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Gene Review

CLDN1  -  claudin 1

Canis lupus familiaris

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Disease relevance of CLDN1

 

High impact information on CLDN1

 

Anatomical context of CLDN1

  • Claudin-1 is an integral membrane protein component of tight junctions [1].
  • Taken together, these results support the hypothesis that Claudin-1 is a direct downstream target gene of Snail family factors in epithelial cells [1].
  • In Ras-transformed Madin-Darby canine kidney cells, occludin, claudin-1, and ZO-1 were absent from cell-cell contacts but were present in the cytoplasm, and the adherens junction protein E-cadherin was weakly expressed [5].
  • After treatment of the Ras-transformed cells with the mitogen-activated protein kinase kinase (MEK1) inhibitor PD98059, which blocks the activation of mitogen-activated protein kinase (MAPK), occludin, claudin-1, and ZO-1 were recruited to the cell membrane, tight junctions were assembled, and E-cadherin protein expression was induced [5].
 

Regulatory relationships of CLDN1

  • Moreover, the formation of the claudin-based TJs required a greater amount of activated Cdc42 than that of the E-cadherin-based AJs [7].
 

Analytical, diagnostic and therapeutic context of CLDN1

References

  1. The transcription factors Slug and Snail act as repressors of Claudin-1 expression in epithelial cells. Martínez-Estrada, O.M., Cullerés, A., Soriano, F.X., Peinado, H., Bolós, V., Martínez, F.O., Reina, M., Cano, A., Fabre, M., Vilaró, S. Biochem. J. (2006) [Pubmed]
  2. Phosphorylation of ephrin-B1 via the interaction with claudin following cell-cell contact formation. Tanaka, M., Kamata, R., Sakai, R. EMBO J. (2005) [Pubmed]
  3. HGF converts ErbB2/Neu epithelial morphogenesis to cell invasion. Khoury, H., Naujokas, M.A., Zuo, D., Sangwan, V., Frigault, M.M., Petkiewicz, S., Dankort, D.L., Muller, W.J., Park, M. Mol. Biol. Cell (2005) [Pubmed]
  4. Involvement of the c-Src-Crk-C3G-Rap1 signaling in the nectin-induced activation of Cdc42 and formation of adherens junctions. Fukuyama, T., Ogita, H., Kawakatsu, T., Fukuhara, T., Yamada, T., Sato, T., Shimizu, K., Nakamura, T., Matsuda, M., Takai, Y. J. Biol. Chem. (2005) [Pubmed]
  5. Restoration of tight junction structure and barrier function by down-regulation of the mitogen-activated protein kinase pathway in ras-transformed Madin-Darby canine kidney cells. Chen, Y., Lu, Q., Schneeberger, E.E., Goodenough, D.A. Mol. Biol. Cell (2000) [Pubmed]
  6. Role of nectin in organization of tight junctions in epithelial cells. Fukuhara, A., Irie, K., Yamada, A., Katata, T., Honda, T., Shimizu, K., Nakanishi, H., Takai, Y. Genes Cells (2002) [Pubmed]
  7. Involvement of nectin-activated Cdc42 small G protein in organization of adherens and tight junctions in Madin-Darby canine kidney cells. Fukuhara, A., Shimizu, K., Kawakatsu, T., Fukuhara, T., Takai, Y. J. Biol. Chem. (2003) [Pubmed]
  8. 2,3-butanedione monoxime (BDM), a potent inhibitor of actin-myosin interaction, induces ion and fluid transport in MDCK monolayers. Castillo, A.M., Reyes, J.L., Sánchez, E., Mondragón, R., Meza, I. J. Muscle Res. Cell. Motil. (2002) [Pubmed]
  9. Modulation of the epithelial barrier by dexamethasone and prolactin in cultured Madin-Darby canine kidney (MDCK) cells. Peixoto, E.B., Collares-Buzato, C.B. Cell Biol. Int. (2006) [Pubmed]
 
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