The world's first wiki where authorship really matters (Nature Genetics, 2008). Due credit and reputation for authors. Imagine a global collaborative knowledge base for original thoughts. Search thousands of articles and collaborate with scientists around the globe.

wikigene or wiki gene protein drug chemical gene disease author authorship tracking collaborative publishing evolutionary knowledge reputation system wiki2.0 global collaboration genes proteins drugs chemicals diseases compound
Hoffmann, R. A wiki for the life sciences where authorship matters. Nature Genetics (2008)
Gene Review

OCLN  -  occludin

Homo sapiens

This record was replaced with 100506658.
Welcome! If you are familiar with the subject of this article, you can contribute to this open access knowledge base by deleting incorrect information, restructuring or completely rewriting any text. Read more.

Disease relevance of OCLN


High impact information on OCLN

  • The development of these junctions seems to depend on two primary processes: the appearance of high levels of the tight junction protein occludin and intracellular signaling processes that control the state of phosphorylation of junctional proteins [5].
  • Occludin and claudins in tight-junction strands: leading or supporting players [6]?
  • Overexpression increased the complexity of tight junction strands visible by freeze-fracture microscopy without affecting the levels of claudin-1, -2, or -3, occludin, or ZO-1 [7].
  • In confluent airway epithelial cells, Der p 1 led to cleavage of the TJ adhesion protein occludin [8].
  • Leaky epithelium in gammadelta(+) iIEL-deficient mice was associated with the absence of phosphorylation of serine residues of occludin and lack of claudin 3 and zona occludens-1 proteins in TJ complexes [9].

Psychiatry related information on OCLN

  • Our findings could be important in unravelling new pathogenic pathways in dementia disorders and new functions of occludin and TJs [10].

Chemical compound and disease context of OCLN


Biological context of OCLN

  • Further transfection studies with various deletion mutants showed that the domain E, especially its COOH-terminal approximately 150 amino acids (domain E358/504), was necessary for the localization of occludin at TJ [13].
  • Binding of an antibody to the first of the putative extracellular loops of occludin confirmed that this sequence was exposed on the cell surface, and synthetic peptides containing the amino acid sequence of this loop inhibit adhesion induced by occludin expression [14].
  • In the present study, we expressed occludin under an inducible promotor in occludin-null fibroblasts to determine whether this protein confers intercellular adhesion [14].
  • These results suggest that the extracellular surface of occludin is directly involved in cell-cell adhesion and the ability to confer adhesiveness correlates with the ability to colocalize with its cytoplasmic binding protein, ZO-1 [14].
  • While the N-terminal extracellular domains of occludin mediate homotypic adhesion, the distal C-terminal cytoplasmic domain of occludin controls protein targeting and endocytosis [15].

Anatomical context of OCLN

  • Furthermore, dendritic cells (DCs) of the medulla, with a major role for selection of thymocytes, expressed CLDN-1 and OCLN as well, implying that the interposition of DCs within the mTEC scaffold is also helped by TJs [16].
  • Occludin is an integral membrane protein localizing at tight junctions (TJ) with four transmembrane domains and a long COOH-terminal cytoplasmic domain (domain E) consisting of 255 amino acids [13].
  • Immunofluorescence and laser scan microscopy revealed that chick full-length occludin introduced into human and bovine epithelial cells was correctly delivered to and incorporated into preexisting TJ [13].
  • The coincidence of the sequence necessary for the ZO-1 association with that for the TJ localization suggests that the association with underlying cytoskeletons through ZO-1 is required for occludin to be localized at TJ [13].
  • Furthermore, neither endogenous occludin nor claudin is required for targeting to ZO-1-containing cell-cell contacts, since in normal rat kidney fibroblasts targeting of chimeras again required only the ZO-binding domain [17].

Associations of OCLN with chemical compounds


Physical interactions of OCLN


Enzymatic interactions of OCLN

  • EGF rapidly increased the levels of phosphorylated MEK (p-MEK) in detergent-soluble fractions and phosphorylated ERK (p-ERK) in detergent-insoluble fractions. p-ERK was colocalized and co-immunoprecipitated with occludin [23].
  • S. flexneri serotype 2a and 5, but not the non-invasive Escherichia coli strain F-18, share the ability to regulate expression of ZO-1, ZO-2, E-cadherin and to dephosphorylate occludin [27].
  • CKI epsilon phosphorylated occludin and co-localised and co-immunoprecipitated with occludin from human endothelial cells [26].

