메뉴 건너뛰기




Volumn 368, Issue 2, 2002, Pages 471-481

Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-β-catenin complexes from the cytoskeleton by oxidative stress

Author keywords

Cell cell adhesion; Epithelium; Paracellular permeability; Tight junction; Tyrosine kinase

Indexed keywords

AMINO ACIDS; BIOLOGICAL MEMBRANES; IMMUNOLOGY; OXIDATION; PRECIPITATION (CHEMICAL);

EID: 0036901407     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20011804     Document Type: Article
Times cited : (371)

References (35)
  • 1
    • 0028799226 scopus 로고
    • Tight junctions and the molecular basis for regulation of paracellular permeability
    • Anderson, J. M. and van Italie, C. M. (1995) Tight junctions and the molecular basis for regulation of paracellular permeability. Am. J. Physiol. 269, G467-G475
    • (1995) Am. J. Physiol. , vol.269
    • Anderson, J.M.1    Van Italie, C.M.2
  • 2
    • 0033168966 scopus 로고    scopus 로고
    • Occludin and claudins in tight junction strands: Leading or supporting players?
    • Tsukita, S. and Furuse, M. (1999) Occludin and claudins in tight junction strands: Leading or supporting players? Trends Cell Biol. 9, 268-273
    • (1999) Trends Cell Biol. , vol.9 , pp. 268-273
    • Tsukita, S.1    Furuse, M.2
  • 4
    • 0033552629 scopus 로고    scopus 로고
    • Direct binding of tight junction-associated MAGUKs, ZO-1, ZO-2 and ZO-3, with the COOH termini of claudins
    • Itoh, M., Furuse, M., Morita, K., Kubota, K., Saitou, M. and Tsukita, S. (1999) Direct binding of tight junction-associated MAGUKs, ZO-1, ZO-2 and ZO-3, with the COOH termini of claudins. J. Cell Biol. 147, 1351-1363
    • (1999) J. Cell Biol. , vol.147 , pp. 1351-1363
    • Itoh, M.1    Furuse, M.2    Morita, K.3    Kubota, K.4    Saitou, M.5    Tsukita, S.6
  • 5
    • 0033521140 scopus 로고    scopus 로고
    • Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3
    • Wittchen, E. S., Haskins, J. and Stevenson, B. R. (1999) Protein interactions at the tight junction. Actin has multiple binding partners, and ZO-1 forms independent complexes with ZO-2 and ZO-3. J. Biol. Chem. 49, 35179-35185
    • (1999) J. Biol. Chem. , vol.49 , pp. 35179-35185
    • Wittchen, E.S.1    Haskins, J.2    Stevenson, B.R.3
  • 6
    • 0028110309 scopus 로고
    • Direct association of occludin and ZO-1 and in possible involvement in the localization of occludin at tight junctions
    • Furuse, M., Itoh, M., Hirose, T., Nagafuchi, A., Yonemura, S., Tsukita, S. and Tsukita, S. (1994) Direct association of occludin and ZO-1 and in possible involvement in the localization of occludin at tight junctions. J. Cell Biol. 127, 1617-1626
    • (1994) J. Cell Biol. , vol.127 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirose, T.3    Nagafuchi, A.4    Yonemura, S.5    Tsukita, S.6    Tsukita, S.7
  • 7
    • 0030047838 scopus 로고    scopus 로고
    • Cytoskeleton-membrane interaction
    • Cowin, P. and Burke, D. (1996) Cytoskeleton-membrane interaction. Curr. Opin. Cell Biol. 8, 56-65
    • (1996) Curr. Opin. Cell Biol. , vol.8 , pp. 56-65
    • Cowin, P.1    Burke, D.2
  • 8
    • 0028572556 scopus 로고
    • E-cadherin and APC compete for the interaction with β-catenin and the cytoskeleton
    • Hulsken, J., Birchmeier, W. and Behrens, J. (1994) E-cadherin and APC compete for the interaction with β-catenin and the cytoskeleton. J. Cell Biol. 127, 2061-2091
    • (1994) J. Cell Biol. , vol.127 , pp. 2061-2091
    • Hulsken, J.1    Birchmeier, W.2    Behrens, J.3
  • 9
