Publication for Epcam and Cldn7

Species	Symbol	Function*	Entrez Gene ID*	Other ID	Gene coexpression	CoexViewer
mmu	Epcam	epithelial cell adhesion molecule	17075			[link]
mmu	Cldn7	claudin 7	53624

Pubmed ID	Priority	Text
25171873	0.99	Ep-Cam, since Ep-Cam depletion results in claudin-7 relocalization to tight junctions.
30015855	0.98	EpCAM and claudin-7 have been demonstrated to colocalize at the basolateral surface of the intestine, pancreas, stomach, lungs and kidneys in wild type (WT) mice, detected by fluorescent immunohistochemistry.
	0.98	claudin-7 is associated with claudin-1 and facilitates the incorporation of claudin-1 into EpCAM-containing complexes.
	0.98	EpCAM-like protein that associates with claudin-7.
	0.98	claudin-7, the levels of claudins 2, 3, and 15 are also reduced in the intestine of EpCAM mutant mice; claudins 2, 3, 7, and 15 co-precipitate with each other from mouse intestinal lysates.
	0.98	EpCAM directly binds claudin-7, which in turn facilitates the incorporation of claudin-1 into the EpCAM-containing complexes.
	0.98	EpCAM and claudin-7, together with E-cadherin, are essential to keep the balance between AJs and cortical tension (Fig. 2A).
	0.98	EpCAM and claudin-7 would result in loss of balance between AJs and cortical tension, affecting the function of AJs leading to the mislocalization of TJs (Fig. 2B).
	0.98	EpCAM and claudin-7 complex, together with E-cadherin, is essential to keep the balance between AJs and cortical tension.
	0.97	Claudin-7 is the first member of the family of claudins which was reported in a study investigating the association between EpCAM and claudins in both non-transformed tissues and metastasizing tumor cell lines.
	0.97	Claudin-7 was first detected in a CD44v6-tetraspanis-EpCAM complex, and later it was confirmed that claudin-7 associates directly with EpCAM.
	0.97	claudin-7 and claudin-1 are associated with the reduction of EpCAM expression indicates that the alterations are post-transcriptional.
	0.97	EpCAM-claudin-7-CD4 4v6-tetraspanis, which may be important during tumori-genesis.
	0.97	EpCAM and claudin-7 proteins are lost in AJs.
	0.97	EpCAM, claudin-7, CO-029, and CD44v6 is frequently formed in colorectal cancer, and this complex, but not the individual molecules, may promote the progression of colorectal cancer and increase the apoptosis resistance of cancer cells.
	0.96	EpCAM mutant embryos, claudin-7 protein is downregulated to undetectable levels in all regions of the intestine examined, but claudin-7 mRNA is still normal in the mutant intestine.
	0.96	Claudin-7 protein is also downregulated to undetectable levels in the pancreas, lungs and stomach of EpCAM knockout mice, but there are still some weak claudin-7 protein signals in the EpCAM mutant kidneys.
	0.96	EpCAM leads to decreased expression and mislocalization of EpCAM in the intestinal epithelium rather than along the plasma membrane, meanwhile, the expression of claudin-7 protein is also decreased, and the co-localization with EpCAM 4 protein is lost, although claudin-7 mRNA levels remain unaltered.
	0.96	claudin-7 and claudin-1 proteins in EpCAM knockout samples or EpCAM knockdown cells.
	0.96	claudin-7 protein is reduced to undetectable levels in the intestines of EpCAM mutant mice and CTE patients.
	0.95	Claudin-7 has been observed in TJs and basolateral membranes; the co-localization of EpCAM and claudin-7 has also been observed on both TJs and basolateral membranes.
	0.95	EpCAM is required for association with claudin-7, and claudin-7 is unable to associate with EpCAM if A279 and G282 are changed to I279 and I282.
	0.94	claudin-7 knockout mice, the precise manner of the interaction between EpCAM and various claudins remains to be determined.
	0.94	EpCAM knockout intestinal epithelium, the EpCAM and claudin-7 complex is completely lost; as is the balance between AJs and cortical tension.
