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Gene Review

Tjp1  -  tight junction protein 1

Rattus norvegicus

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Disease relevance of Tjp1_predicted


High impact information on Tjp1_predicted


Biological context of Tjp1_predicted


Anatomical context of Tjp1_predicted

  • Connexin-43 (Cx43), the most ubiquitously expressed vertebrate gap junction protein, has been shown to interact directly with Zonula Occludens-1 (ZO-1) [11].
  • Immunoreactivity for ZO-1 was strong at proximal and distal junctional complexes of differentiating ameloblasts, while it was weak and punctuate at the distal region of differentiating odontoblasts [7].
  • Thus, our results showed that ZO-1, occludin, and claudin-1 are differentially expressed as TJs assemble for regulating polarity and/or paracellular permeability in differentiating ameloblasts and odontoblasts [7].
  • On the other hand, the intensity of ZO-1 staining in hepatocytes increased and did not change in BECs compared with that of control rats [12].
  • In control rats, immunostaining for 7H6 and ZO-1 colocalized to the apical site of BECs and was continuous along the bile canaliculi [12].

Associations of Tjp1_predicted with chemical compounds

  • Indeed, SB202190, a specific p38 MAP kinase inhibitor, blocked the CdCl(2)-induced occludin and ZO-1 loss from the BTB [13].
  • The subcellular localization of PMP22 in cultured brain endothelia was confirmed by internalization with ZO-1 after EGTA-induced disruption of cell junctions [14].
  • Diffuse cytoplasmic staining of alpha-catenin, beta-catenin, ZO-1, and Cx43 was seen in the cytoplasm when cardiomyocytes were cultured in low Ca(2+) medium [15].
  • Immunolocalization of tight junction proteins, occludin and ZO-1, and glucose transporter GLUT1 in the cells of the blood-nerve barrier [16].
  • To test this hypothesis, Western and Northern blot analysis were carried out to measure the steady-state level of occludin and zonula occludens-one (ZO-1) proteins and mRNA levels in cerebral tissue of streptozotocin-induced diabetic rats and the results were compared to insulin treated diabetic rats and vehicle injected control rats [17].

Physical interactions of Tjp1_predicted

  • Immunoblot analysis of associated proteins showed that the C-terminal domain of connexin-43 binds to the N-terminal domain of ZO-1 [5].

Other interactions of Tjp1_predicted

  • Moreover, binding of c-Src to Cx43CT prevented and reversed ZO-1/Cx43CT binding [18].
  • Immunoprecipitation of Triton X-100 cardiomyocyte extracts using anti-beta-catenin antibodies showed that beta-catenin was associated with alpha-catenin, ZO-1, and Cx43 at 2 h after Ca(2+) switch [15].
  • Presumably, some of these proteins (e.g., occludin, claudin-5 and ZO-1) could be considered sensitive indicators of normal and also of disturbed functional state of the BBB [19].