    • 0024755646 scopus 로고
    • Transmembrane control of cadherin-mediated cell adhesion: A 94 kDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin
    • Nagafuchi, A. and Takeichi, M. (1989) Transmembrane control of cadherin-mediated cell adhesion: A 94 kDa protein functionally associated with a specific region of the cytoplasmic domain of E-cadherin. Cell Reg. 1, 37-44
    • (1989) Cell Reg. , vol.1 , pp. 37-44
    • Nagafuchi, A.1    Takeichi, M.2
  • 10
    • 0035094841 scopus 로고    scopus 로고
    • 2+ regulation of paracellular permeability in the middle intestine of the eel, Anguilla anguilla
    • 2+ regulation of paracellular permeability in the middle intestine of the eel, Anguilla anguilla. J. Comp. Physiol. 171, 85-90
    • (2001) J. Comp. Physiol. , vol.171 , pp. 85-90
    • Trischitta, F.1    Donaro, M.G.2    Faggo, C.3    Lionetto, M.G.4
  • 11
    • 0030962405 scopus 로고    scopus 로고
    • The chloride conductance of tight junctions of rat ileum can be increased by cAMP but not by carbachol
    • Bijlsma, P. B., Bakker, R. and Groot, J. A. (1997) The chloride conductance of tight junctions of rat ileum can be increased by cAMP but not by carbachol. J. Membr. Biol 157, 127-137
    • (1997) J. Membr. Biol. , vol.157 , pp. 127-137
    • Bijlsma, P.B.1    Bakker, R.2    Groot, J.A.3
  • 12
    • 0029862538 scopus 로고    scopus 로고
    • Involvement of a heterotrimeric G protein alpha subunit in tight junction biogenesis
    • Denker, B. M., Saha, C., Khawaja, S. and Nigam, S. K. (1996) Involvement of a heterotrimeric G protein alpha subunit in tight junction biogenesis. J. Biol. Chem. 271, 25750-25753
    • (1996) J. Biol. Chem. , vol.271 , pp. 25750-25753
    • Denker, B.M.1    Saha, C.2    Khawaja, S.3    Nigam, S.K.4
  • 13
    • 0031087537 scopus 로고    scopus 로고
    • Dual role for AIF4(-)-sensitive G proteins in the function of T84 epithelial cells: Transport and barrier effects
    • Ries, J., Stein, J., Traynis-Kaplan, A. E. and Barrett, K. A. (1997) Dual role for AIF4(-)-sensitive G proteins in the function of T84 epithelial cells: Transport and barrier effects. Am. J. Physiol. 272, C794-C803
    • (1997) Am. J. Physiol. , vol.272
    • Ries, J.1    Stein, J.2    Traynis-Kaplan, A.E.3    Barrett, K.A.4
  • 15
    • 0034823910 scopus 로고    scopus 로고
    • Rho kinase regulates tight junction function and is necessary for tight junction assembly in polarized intestinal epithelia
    • Walsh, S. W., Hopkins, A. M., Chen, J., Narumiya, S., Parkos, C. A. and Nusrat, A. (2001) Rho kinase regulates tight junction function and is necessary for tight junction assembly in polarized intestinal epithelia. Gastroenterology 121, 566-579
    • (2001) Gastroenterology , vol.121 , pp. 566-579
    • Walsh, S.W.1    Hopkins, A.M.2    Chen, J.3    Narumiya, S.4    Parkos, C.A.5    Nusrat, A.6
  • 16
    • 0030869798 scopus 로고    scopus 로고
    • Oxidant-induced disruption of intestinal epithelial barrier function: Role of protein tyrosine phosphorylation
    • Rao, R. K., Baker, R. D., Baker, S. S., Gupta, A. and Holycross, M. (1997) Oxidant-induced disruption of intestinal epithelial barrier function: Role of protein tyrosine phosphorylation. Am. J. Physiol. 273, G812-G823
    • (1997) Am. J. Physiol. , vol.273
    • Rao, R.K.1    Baker, R.D.2    Baker, S.S.3    Gupta, A.4    Holycross, M.5
  • 17
    • 0033559765 scopus 로고    scopus 로고
    • Inhibition of oxidant-induced barrier disruption and protein tyrosine phosphorylation in Caco-2 cell monolayers by epidermal growth factor