	0.92	Claudin-7 was not detected in the intestine, lungs, stomach, and pancreas of EpCAM mutant mice, however is still detected in the kidney epithelium, albeit at reduced levels.
	0.92	EpCAM, claudin-7, other claudins, occludin and other junction connections is equal with the cortical tension between two epithelial cells; but the direction of the total pulling force is opposite to that of cortical tension.
	0.91	EpCAM is directly associated with claudin-7.
	0.90	EpCAM mutant mice, but it is normal in claudin-7 knockout mice.
	0.80	Claudin-7 protein is decreased when EpCAM is lost.
30623107	0.98	Epcam and claudin-7 was severely disrupted by Spint2 deletion.
	0.98	Epcam immunoreactivity and mislocalization within the cytoplasm of disorganized epithelial cells, particularly in cells forming tufts, as well as accompanying decreases in claudin-7 immunoreactivity (Fig. 6a).
	0.98	Epcam and claudin-7 in organoids after 4-OHT treatment (Fig. 7a).
	0.98	Epcam/claudin-7 complex in the intestine.
	0.98	Epcam cleavage by matriptase and destabilization of the Epcam/claudin-7 complex.
	0.97	Epcam in the absence of Hai-2 as well as markedly decreased claudin-7 levels (Fig. 7a).
	0.97	Epcam and claudin-7 mRNA levels were not affected (Supplementary Fig. 4), indicating that the decrease in cell surface Epcam and claudin-7 in response to Spint2-deletion occurred at a post-translational level.
	0.97	Epcam cleavage in a dose-dependent manner, accompanying stabilization of claudin-7 (Fig. 9c).
	0.97	Epcam/claudin-7 complex in the intestine, and Hai-2 may have additional, vital functions for epithelial cells in vivo.
	0.97	Epcam/claudin-7 complex.
	0.96	Epcam cleavage accompanied by significantly decreased intensity of claudin-7 bands; this effect was rescued completely by aprotinin.
	0.96	Epcam cleavage, stabilized claudin-7 levels (Fig. 8c, d) and rescued destruction of crypt organoids caused by Hai-2 ablation (Fig. 8e).
	0.96	EPCAM gene wherein abnormal EpCAM function destabilizes EpCAM-associated claudin-7, which eventually results in abnormally enhanced epithelial permeability.
	0.96	Epcam cleavage in the absence of Hai-2, and consequently maintained the claudin-7 levels and rescued organoids from subsequent rupture.
	0.95	Epcam cleavage with decreased claudin-7 levels and resulted in organoid rupture.
	0.95	Epcam and claudin-7 after Hai-2 ablation and increased mucosal permeability in vivo.
	0.94	Epcam and one of its essential partners in the intestinal epithelium, claudin-7.
	0.94	Epcam cleavage and concomitant decreases in claudin-7 levels (Fig. 7a).
	0.89	Epcam and claudin-7 immunoreactivity was also observed in Hai-2-deficient extrahepatic biliary epithelium (Fig. 6d).
	0.85	Epcam cleavage and claudin-7 loss were alleviated by Prss8 ablation.
	0.78	Epcam/claudin-7 complex by Hai-2 loss
29617460	0.98	EpCAM in cultured intestinal epithelial cells, causing premature degradation of the tight junction protein claudin-7.
	0.97	EpCAM protein expression was an early event in the HAI-2-deficient intestine, and that this was followed by a progressive loss of claudin-7, claudin-1 and E-cadherin, but an increase in gene and protein expression of claudin-4.
	0.97	EpCAM protein, followed by a decrease in claudin-7 expression in Spint2-/-;Prss8R44Q/R44Q mice mimic closely molecular changes induced by unregulated matriptase activity in HAI-2-silenced intestinal cell monolayers.
	0.96	EpCAM and claudin-1 as early as on E18.5, followed by a decreased expression of E-cadherin and claudin-7, and an increased expression of claudin-4 on postnatal days 2 and 4.
