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Volumn 91, Issue 9, 2011, Pages 1396-1409

Epidermal growth factor protects the apical junctional complexes from hydrogen peroxide in bile duct epithelium

Author keywords

adherens junctions; cholangiocyte; EGF; oxidative stress; protein kinase; tight junction

Indexed keywords

1 (5 IODO 1 NAPHTHALENESULFONYL)HEXAHYDRO 1H 1,4 DIAZEPINE; 3 [8 [(DIMETHYLAMINO)METHYL] 6,7,8,9 TETRAHYDROPYRIDO[1,2 A]INDOL 10 YL] 4 (1 METHYL 1H INDOL 3 YL) 1H PYRROLE 2,5 DIONE; 4 AMINO 7 TERT BUTYL 5 (4 CHLOROPHENYL)PYRAZOLO[3,4 D]PYRIMIDINE; ACTIN; BETA CATENIN; CLAUDIN 3; EPIDERMAL GROWTH FACTOR; HYDROGEN PEROXIDE; INULIN; MYOSIN LIGHT CHAIN; PROTEIN KINASE C INHIBITOR; SCAFFOLD PROTEIN; TYROSINE; UNCLASSIFIED DRUG; UVOMORULIN; ZONA OCCLUDEN 1;

EID: 80052279411     PISSN: 00236837     EISSN: 15300307     Source Type: Journal    
DOI: 10.1038/labinvest.2011.73     Document Type: Article
Times cited : (27)