    • Rao, R. K., Baker, R. D. and Baker, S. S. (1999) Inhibition of oxidant-induced barrier disruption and protein tyrosine phosphorylation in Caco-2 cell monolayers by epidermal growth factor. Biochem. Pharmacol 57, 685-695
    • (1999) Biochem. Pharmacol. , vol.57 , pp. 685-695
    • Rao, R.K.1    Baker, R.D.2    Baker, S.S.3
  • 19
    • 0034967963 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in acetaldehyde mediated disruption of tight junctions
    • Atkinson, K. J. and Rao, R. K. (2001) Role of tyrosine phosphorylation in acetaldehyde mediated disruption of tight junctions. Am. J. Physiol. Gastrointest. Liver Physiol. 280, G1280-G1288
    • (2001) Am. J. Physiol. Gastrointest. Liver Physiol. , vol.280
    • Atkinson, K.J.1    Rao, R.K.2
  • 20
    • 0028931103 scopus 로고
    • Evidence that tyrosine phosphorylation may increase tight junction permeability
    • Staddon, J. M., Herrenknecht, K., Smales, C. and Rubin, L. L. (1995) Evidence that tyrosine phosphorylation may increase tight junction permeability. J. Cell Sci. 108, 609-619
    • (1995) J. Cell Sci. , vol.108 , pp. 609-619
    • Staddon, J.M.1    Herrenknecht, K.2    Smales, C.3    Rubin, L.L.4
  • 22
    • 0029041046 scopus 로고
    • Regulated assembly of tight junctions by protein kinase C
    • Stuart, R. O. and Nigam, S. K. (1995) Regulated assembly of tight junctions by protein kinase C. Proc. Natl. Acad. Sci. U.S.A. 92, 6072-6076
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 6072-6076
    • Stuart, R.O.1    Nigam, S.K.2
  • 23
    • 0033783241 scopus 로고    scopus 로고
    • Protein kinase C activation leads to dephosphorylation of occludin and tight junction permeability increase in LLC-PK1 epithelial cell sheets
    • Clarke, H., Soler, A. P. and Mullin, J. M. (2000) Protein kinase C activation leads to dephosphorylation of occludin and tight junction permeability increase in LLC-PK1 epithelial cell sheets. J. Cell Sci. 113, 3187-3196
    • (2000) J. Cell Sci. , vol.113 , pp. 3187-3196
    • Clarke, H.1    Soler, A.P.2    Mullin, J.M.3
  • 24
    • 0034715892 scopus 로고    scopus 로고
    • The transient increase of tight junction permeability induced by bryostatin 1 correlates with rapid downregulation of protein kinase C-α
    • Clarke, H., Ginanni, N., Laughlin, K. V., Smith, J. B., Pettit, G. R. and Mullin, J. M. (2000) The transient increase of tight junction permeability induced by bryostatin 1 correlates with rapid downregulation of protein kinase C-α. Exp. Cell Res. 261, 239-249
    • (2000) Exp. Cell Res. , vol.261 , pp. 239-249
    • Clarke, H.1    Ginanni, N.2    Laughlin, K.V.3    Smith, J.B.4    Pettit, G.R.5    Mullin, J.M.6
  • 27
    • 0028953668 scopus 로고
    • Increased Tyr phosphorylation of ZO-1 during modification of tight junctions between glomerular foot processes
    • Kurihara, H., Anderson, J. M. and Farquhar, M. G. (1995) Increased Tyr phosphorylation of ZO-1 during modification of tight junctions between glomerular foot processes. Am. J. Physiol. 268, F514-F524
    • (1995) Am. J. Physiol. , vol.268
    • Kurihara, H.1    Anderson, J.M.2    Farquhar, M.G.3
  • 28
    • 0028819708 scopus 로고
    • Effects of tyrosine phosphorylation on tight junctions in temperature-sensitive v-src-transfected MDCK cells
    • Takeda, H. and Tsukita, S. (1995) Effects of tyrosine phosphorylation on tight junctions in temperature-sensitive v-src-transfected MDCK cells. Cell Struct. Funct. 20, 387-393