	0.91	EpCAM, E-cadherin, and claudin-7, indicating that the phenotype of Spint2-/-; Prss8R44Q/R44Q mice recapitulates early events in the development of CTE in humans and provides an excellent model for study of the etiology and treatment of this debilitating disease.
28455726	0.98	claudin-7 was shown to complex with EpCAM, an epithelial adhesion molecule enriched at the basolateral membrane of intestinal and other cells.
	0.98	EpCAM was knocked down in intestinal cells, the small amount of claudin -7 remaining was localized to tight junctions.
	0.98	claudin-7 recruits EpCAM to glycolipid-enriched membrane domains, often designated as lipid rafts.
	0.97	claudin-7 knockout mice led Ding and associates to conclude that claudin-7, interacting with EpCAM and integrin-alpha2 mediates lateral cell-cell interactions as well as interactions with the cell-matrix.
30304739	0.98	EpCAM leads to loss of Claudin-7 from intestinal epithelial cells in mice and to defective tight junctions.
	0.97	EpCAM causes loss of Claudin-7 from the intestinal epithelium which is associated with congenital tufting enteropathy and loss of intestinal epithelial integrity in mice and humans.
	0.96	EpCAM in mice has been reported to cause loss of Claudin-7 protein from intestinal epithelium but not of Claudin-7 mRNA.
28084299	0.98	claudin-7, a component of the paracellular barrier permeability, was impaired in CTE enterocytes (Fig. 1e), as seen in EpCAM mutant mice.
	0.97	claudin-7 mislocalization to TCs and expression level decrease occurs in EpCAM-deprived cells (Figs 1e and 2h, Supplementary Fig. 2) and EpCAM mutant mice, as previously reported.
30288105	0.98	claudin-7 knockout mice show that the interaction of EpCAM with claudin is important in the gut.
	0.98	EpCAM recruits claudin-7 into TJs, and EpCAM knockout mice show downregulated claudin-7 expression and disruption of TJs.
21377456	0.98	EpCAM can also form complexes with the tight junction protein claudin-7, the variant isoform of cell-matrix adhesion protein CD44v6, and tetraspanin CD9, and this association-facilitated metastasis.
24665398	0.98	EpCAM and claudin-7 tend to be overexpressed by some highly metastatic tumors, however, EpCAM also has a role in regulating tight junction assembly, since EpCAM deficient mice have decreased incorporation of several claudins into junctions.
25123931	0.98	claudin-7 to tight junctions in mouse epithelial cells is regulated by EpCAM, while another report revealed that forced expression of snail leads to a reduction in claudin-7 expression.
27106675	0.98	EpCAM accomplishes this by associating with claudin-1 and claudin-7 and protecting these TJ-associated proteins from lysosomal degradation.
28368391	0.98	EpCAM, claudin-7 and CD44 (for a review, see Hemler).
29371425	0.98	Epcam, Cldn6 and Cldn7 were upregulated in single Mesp1 KO cells (Fig. 2D-F and Table S1), consistent with the defect of exiting the pluripotent epiblast stage.
29498629	0.98	epithelial cell adhesion molecule (EpCAM) and its associated protein Claudin-7 were shown to promote pluripotency reprogramming through upregulation of pluripotency transcription factors and repression of p53 and p21 expression.
24665401	0.96	EpCAM knockout mice show defects in intestinal barrier function, decreases in the levels of claudin-2, -3 and -15 and loss of claudin-7 along with disarranged tight junction fibrils.
25307947	0.96	EpCAM, Claudin7, and Oct 4, which were all increased in the SPTBN1 knockdown HCC cell lines (Figure 2).
23284647	0.95	Cldn7, Dsg2, Gjb3, Tjp2, Esrp1, Rab25, and Epcam (Figure 4J).
24885350	0.89	EpCAM or claudin-7 reduces tumor growth and metastasis in mice, and knockdown of both is more effective.
21460854	0.80	Epcam, claudin4, and claudin7, that are highly expressed in 4T1-miR-155 cells and represent genes that are over-expressed in 4T1-miR-155 epithelial cells.