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These results identify EpCAM (show EPCAM Proteins) as a substrate of matriptase (show ST14 Proteins) and link HAI-2 (show SPINT2 Proteins), matriptase (show ST14 Proteins), EpCAM (show EPCAM Proteins), and claudin-7 in a functionally important pathway that causes disease when it is dysregulated.
84/118, 64/118, 52/118 reaction with claudin-1, claudin-3 (show CLDN3 Proteins) and claudin-4 (show CLDN4 Proteins) in cancer and colon polyps had a membrane localization, respectively.Mislocalization claudin-3 (show CLDN3 Proteins) to nucleus in colon cancer and mislocalization claudin-4 (show CLDN4 Proteins) to nucleus in adenomas of the colon were detected for the first time.
suggest that the reduction of CLDN5 (show CLDN5 Proteins), 7, and 18 expression loses the suppressive ability of interaction between PDK1 (show PDK1 Proteins) and Akt (show AKT1 Proteins) and causes sustained phosphorylation of Akt (show AKT1 Proteins), resulting in the disordered proliferation in lung squamous carcinoma cells
These results suggested that increase of Cldn4 (show CLDN4 Proteins)-expression may be involved in early molecular events during carcinogenesis of adenocarcinoma, whereas increase of Cldn7-expression may be associated with tumor invasion or progression.
that the dysregulated expression of these miRNAs, in conjunction with the high claudin 1 levels, could serve as a useful biomarker that identifies a subset of tumors within the poorly characterized basal-like subtype of breast cancer
localization of Cldn3 (show CLDN3 Proteins), Cldn7 and Cldn10 (show CLDN10 Proteins) proteins in the different compartments of murine endometrium up to day 8.5 of pregnancy (dpc) as well as in human endometrium and first trimester decidua
The expression of claudin-7 has no obviously difference between cervical carcinoma tissues and adjacent non-neoplastic tissues.
We identified hepatocyte nuclear factor 4alpha as a regulatory factor that bound endogenous CLDN7 promoter in differentiating intestinal epithelial cells and stimulated CLDN7 promoter activity.
claudin 1 and claudin 4 (show CLDN4 Proteins) are differentially involved in atopic dermatitis pathogenesis
we identified a previously unrecognized function of claudin-7 in regulating cell proliferation and maintaining epithelial cell attachment through engaging integrin beta1.
Data show that claudin-4 (show CLDN4 Proteins) and claudin-7 were observed in hepatocytes of severely damaged mouse and human livers.
The intestine-specific Cldn7 deficiency caused colonic inflammation, even though TJ structures were still present due to other claudins.
Salmonella targets the tight junction protein (show OCLN Proteins) claudin-2 (show CLDN2 Proteins) to facilitate bacterial invasion.
In mice, claudin-7 has non-TJ functions, including maintenance of epithelial cell-matrix interactions and intestinal homeostasis.
TSLP (show TSLP Proteins) induces expression of tight junction protein (show OCLN Proteins) claudin-7 in dendritic cells via NF-kappaB (show NFKB1 Proteins) as well as via TLRs and may control tight junctions of DCs to preserve the epithelial barrier during allergic inflammation
Claudin-7 is essential for NaCl homeostasis in distal nephrons, and the paracellular ion transport pathway plays indispensable roles in keeping ionic balance in kidneys.
claudin-7 was found in the same nephron segments as claudin-8 (show CLDN8 Proteins), but it was expressed primarily at the basolateral membrane
claudin 7 might be involved in vesicle trafficking to the basolateral membrane, possibly stabilizing cytoplasmic vesicles or participating in cell-matrix interactions
Tumor necrosis factor-alpha (show TNF Proteins) increases claudin-1 (show CLDN1 Proteins), 4, and 7 expression in renal tubular cells, altering permeability and transepithelial electrical resistance.
the effect of claudin-7 overexpression in LLC-PK1 cells on paracellular transport is mediated through a concurrent decrease in the paracellular conductance to Cl(-) and an increase in the paracellular conductance to Na(+).
These findings indicate that claudin-4 (show CLDN4 Proteins) and -7 may play a role in the gingiva junctional epithelium even in the absence of tight junctions.
This gene encodes a member of the claudin family. Claudins are integral membrane proteins and components of tight junction strands. Tight junction strands serve as a physical barrier to prevent solutes and water from passing freely through the paracellular space between epithelial or endothelial cell sheets, and also play critical roles in maintaining cell polarity and signal transductions. Differential expression of this gene has been observed in different types of malignancies, including breast cancer, ovarian cancer, hepatocellular carcinomas, urinary tumors, prostate cancer, lung cancer, head and neck cancers, thyroid carcinomas, etc.. Alternatively spliced transcript variants encoding different isoforms have been found.
, claudin-like protein ZF4A22
, clostridium perfringens enterotoxin receptor-like 2