Co-localisations of OCLN


Regulatory relationships of OCLN


Other interactions of OCLN

  • We concluded that occludin itself can localize at TJ and directly associate with ZO-1 [13].
  • The cellular changes contributing to the increased permeability and increased na??ve monocyte transendothelial migration include the disruption of actin stress fiber formation and the decreased expression of lateral junction proteins (occludin and vascular endothelial cadherin) [35].
  • In studies of human premature infants, we used immunomicroscopy to determine if amounts of the TJ proteins ZO-1, claudin and occludin increase with gestational age in vessels of germinal matrix (GM) and cortex [36].
  • Immunostaining for occludin, claudins 1 and 5 and VE-cadherin was carried out on fixed tissue [37].
  • Occludin staining was seen at the junctional complex, where it was not continuous, but dotted along the cell junctions.The transcripts for claudin-1 and several other claudin isotypes, such as -2, -3, -4, -7, -9 and -14 were identified [38].

Analytical, diagnostic and therapeutic context of OCLN


  1. Tight junctions and compression therapy in chronic venous insufficiency. Herouy, Y., Kahle, B., Idzko, M., Eberth, I., Norgauer, J., Pannier, F., Rabe, E., Jünger, M., Bruckner-Tuderman, L. Int. J. Mol. Med. (2006) [Pubmed]
  2. Membrane-type 1 matrix metalloproteinase expression is regulated by zonula occludens-1 in human breast cancer cells. Polette, M., Gilles, C., Nawrocki-Raby, B., Lohi, J., Hunziker, W., Foidart, J.M., Birembaut, P. Cancer Res. (2005) [Pubmed]
  3. Expression of ZO-1 and occludin in normal human placenta and in hydatidiform moles. Marzioni, D., Banita, M., Felici, A., Paradinas, F.J., Newlands, E., De Nictolis, M., Mühlhauser, J., Castellucci, M. Mol. Hum. Reprod. (2001) [Pubmed]
  4. Claudins 1, 4, 5, 7 and occludin in ameloblastomas and developing human teeth. Bello, I.O., Soini, Y., Slootweg, P.J., Salo, T. J. Oral Pathol. Med. (2007) [Pubmed]
  5. The cell biology of the blood-brain barrier. Rubin, L.L., Staddon, J.M. Annu. Rev. Neurosci. (1999) [Pubmed]
  6. Occludin and claudins in tight-junction strands: leading or supporting players? Tsukita, S., Furuse, M. Trends Cell Biol. (1999) [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. Der p 1 facilitates transepithelial allergen delivery by disruption of tight junctions. Wan, H., Winton, H.L., Soeller, C., Tovey, E.R., Gruenert, D.C., Thompson, P.J., Stewart, G.A., Taylor, G.W., Garrod, D.R., Cannell, M.B., Robinson, C. J. Clin. Invest. (1999) [Pubmed]
  9. Intraepithelial gammadelta(+) Lymphocytes Maintain the Integrity of Intestinal Epithelial Tight Junctions in Response to Infection. Dalton, J.E., Cruickshank, S.M., Egan, C.E., Mears, R., Newton, D.J., Andrew, E.M., Lawrence, B., Howell, G., Else, K.J., Gubbels, M.J., Striepen, B., Smith, J.E., White, S.J., Carding, S.R. Gastroenterology (2006) [Pubmed]
  10. Occludin is overexpressed in Alzheimer's disease and vascular dementia. Romanitan, M.O., Popescu, B.O., Winblad, B., Bajenaru, O.A., Bogdanovic, N. J. Cell. Mol. Med. (2007) [Pubmed]
  11. Biphasic effects of 17-beta-estradiol on expression of occludin and transendothelial resistance and paracellular permeability in human vascular endothelial cells. Ye, L., Martin, T.A., Parr, C., Harrison, G.M., Mansel, R.E., Jiang, W.G. J. Cell. Physiol. (2003) [Pubmed]
  12. Effects of VEGFR-1, VEGFR-2, and IGF-IR hammerhead ribozymes on glucose-mediated tight junction expression in cultured human retinal endothelial cells. Spoerri, P.E., Afzal, A., Li Calzi, S., Shaw, L.C., Cai, J., Pan, H., Boulton, M., Grant, M.B. Mol. Vis. (2006) [Pubmed]