    • (1995) Cell Struct. Funct. , vol.20 , pp. 387-393
    • Takeda, H.1    Tsukita, S.2
  • 29
    • 0024593744 scopus 로고
    • Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability
    • Hidalgo, I. J., Raub, T. J. and Borchardt, R. T. (1989) Characterization of the human colon carcinoma cell line (Caco-2) as a model system for intestinal epithelial permeability. Gastroenterology 96, 736-749
    • (1989) Gastroenterology , vol.96 , pp. 736-749
    • Hidalgo, I.J.1    Raub, T.J.2    Borchardt, R.T.3
  • 30
    • 0027444694 scopus 로고
    • On the role of the platelet membrane skeleton in mediating signal transduction
    • Fox, J. E. B., Lipfer, L., Clark, E. A., Reynolds, C. C., Austin, C. D. and Brugge, J. S. (1993) On the role of the platelet membrane skeleton in mediating signal transduction. J. Biol. Chem 268, 25973-25984
    • (1993) J. Biol. Chem. , vol.268 , pp. 25973-25984
    • Fox, J.E.B.1    Lipfer, L.2    Clark, E.A.3    Reynolds, C.C.4    Austin, C.D.5    Brugge, J.S.6
  • 31
    • 2242468547 scopus 로고    scopus 로고
    • Protein kinase C activation leads to dephosphorylation of occludin and tight junction permeability increase in LLC-PK1 cells
    • Clarke, H., Soler, A. P. and Mullin, J. M. (2000) Protein kinase C activation leads to dephosphorylation of occludin and tight junction permeability increase in LLC-PK1 cells. J. Cell Sci. 14, 1139-1146
    • (2000) J. Cell Sci. , vol.14 , pp. 1139-1146
    • Clarke, H.1    Soler, A.P.2    Mullin, J.M.3
  • 32
    • 0033579480 scopus 로고    scopus 로고
    • Regulation of E-cadherin/β-catenin association by tyrosine phosphorylation
    • Roura, S., Miravet, S., Piedra, J., Garcia de Herreros, A. and Dunach, M. (1999) Regulation of E-cadherin/β-catenin association by tyrosine phosphorylation. J. Biol. Chem. 274, 36734-36740
    • (1999) J. Biol. Chem. , vol.274 , pp. 36734-36740
    • Roura, S.1    Miravet, S.2    Piedra, J.3    Garcia de Herreros, A.4    Dunach, M.5
  • 33
    • 0026529501 scopus 로고
    • The effect of tyrosine specific protein phosphorylation on the assembly of adherens type junctions
    • Volberg, T., Zick, Y., Dror, R., Sabanay, I., Gilon, C., Levitzki, A. and Geiger, B. (1992) The effect of tyrosine specific protein phosphorylation on the assembly of adherens type junctions. EMBO J. 11, 1733-1742
    • (1992) EMBO J. , vol.11 , pp. 1733-1742
    • Volberg, T.1    Zick, Y.2    Dror, R.3    Sabanay, I.4    Gilon, C.5    Levitzki, A.6    Geiger, B.7
  • 34
    • 0029089328 scopus 로고
    • Cytosketetal regulation of Caco-2 intestinal monolayer paracellular permeability
    • Ma, T. Y., Hollander, D., Tran, L. T., Nguyen, D., Hoa, N. and Bhalla, D. (1995) Cytosketetal regulation of Caco-2 intestinal monolayef paracellular permeability. J. Cell Physiol. 164, 533-545
    • (1995) J. Cell Physiol. , vol.164 , pp. 533-545
    • Ma, T.Y.1    Hollander, D.2    Tran, L.T.3    Nguyen, D.4    Hoa, N.5    Bhalla, D.6
  • 35
    • 0033491912 scopus 로고    scopus 로고
    • Occludin proteolysis and increased permeability in endothelial cells through tyrosine phosphatase inhibition
    • Wachtel, M., Frei, K., Ehler, E., Fontana, A., Winterhalter, K. and Gloor, S. M. (1999) Ocdudin proteolysis and increased permeability in endothelial cells through tyrosine phosphatase inhibition. J. Cell Sci. 112, 4347-4356
    • (1999) J. Cell Sci. , vol.112 , pp. 4347-4356
    • Wachtel, M.1    Frei, K.2    Ehler, E.3    Fontana, A.4    Winterhalter, K.5    Gloor, S.M.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.