References (43)
  • 4
    • 77954008878 scopus 로고    scopus 로고
    • Bile duct paucity is part of the neonatal ichthyosis-sclerosing cholangitis phenotype
    • Nagtzaam IF, van Geel M, Driessen A, et al. Bile duct paucity is part of the neonatal ichthyosis-sclerosing cholangitis phenotype. Br J Dermatol 2010;163:205-207.
    • (2010) Br J Dermatol , vol.163 , pp. 205-207
    • Nagtzaam, I.F.1    Van Geel, M.2    Driessen, A.3
  • 7
    • 52049083402 scopus 로고    scopus 로고
    • Oxidative stress-induced disruption of epithelial and endothelial tight junctions
    • Rao R. Oxidative stress-induced disruption of epithelial and endothelial tight junctions. Front Biosci 2008;13:7210-7226.
    • (2008) Front Biosci , vol.13 , pp. 7210-7226
    • Rao, R.1
  • 8
    • 67249146480 scopus 로고    scopus 로고
    • Occludin phosphorylation in regulation of epithelial tight junctions
    • Rao R. Occludin phosphorylation in regulation of epithelial tight junctions. Ann N Y Acad Sci 2009;1165:62-68.
    • (2009) Ann N y Acad Sci , vol.1165 , pp. 62-68
    • Rao, R.1
  • 9
    • 0027220666 scopus 로고
    • Immunofluorescence and immunoelectron microscopy analyses of a human monoclonal anti-epithelial cell surface antibody that recognizes a 185-kD polypeptide: A component of the paraneoplastic pemphigus antigen complex?
    • Joly P, Gilbert D, Thomine E, et al. Immunofluorescence and immunoelectron microscopy analyses of a human monoclonal antiepithelial cell surface antibody that recognizes a 185-kD polypeptide: a component of the paraneoplastic pemphigus antigen complex? J Invest Dermatol 1993;101:339-345. (Pubitemid 23269908)
    • (1993) Journal of Investigative Dermatology , vol.101 , Issue.3 , pp. 339-345
    • Joly, P.1    Gilbert, D.2    Thomine, E.3    Delpech, A.4    Verdier, S.5    Lauret, P.6    Tron, F.7
  • 10
  • 11
    • 0034822702 scopus 로고    scopus 로고
    • Identification of novel molecules and pathogenic pathways in primary biliary cirrhosis: cDNA array analysis of intrahepatic differential gene expression
    • DOI 10.1136/gut.49.4.565
    • Shackel NA, McGuinness PH, Abbott CA, et al. Identification of novel molecules and pathogenic pathways in primary biliary cirrhosis: cDNA array analysis of intrahepatic differential gene expression. Gut 2001;49:565-576. (Pubitemid 32896989)
    • (2001) Gut , vol.49 , Issue.4 , pp. 565-576
    • Shackel, N.A.1    McGuinness, P.H.2    Abbott, C.A.3    Gorrell, M.D.4    McCaughan, G.W.5
  • 12
    • 14844297409 scopus 로고    scopus 로고
    • Study of antioxidant enzymes level and phagocytic activity in chronic liver disease patients
    • Salem TA, El-Refaei MF, Badra GA. Study of antioxidant enzymes level and phagocytic activity in chronic liver disease patients. Egypt J Immunol 2003;10:37-45.
    • (2003) Egypt J Immunol , vol.10 , pp. 37-45
    • Salem, T.A.1    El-Refaei, M.F.2    Badra, G.A.3
  • 13
    • 77957943397 scopus 로고    scopus 로고
    • Serum oxidative stress is increased in patients with post cholecystectomy bile duct injury
    • Miranda-Diaz AG, Hermosillo-Sandoval JM, Ortiz GG, et al. Serum oxidative stress is increased in patients with post cholecystectomy bile duct injury. Rev Esp Enferm Dig 2010;102:352-356.
    • (2010) Rev Esp Enferm Dig , vol.102 , pp. 352-356
    • Miranda-Diaz, A.G.1    Hermosillo-Sandoval, J.M.2    Ortiz, G.G.3
  • 14
    • 67651236487 scopus 로고    scopus 로고
    • Surgically-induced bile duct injury is followed by early hepatic oxidative stress. A preliminary experimental study in rats
    • Lissidini G, Piccinni G, Portincasa P, et al. Surgically-induced bile duct injury is followed by early hepatic oxidative stress. A preliminary experimental study in rats. Hepatogastroenterology 2009;56: 602-605.
    • (2009) Hepatogastroenterology , vol.56 , pp. 602-605
    • Lissidini, G.1    Piccinni, G.2    Portincasa, P.3
  • 15
    • 70349191559 scopus 로고    scopus 로고
    • The role of mitochondria in cholestatic liver injury
    • Tiao MM, Lin TK, Wang PW, et al. The role of mitochondria in cholestatic liver injury. Chang Gung Med J 2009;32:346-353.
    • (2009) Chang Gung Med J , vol.32 , pp. 346-353
    • Tiao, M.M.1    Lin, T.K.2    Wang, P.W.3
  • 17
    • 0036190844 scopus 로고    scopus 로고
    • Viral gene delivery of superoxide dismutase attenuates experimental cholestasis-induced liver fibrosis in the rat
    • DOI 10.1038/sj/gt/3301638
    • Zhong Z, Froh M, Wheeler MD, et al. Viral gene delivery of superoxide dismutase attenuates experimental cholestasis-induced liver fibrosis in the rat. Gene Ther 2002;9:183-191. (Pubitemid 34189578)
    • (2002) Gene Therapy , vol.9 , Issue.3 , pp. 183-191
    • Zhong, Z.1    Froh, M.2    Wheeler, M.D.3    Smutney, O.4    Lehmann, T.G.5    Thurman, R.G.6
  • 18
    • 0035170217 scopus 로고    scopus 로고
    • Nitric oxide-mediated inhibition of DNA repair potentiates oxidative DNA damage in cholangiocytes