  13. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. Furuse, M., Itoh, M., Hirase, T., Nagafuchi, A., Yonemura, S., Tsukita, S., Tsukita, S. J. Cell Biol. (1994) [Pubmed]
  14. Occludin confers adhesiveness when expressed in fibroblasts. Van Itallie, C.M., Anderson, J.M. J. Cell. Sci. (1997) [Pubmed]
  15. Structure of the conserved cytoplasmic C-terminal domain of occludin: identification of the ZO-1 binding surface. Li, Y., Fanning, A.S., Anderson, J.M., Lavie, A. J. Mol. Biol. (2005) [Pubmed]
  16. Cellular Networks of Human Thymic Medullary Stromas Coordinated by p53-Related Transcription Factors. Ichimiya, S., Kojima, T. J. Histochem. Cytochem. (2006) [Pubmed]
  17. Connexin-occludin chimeras containing the ZO-binding domain of occludin localize at MDCK tight junctions and NRK cell contacts. Mitic, L.L., Schneeberger, E.E., Fanning, A.S., Anderson, J.M. J. Cell Biol. (1999) [Pubmed]
  18. Interaction between the transforming growth factor-beta type II receptor/Smad pathway and beta-catenin during transforming growth factor-beta1-mediated adherens junction disassembly. Tian, Y.C., Phillips, A.O. Am. J. Pathol. (2002) [Pubmed]
  19. Occludin proteolysis and increased permeability in endothelial cells through tyrosine phosphatase inhibition. Wachtel, M., Frei, K., Ehler, E., Fontana, A., Winterhalter, K., Gloor, S.M. J. Cell. Sci. (1999) [Pubmed]
  20. Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stress. Rao, R.K., Basuroy, S., Rao, V.U., Karnaky Jr, K.J., Gupta, A. Biochem. J. (2002) [Pubmed]
  21. Polyamines are necessary for synthesis and stability of occludin protein in intestinal epithelial cells. Guo, X., Rao, J.N., Liu, L., Zou, T., Keledjian, K.M., Boneva, D., Marasa, B.S., Wang, J.Y. Am. J. Physiol. Gastrointest. Liver Physiol. (2005) [Pubmed]
  22. A protein kinase A-dependent mechanism by which rotavirus affects the distribution and mRNA level of the functional tight junction-associated protein, occludin, in human differentiated intestinal Caco-2 cells. Beau, I., Cotte-Laffitte, J., Amsellem, R., Servin, A.L. J. Virol. (2007) [Pubmed]
  23. MAPK interacts with occludin and mediates EGF-induced prevention of tight junction disruption by hydrogen peroxide. Basuroy, S., Seth, A., Elias, B., Naren, A.P., Rao, R. Biochem. J. (2006) [Pubmed]
  24. Nonreceptor tyrosine kinase c-Yes interacts with occludin during tight junction formation in canine kidney epithelial cells. Chen, Y.H., Lu, Q., Goodenough, D.A., Jeansonne, B. Mol. Biol. Cell (2002) [Pubmed]
  25. JRAB/MICAL-L2 Is a Junctional Rab13-binding Protein Mediating the Endocytic Recycling of Occludin. Terai, T., Nishimura, N., Kanda, I., Yasui, N., Sasaki, T. Mol. Biol. Cell (2006) [Pubmed]
  26. Casein kinase I epsilon associates with and phosphorylates the tight junction protein occludin. McKenzie, J.A., Riento, K., Ridley, A.J. FEBS Lett. (2006) [Pubmed]
  27. Shigella flexneri regulates tight junction-associated proteins in human intestinal epithelial cells. Sakaguchi, T., Köhler, H., Gu, X., McCormick, B.A., Reinecker, H.C. Cell. Microbiol. (2002) [Pubmed]
  28. Rab13 mediates the continuous endocytic recycling of occludin to the cell surface. Morimoto, S., Nishimura, N., Terai, T., Manabe, S., Yamamoto, Y., Shinahara, W., Miyake, H., Tashiro, S., Shimada, M., Sasaki, T. J. Biol. Chem. (2005) [Pubmed]