Analytical, diagnostic and therapeutic context of Tjp1_predicted


  1. Hepatic immunohistochemical localization of the tight junction protein ZO-1 in rat models of cholestasis. Anderson, J.M., Glade, J.L., Stevenson, B.R., Boyer, J.L., Mooseker, M.S. Am. J. Pathol. (1989) [Pubmed]
  2. Impact of cyclosporin on podocyte ZO-1 expression in puromycin aminonucleoside nephrosis rats. Kim, B.S., Park, H.C., Kang, S.W., Choi, K.H., Ha, S.K., Han, D.S., Lee, H.Y. Yonsei Med. J. (2005) [Pubmed]
  3. Histamine, ZO-1 and increased blood-retinal barrier permeability in diabetic retinopathy. Gardner, T.W. Transactions of the American Ophthalmological Society. (1995) [Pubmed]
  4. Connexin 43 interacts with zona occludens-1 and -2 proteins in a cell cycle stage-specific manner. Singh, D., Solan, J.L., Taffet, S.M., Javier, R., Lampe, P.D. J. Biol. Chem. (2005) [Pubmed]
  5. Direct association of the gap junction protein connexin-43 with ZO-1 in cardiac myocytes. Toyofuku, T., Yabuki, M., Otsu, K., Kuzuya, T., Hori, M., Tada, M. J. Biol. Chem. (1998) [Pubmed]
  6. The gap junction protein connexin43 interacts with the second PDZ domain of the zona occludens-1 protein. Giepmans, B.N., Moolenaar, W.H. Curr. Biol. (1998) [Pubmed]
  7. Tight junctions in differentiating ameloblasts and odontoblasts differentially express ZO-1, occludin, and claudin-1 in early odontogenesis of rat molars. João, S.M., Arana-Chavez, V.E. The anatomical record. Part A, Discoveries in molecular, cellular, and evolutionary biology. (2004) [Pubmed]
  8. Prolonged positive modulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazolepropionic acid (AMPA) receptors induces calpain-mediated PSD-95/Dlg/ZO-1 protein degradation and AMPA receptor down-regulation in cultured hippocampal slices. Jourdi, H., Lu, X., Yanagihara, T., Lauterborn, J.C., Bi, X., Gall, C.M., Baudry, M. J. Pharmacol. Exp. Ther. (2005) [Pubmed]
  9. Correlation of zonula occludens ZO-1 antigen expression and transendothelial resistance in porcine and rat cultured cerebral endothelial cells. Krause, D., Mischeck, U., Galla, H.J., Dermietzel, R. Neurosci. Lett. (1991) [Pubmed]
  10. Electromagnetic fields (1.8 GHz) increase the permeability to sucrose of the blood-brain barrier in vitro. Schirmacher, A., Winters, S., Fischer, S., Goeke, J., Galla, H.J., Kullnick, U., Ringelstein, E.B., Stögbauer, F. Bioelectromagnetics. (2000) [Pubmed]
  11. Identification of connexin-43 interacting proteins. Singh, D., Lampe, P.D. Cell Commun. Adhes. (2003) [Pubmed]
  12. Cholestasis in a rat model of graft-versus-host disease is accompanied by alteration of the expression and distribution of tight-junction-associated proteins. Sasatomi, K., Sakisaka, S., Kawaguchi, T., Hanada, S., Taniguchi, E., Koga, H., Harada, M., Sata, M. Int. J. Mol. Med. (2005) [Pubmed]
  13. Regulation of blood-testis barrier dynamics: an in vivo study. Wong, C.H., Mruk, D.D., Lui, W.Y., Cheng, C.Y. J. Cell. Sci. (2004) [Pubmed]
  14. The temporospatial expression of peripheral myelin protein 22 at the developing blood-nerve and blood-brain barriers. Roux, K.J., Amici, S.A., Notterpek, L. J. Comp. Neurol. (2004) [Pubmed]
  15. Role of catenins in the development of gap junctions in rat cardiomyocytes. Wu, J.C., Tsai, R.Y., Chung, T.H. J. Cell. Biochem. (2003) [Pubmed]
  16. Immunolocalization of tight junction proteins, occludin and ZO-1, and glucose transporter GLUT1 in the cells of the blood-nerve barrier. Tserentsoodol, N., Shin, B.C., Koyama, H., Suzuki, T., Takata, K. Arch. Histol. Cytol. (1999) [Pubmed]
  17. Diabetes-related changes in rat cerebral occludin and zonula occludens-1 (ZO-1) expression. Chehade, J.M., Haas, M.J., Mooradian, A.D. Neurochem. Res. (2002) [Pubmed]
  18. Regulation of connexin43 protein complexes by intracellular acidification. Duffy, H.S., Ashton, A.W., O'Donnell, P., Coombs, W., Taffet, S.M., Delmar, M., Spray, D.C. Circ. Res. (2004) [Pubmed]
  19. Immunogold localization of tight junctional proteins in normal and osmotically-affected rat blood-brain barrier. Dobrogowska, D.H., Vorbrodt, A.W. J. Mol. Histol. (2004) [Pubmed]
  20. Age-related changes in rat cerebral occludin and zonula occludens-1 (ZO-1). Mooradian, A.D., Haas, M.J., Chehade, J.M. Mech. Ageing Dev. (2003) [Pubmed]
  21. Effect of stress on the paracellular barrier in the rat ileum. Mazzon, E., Sturniolo, G.C., Puzzolo, D., Frisina, N., Fries, W. Gut (2002) [Pubmed]
  22. Altered hepatic localization and expression of occludin after common bile duct ligation. Fallon, M.B., Brecher, A.R., Balda, M.S., Matter, K., Anderson, J.M. Am. J. Physiol. (1995) [Pubmed]
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