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Gene Review

OCLN  -  occludin

Canis lupus familiaris

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Disease relevance of OCLN

  • Distinct effects of Vibrio cholerae haemagglutinin/protease on the structure and localization of the tight junction-associated proteins occludin and ZO-1 [1].

High impact information on OCLN

  • The tight junction components ZO-1, ZO-2, endogenous ZO-3, and occludin were mislocalized during the early stages of tight junction assembly [2].
  • NZO-3 expression did not alter expression levels of ZO-1, ZO-2, endogenous ZO-3, occludin, or E-cadherin; however, the amount of Triton X-100-soluble, signaling-active beta-catenin was increased in NZO-3-expressing cells during junction assembly [2].
  • In vitro binding experiments showed that ZO-1 and actin preferentially bind to NZO-3, whereas both NZO-3 and the carboxy-terminal half of the molecule (CZO-3) contain binding sites for occludin and cingulin [2].
  • In cultured monolayers of pure W cells, ouabain triggers the "P-->A mechanism" (from pump/adhesion) consisting of a cascade of phosphorylations that retrieves adhesion-associated molecules occludin and beta-catenin and results in detachment of the cell [3].
  • Inhibition of membrane traffic with 0.4 M sucrose also blocked occludin internalization and TER loss [4].

Biological context of OCLN


Anatomical context of OCLN

  • In the Madin-Darby canine kidney epithelial cell line, the proteins occludin and ZO-1 are structural components of the tight junctions that seal the paracellular spaces between the cells and contribute to the epithelial barrier function [7].
  • Hence, specific domains and functional properties of occludin modulate transepithelial migration of neutrophils [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 [7].
  • 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 [7].
  • Moreover, the apical structure of filamentous actin (F-actin) was disturbed and tight junction-associated proteins (ZO-1 and occludin) were dispersed along the basolateral membranes [9].

Associations of OCLN with chemical compounds

  • Western blot analysis showed that occludin bands of 66-85 kDa were digested by HA/P to two predominant bands of around 50 kDa and 35 kDa, and that this degradation was greatly attenuated when the specific bacterial metalloproteinase inhibitor Zincov was co-administered [1].
  • Diatrizoate, and to a lesser extent ioxaglate, reduced the number of viable MDCK cells and showed a redistribution of the E-cadherin, ZO-1 and occludin immunofluorescence signal with a parallel decrease of the TMR indicating an impaired monolayer integrity [10].
  • Expression of Rho mutant proteins in MDCK cells also altered levels of occludin serine/threonine phosphorylation, indicating that occludin is a target for Rho signaling [11].
  • Furthermore, depletion of tight junction-localized occludin by an occludin extracellular domian peptide (20) correlated with a decrease in the HMW forms of occludin [12].

Other interactions of OCLN


Analytical, diagnostic and therapeutic context of OCLN


  1. Distinct effects of Vibrio cholerae haemagglutinin/protease on the structure and localization of the tight junction-associated proteins occludin and ZO-1. Wu, Z., Nybom, P., Magnusson, K.E. Cell. Microbiol. (2000) [Pubmed]
  2. Exogenous expression of the amino-terminal half of the tight junction protein ZO-3 perturbs junctional complex assembly. Wittchen, E.S., Haskins, J., Stevenson, B.R. J. Cell Biol. (2000) [Pubmed]
  3. Contacts and cooperation between cells depend on the hormone ouabain. Larre, I., Ponce, A., Fiorentino, R., Shoshani, L., Contreras, R.G., Cereijido, M. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  4. Actin depolymerization disrupts tight junctions via caveolae-mediated endocytosis. Shen, L., Turner, J.R. Mol. Biol. Cell (2005) [Pubmed]
  5. Occludin modulates transepithelial migration of neutrophils. Huber, D., Balda, M.S., Matter, K. J. Biol. Chem. (2000) [Pubmed]
  6. Reassembly of the tight junction after oxidative stress depends on tyrosine kinase activity. Meyer, T.N., Schwesinger, C., Ye, J., Denker, B.M., Nigam, S.K. J. Biol. Chem. (2001) [Pubmed]
  7. 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]
  8. Expression of occludin in canine testis and epididymis. Gye, M.C. Reprod. Domest. Anim. (2004) [Pubmed]
  9. Apically exposed, tight junction-associated beta1-integrins allow binding and YopE-mediated perturbation of epithelial barriers by wild-type Yersinia bacteria. Tafazoli, F., Holmström, A., Forsberg, A., Magnusson, K.E. Infect. Immun. (2000) [Pubmed]
  10. Ionic radiocontrast media disrupt intercellular contacts via an extracellular calcium-independent mechanism. Schick, C.S., Bangert, R., Kübler, W., Haller, C. Exp. Nephrol. (2002) [Pubmed]
  11. Rho GTPase signaling regulates tight junction assembly and protects tight junctions during ATP depletion. Gopalakrishnan, S., Raman, N., Atkinson, S.J., Marrs, J.A. Am. J. Physiol. (1998) [Pubmed]
  12. Phosphorylation of occludin correlates with occludin localization and function at the tight junction. Wong, V. Am. J. Physiol. (1997) [Pubmed]
  13. The specific fates of tight junction proteins in apoptotic epithelial cells. Bojarski, C., Weiske, J., Schöneberg, T., Schröder, W., Mankertz, J., Schulzke, J.D., Florian, P., Fromm, M., Tauber, R., Huber, O. J. Cell. Sci. (2004) [Pubmed]
  14. Platelet-derived growth factor mediates tight junction redistribution and increases permeability in MDCK cells. Harhaj, N.S., Barber, A.J., Antonetti, D.A. J. Cell. Physiol. (2002) [Pubmed]
  15. Comparative cytotoxicity of ionic and non-ionic radiocontrast agents on MDCK cell monolayers in vitro. Schick, C.S., Haller, C. Nephrol. Dial. Transplant. (1999) [Pubmed]
  16. Transplantable urothelial cell sheets harvested noninvasively from temperature-responsive culture surfaces by reducing temperature. Shiroyanagi, Y., Yamato, M., Yamazaki, Y., Toma, H., Okano, T. Tissue engineering. (2003) [Pubmed]
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