  29. VAP-33 localizes to both an intracellular vesicle population and with occludin at the tight junction. Lapierre, L.A., Tuma, P.L., Navarre, J., Goldenring, J.R., Anderson, J.M. J. Cell. Sci. (1999) [Pubmed]
  30. Analysis of invasion-metastasis mechanism in pancreatic cancer: involvement of tight junction transmembrane protein occludin and MEK/ERK signal transduction pathway in cancer cell dissociation. Tan, X., Tamori, Y., Egami, H., Ishikawa, S., Kurizaki, T., Takai, E., Hirota, M., Ogawa, M. Oncol. Rep. (2004) [Pubmed]
  31. E-cadherin induces mesenchymal-to-epithelial transition in human ovarian surface epithelium. Auersperg, N., Pan, J., Grove, B.D., Peterson, T., Fisher, J., Maines-Bandiera, S., Somasiri, A., Roskelley, C.D. Proc. Natl. Acad. Sci. U.S.A. (1999) [Pubmed]
  32. Expression of kinase-inactive c-Src delays oxidative stress-induced disassembly and accelerates calcium-mediated reassembly of tight junctions in the Caco-2 cell monolayer. Basuroy, S., Sheth, P., Kuppuswamy, D., Balasubramanian, S., Ray, R.M., Rao, R.K. J. Biol. Chem. (2003) [Pubmed]
  33. Raf 1 represses expression of the tight junction protein occludin via activation of the zinc-finger transcription factor slug. Wang, Z., Wade, P., Mandell, K.J., Akyildiz, A., Parkos, C.A., Mrsny, R.J., Nusrat, A. Oncogene (2007) [Pubmed]
  34. Cellular and molecular mechanisms of heat stress-induced up-regulation of occludin protein expression: regulatory role of heat shock factor-1. Dokladny, K., Ye, D., Kennedy, J.C., Moseley, P.L., Ma, T.Y. Am. J. Pathol. (2008) [Pubmed]
  35. Human Cytomegalovirus (HCMV) Infection of Endothelial Cells Promotes Naive Monocyte Extravasation and Transfer of Productive Virus To Enhance Hematogenous Dissemination of HCMV. Bentz, G.L., Jarquin-Pardo, M., Chan, G., Smith, M.S., Sinzger, C., Yurochko, A.D. J. Virol. (2006) [Pubmed]
  36. Immunolocalization of tight junction proteins in blood vessels in human germinal matrix and cortex. Anstrom, J.A., Thore, C.R., Moody, D.M., Brown, W.R. Histochem. Cell Biol. (2007) [Pubmed]
  37. Cell junctional proteins in the human corpus luteum: changes during the normal cycle and after HCG treatment. Groten, T., Fraser, H.M., Duncan, W.C., Konrad, R., Kreienberg, R., Wulff, C. Hum. Reprod. (2006) [Pubmed]
  38. Tight junction-related protein expression and distribution in human corneal epithelium. Ban, Y., Dota, A., Cooper, L.J., Fullwood, N.J., Nakamura, T., Tsuzuki, M., Mochida, C., Kinoshita, S. Exp. Eye Res. (2003) [Pubmed]
  39. The HIV protease inhibitors saquinavir, ritonavir, and nelfinavir induce apoptosis and decrease barrier function in human intestinal epithelial cells. Bode, H., Lenzner, L., Kraemer, O.H., Kroesen, A.J., Bendfeldt, K., Schulzke, J.D., Fromm, M., Stoltenburg-Didinger, G., Zeitz, M., Ullrich, R. Antivir. Ther. (Lond.) (2005) [Pubmed]
  40. Organization and formation of the tight junction system in human epidermis and cultured keratinocytes. Brandner, J.M., Kief, S., Grund, C., Rendl, M., Houdek, P., Kuhn, C., Tschachler, E., Franke, W.W., Moll, I. Eur. J. Cell Biol. (2002) [Pubmed]
  41. Crystallization and preliminary X-ray diffraction of the ZO-binding domain of human occludin. Peng, B.H., White, M.A., Campbell, G.A., Robert, J.J., Lee, J.C., Sutton, R.B. Acta Crystallograph. Sect. F Struct. Biol. Cryst. Commun. (2005) [Pubmed]
  42. Constitutive activation of Rho proteins by CNF-1 influences tight junction structure and epithelial barrier function. Hopkins, A.M., Walsh, S.V., Verkade, P., Boquet, P., Nusrat, A. J. Cell. Sci. (2003) [Pubmed]
WikiGenes - Universities