function in mediating the effects of vitamin D. For example, 1,25D induces RANKL, SPP1 (osteopontin), and BGP (osteocalcin) to govern bone mineral remodeling; TRPV6, CaBP(9k), and claudin 2 to promote intestinal calcium absorption; and TRPV5, klotho, and Npt2c to regulate renal calcium and phosphate reabsorption.
Common genetic variants in the CLDN2 and PRSS1-PRSS2 loci alter risk for alcohol-related and sporadic pancreatitis.
Devlin et al., Pittsburgh, United States. In Nat Genet, 2012
The CLDN2 risk allele is associated with atypical localization of claudin-2 in pancreatic acinar cells.
Claudins and the kidney.
Yu et al., Saint Louis, United States. In Annu Rev Physiol, 2012
Recent evidence has identified claudin-2 as constituting the cation-reabsorptive pathway in the proximal tubule; claudin-14, -16, and -19 as forming a complex that regulates calcium transport in the thick ascending limb of the loop of Henle; and claudin-4, -7, and -8 as determinants of collecting duct chloride permeability.
Claudin-2 promotes breast cancer liver metastasis by facilitating tumor cell interactions with hepatocytes.
Siegel et al., Montréal, Canada. In Mol Cell Biol, 2012
during breast cancer liver metastasis, claudin-2 shifts from acting within tight-junctional complexes to functioning as an adhesion molecule between breast cancer cells and hepatocytes.
SUMOylation of claudin-2.
Anderson et al., Bethesda, United States. In Ann N Y Acad Sci, 2012
Stable expression of inducible GFP-SUMO-1 in MDCK cells resulted in decreased levels of claudin-2 protein by immunoblot and decreased claudin-2 membrane expression
Claudins and other tight junction proteins.
Fromm et al., Berlin, Germany. In Compr Physiol, 2012
In contrast, a significant number of claudins form channels across TJs which feature selectivity for cations (claudins 2, 10b, and 15), anions (claudin-10a and -17), or are permeable to water (claudin-2).
Claudin-1, claudin-2 and claudin-11 genes differentially associate with distinct types of anti-inflammatory macrophages in vitro and with parasite- and tumour-elicited macrophages in vivo.
Van Ginderachter et al., Brussels, Belgium. In Scand J Immunol, 2012
we identified Cldn1, Cldn2 and Cldn11 as genes that discriminate between diverse types of M2 macrophages
Increase in claudin-2 expression by an EGFR/MEK/ERK/c-Fos pathway in lung adenocarcinoma A549 cells.
Sugatani et al., Shizuoka, Japan. In Biochim Biophys Acta, 2012
These results suggest that EGF is secreted from A549 cells by MMP and increases claudin-2 expression mediated via the activation of an EGFR/MEK/ERK pathway.
Interleukin-6 (IL-6) regulates claudin-2 expression and tight junction permeability in intestinal epithelium.
Tanabe et al., Hiroshima, Japan. In J Biol Chem, 2011
Claudin-2 promoter activity is increased by IL-6 in a MEK/ERK and PI3K-dependent manner
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