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Gene Review

CLDN4  -  claudin 4

Homo sapiens

Synonyms: CPE-R, CPE-receptor, CPER, CPETR, CPETR1, ...
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Disease relevance of CLDN4


Psychiatry related information on CLDN4


High impact information on CLDN4

  • To test whether members of the claudin family of tight junction proteins influence paracellular ionic selectivity, we expressed human claudin-4 in cultured MDCK cells using an inducible promoter [7].
  • A decrease in conductance correlated directly with the kinetics of claudin-4 induction [7].
  • Epithelial resistance was diminished from 44 +/- 3 to 29 +/- 2 Omega x cm(2), and this was accompanied by a decrease in occludin and claudin-4 expression [8].
  • Using expression profiling, we previously found claudin-4 to be overexpressed in pancreatic cancer [9].
  • RESULTS: Expression analyses showed that claudin-4 was overexpressed in most pancreatic cancer tissues and cell lines and several other gastrointestinal tumors [9].

Chemical compound and disease context of CLDN4

  • The expression of E-cadherin, claudin 4, and ZO-1 was analyzed immuno-histochemically using formalin-fixed, paraffin-embedded tissues obtained from 49 patients who underwent radical resection for advanced gastric cancer [10].
  • Statistical analyses showed that the beta8 integrin subunit, claudin-4, and S100A1 provided the best distinction between ovarian carcinoma and normal ovary tissues, and may serve as the best candidate tumor markers among the seven genes studied [11].

Biological context of CLDN4


Anatomical context of CLDN4

  • CONCLUSIONS: These results show that CLDN3 and CLDN4 are frequently up-regulated in ovarian tumors and cell lines and may represent novel markers for this disease [4].
  • However, CLDN4 was highly positive in normal epithelial cells and was decreased or absent in 17 out of 21 ductal carcinoma grade 1, in special types of breast carcinoma (mucinous, papillary, tubular) and in areas of apocrine metaplasia [3].
  • The observations of lack of claudin 4 and low expression of claudin 3 in OSE strengthen our current knowledge about the biological nature of these cells as an undeveloped epithelium [5].
  • Northern blot analysis of CPETR1 demonstrates tissue specificity, with expression in kidney, lung, thyroid, and gastrointestinal tissues [12].
  • Human and mouse cDNAs showing homology to the Clostridium perfringens enterotoxin (CPE) receptor gene (CPE-R) from Vero cells (DDBJ/EMBL/GenBankTM accession no. D88492) (Katahira, J., Inoue, N., Horiguchi, Y., Matsuda, M., and Sugimoto, N. (1997) J. Cell Biol. 136, 1239-1247) were cloned [13].

Associations of CLDN4 with chemical compounds


Regulatory relationships of CLDN4


Other interactions of CLDN4


Analytical, diagnostic and therapeutic context of CLDN4


  1. Crucial roles of Sp1 and epigenetic modifications in the regulation of the CLDN4 promoter in ovarian cancer cells. Honda, H., Pazin, M.J., Ji, H., Wernyj, R.P., Morin, P.J. J. Biol. Chem. (2006) [Pubmed]
  2. Role of claudins in tumorigenesis. Swisshelm, K., Macek, R., Kubbies, M. Adv. Drug Deliv. Rev. (2005) [Pubmed]
  3. Claudin-1, -3 and -4 proteins and mRNA expression in benign and malignant breast lesions: a research study. Tokés, A.M., Kulka, J., Paku, S., Szik, A., Páska, C., Novák, P.K., Szilák, L., Kiss, A., Bögi, K., Schaff, Z. Breast Cancer Res. (2005) [Pubmed]
  4. Tight junction proteins claudin-3 and claudin-4 are frequently overexpressed in ovarian cancer but not in ovarian cystadenomas. Rangel, L.B., Agarwal, R., D'Souza, T., Pizer, E.S., Alò, P.L., Lancaster, W.D., Gregoire, L., Schwartz, D.R., Cho, K.R., Morin, P.J. Clin. Cancer Res. (2003) [Pubmed]
  5. Differences in expression patterns of the tight junction proteins,claudin 1, 3, 4 and 5, in human ovarian surface epithelium as compared to epithelia in inclusion cysts and epithelial ovarian tumours. Zhu, Y., Brännström, M., Janson, P.O., Sundfeldt, K. Int. J. Cancer (2006) [Pubmed]
  6. Psychometric properties of the Chinese version of the Psycho-educational Profile-Revised (CPEP-R). Shek, D.T., Tsang, S.K., Lam, L.L., Tang, F.L., Cheung, P.M. Journal of autism and developmental disorders. (2005) [Pubmed]
  7. Regulated expression of claudin-4 decreases paracellular conductance through a selective decrease in sodium permeability. Van Itallie, C., Rahner, C., Anderson, J.M. J. Clin. Invest. (2001) [Pubmed]
  8. Mechanisms of diarrhea in collagenous colitis. Bürgel, N., Bojarski, C., Mankertz, J., Zeitz, M., Fromm, M., Schulzke, J.D. Gastroenterology (2002) [Pubmed]
  9. Claudin-4: a new target for pancreatic cancer treatment using Clostridium perfringens enterotoxin. Michl, P., Buchholz, M., Rolke, M., Kunsch, S., Löhr, M., McClane, B., Tsukita, S., Leder, G., Adler, G., Gress, T.M. Gastroenterology (2001) [Pubmed]
  10. Loss of the tight junction protein claudin 4 correlates with histological growth-pattern and differentiation in advanced gastric adenocarcinoma. Lee, S.K., Moon, J., Park, S.W., Song, S.Y., Chung, J.B., Kang, J.K. Oncol. Rep. (2005) [Pubmed]
  11. Differential gene expression in ovarian carcinoma: identification of potential biomarkers. Hibbs, K., Skubitz, K.M., Pambuccian, S.E., Casey, R.C., Burleson, K.M., Oegema, T.R., Thiele, J.J., Grindle, S.M., Bliss, R.L., Skubitz, A.P. Am. J. Pathol. (2004) [Pubmed]
  12. Genes for the CPE receptor (CPETR1) and the human homolog of RVP1 (CPETR2) are localized within the Williams-Beuren syndrome deletion. Paperna, T., Peoples, R., Wang, Y.K., Kaplan, P., Francke, U. Genomics (1998) [Pubmed]
  13. Clostridium perfringens enterotoxin utilizes two structurally related membrane proteins as functional receptors in vivo. Katahira, J., Sugiyama, H., Inoue, N., Horiguchi, Y., Matsuda, M., Sugimoto, N. J. Biol. Chem. (1997) [Pubmed]
  14. Novel effects of azithromycin on tight junction proteins in human airway epithelia. Asgrimsson, V., Gudjonsson, T., Gudmundsson, G.H., Baldursson, O. Antimicrob. Agents Chemother. (2006) [Pubmed]
  15. Overexpression of human WNK1 increases paracellular chloride permeability and phosphorylation of claudin-4 in MDCKII cells. Ohta, A., Yang, S.S., Rai, T., Chiga, M., Sasaki, S., Uchida, S. Biochem. Biophys. Res. Commun. (2006) [Pubmed]
  16. Depletion of Caco-2 cell cholesterol disrupts barrier function by altering the detergent solubility and distribution of specific tight-junction proteins. Lambert, D., O'Neill, C.A., Padfield, P.J. Biochem. J. (2005) [Pubmed]
  17. Induction of claudin-4 by nonsteroidal anti-inflammatory drugs and its contribution to their chemopreventive effect. Mima, S., Tsutsumi, S., Ushijima, H., Takeda, M., Fukuda, I., Yokomizo, K., Suzuki, K., Sano, K., Nakanishi, T., Tomisato, W., Tsuchiya, T., Mizushima, T. Cancer Res. (2005) [Pubmed]
  18. The claudin gene family: expression in normal and neoplastic tissues. Hewitt, K.J., Agarwal, R., Morin, P.J. BMC Cancer (2006) [Pubmed]
  19. Claudin-3 and claudin-4 expression in ovarian epithelial cells enhances invasion and is associated with increased matrix metalloproteinase-2 activity. Agarwal, R., D'Souza, T., Morin, P.J. Cancer Res. (2005) [Pubmed]
  20. PPARgamma-regulated tight junction development during human urothelial cytodifferentiation. Varley, C.L., Garthwaite, M.A., Cross, W., Hinley, J., Trejdosiewicz, L.K., Southgate, J. J. Cell. Physiol. (2006) [Pubmed]
  21. Endothelia of term human placentae display diminished expression of tight junction proteins during preeclampsia. Liévano, S., Alarcón, L., Chávez-Munguía, B., González-Mariscal, L. Cell Tissue Res. (2006) [Pubmed]
  22. Claudin-4 expression decreases invasiveness and metastatic potential of pancreatic cancer. Michl, P., Barth, C., Buchholz, M., Lerch, M.M., Rolke, M., Holzmann, K.H., Menke, A., Fensterer, H., Giehl, K., Löhr, M., Leder, G., Iwamura, T., Adler, G., Gress, T.M. Cancer Res. (2003) [Pubmed]
  23. Expression, solubilization, and biochemical characterization of the tight junction transmembrane protein claudin-4. Mitic, L.L., Unger, V.M., Anderson, J.M. Protein Sci. (2003) [Pubmed]
  24. Differential expression of claudin-4 between intestinal and diffuse-type gastric cancer. Kuo, W.L., Lee, L.Y., Wu, C.M., Wang, C.C., Yu, J.S., Liang, Y., Lo, C.H., Huang, K.H., Hwang, T.L. Oncol. Rep. (2006) [Pubmed]
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