    • Jaiswal M, LaRusso NF, Shapiro RA, et al. Nitric oxide-mediated inhibition of DNA repair potentiates oxidative DNA damage in cholangiocytes. Gastroenterology 2001;120:190-199. (Pubitemid 32061883)
    • (2001) Gastroenterology , vol.120 , Issue.1 , pp. 190-199
    • Jaiswal, M.1    LaRusso, N.F.2    Shapiro, R.A.3    Billiar, T.R.4    Gores, G.J.5
  • 21
    • 0023949917 scopus 로고
    • Functional coupling of tight junctions and microfilaments in T84 monolayers
    • Madara JL, Stafford J, Barenberg D, et al. Functional coupling of tight junctions and microfilaments in T84 monolayers. Am J Physiol 1988;254(3 Part 1):G416-G423.
    • (1988) Am J Physiol , vol.254 , Issue.3 PART 1
    • Madara, J.L.1    Stafford, J.2    Barenberg, D.3
  • 22
    • 0019258703 scopus 로고
    • Occluding junctions and cytoskeletal components in a cultured transporting epithelium
    • DOI 10.1083/jcb.87.3.746
    • Meza I, Ibarra G, Sabanero M, et al. Occluding junctions and cytoskeletal components in a cultured transporting epithelium. J Cell Biol 1980;87(3 Part 1):746-754. (Pubitemid 11161806)
    • (1980) Journal of Cell Biology , vol.87 , Issue.3 , pp. 746-754
    • Meza, I.1    Ibarra, G.2    Sabanero, M.3
  • 23
    • 0028289263 scopus 로고
    • Concentration-dependent effects of cytochalasin D on tight junctions and actin filaments in MDCK epithelial cells
    • Stevenson BR, Begg DA. Concentration-dependent effects of cytochalasin D on tight junctions and actin filaments in MDCK epithelial cells. J Cell Sci 1994;107(Part 3):367-375. (Pubitemid 24091844)
    • (1994) Journal of Cell Science , vol.107 , Issue.3 , pp. 367-375
    • Stevenson, B.R.1    Begg, D.A.2
  • 24
    • 0025859096 scopus 로고
    • Biologically active peptides in the gastrointestinal lumen
    • Rao RK. Biologically active peptides in the gastrointestinal lumen. Life Sci 1991;48:1685-1704.
    • (1991) Life Sci , vol.48 , pp. 1685-1704
    • Rao, R.K.1
  • 25
    • 59449086585 scopus 로고    scopus 로고
    • Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctions
    • Elias BC, Suzuki T, Seth A, et al. Phosphorylation of Tyr-398 and Tyr-402 in occludin prevents its interaction with ZO-1 and destabilizes its assembly at the tight junctions. J Biol Chem 2009;284:1559-1569.
    • (2009) J Biol Chem , vol.284 , pp. 1559-1569
    • Elias, B.C.1    Suzuki, T.2    Seth, A.3
  • 27
    • 41249094587 scopus 로고    scopus 로고
    • Role of phospholipase Cgamma-induced activation of protein kinase Cepsilon (PKCepsilon) and PKCbetaI in epidermal growth factor-mediated protection of tight junctions from acetaldehyde in Caco-2 cell monolayers
    • Suzuki T, Seth A, Rao R. Role of phospholipase Cgamma-induced activation of protein kinase Cepsilon (PKCepsilon) and PKCbetaI in epidermal growth factor-mediated protection of tight junctions from acetaldehyde in Caco-2 cell monolayers. J Biol Chem 2008;283: 3574-3583.
    • (2008) J Biol Chem , vol.283 , pp. 3574-3583
    • Suzuki, T.1    Seth, A.2    Rao, R.3
  • 28
    • 55249116749 scopus 로고    scopus 로고
    • Plasma superoxide radical in jaundiced patients and role of xanthine oxidase
    • Assimakopoulos SF, Grintzalis K, Thomopoulos KC, et al. Plasma superoxide radical in jaundiced patients and role of xanthine oxidase. Am J Med Sci 2008;336:230-236.
    • (2008) Am J Med Sci , vol.336 , pp. 230-236
    • Assimakopoulos, S.F.1    Grintzalis, K.2    Thomopoulos, K.C.3
  • 29
    • 33750063973 scopus 로고    scopus 로고
    • Molecular mechanisms of cholangiopathy in primary biliary cirrhosis
    • DOI 10.1007/s00795-006-0321-z
    • Harada K, Nakanuma Y. Molecular mechanisms of cholangiopathy in primary biliary cirrhosis. Med Mol Morphol 2006;39:55-61. (Pubitemid 44576783)
    • (2006) Medical Molecular Morphology , vol.39 , Issue.2 , pp. 55-61
    • Harada, K.1    Nakanuma, Y.2
  • 30
    • 0028110309 scopus 로고
    • Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions
    • DOI 10.1083/jcb.127.6.1617
    • Furuse M, Itoh M, Hirase T, et al. Direct association of occludin with ZO-1 and its possible involvement in the localization of occludin at tight junctions. J Cell Biol 1994;127(6 Part 1):1617-1626. (Pubitemid 24380900)
    • (1994) Journal of Cell Biology , vol.127 , Issue.6 , pp. 1617-1626
    • Furuse, M.1    Itoh, M.2    Hirase, T.3    Nagaftichi, A.4    Yonemura, S.5    Tsukita, S.6    Tsukita, S.7
  • 31
    • 72149110115 scopus 로고    scopus 로고
    • Effects of hydrogen peroxide and apolipoprotein e isoforms on apolipoprotein e trafficking in HepG2 cells
    • Sabaretnam T, Harris MJ, Kockx M, et al. Effects of hydrogen peroxide and apolipoprotein E isoforms on apolipoprotein E trafficking in HepG2 cells. Clin Exp Pharmacol Physiol 2009;36:e96-e102.
    • (2009) Clin Exp Pharmacol Physiol , vol.36
    • Sabaretnam, T.1    Harris, M.J.2    Kockx, M.3
  • 32
    • 64849115316 scopus 로고    scopus 로고
    • Hydrogen peroxide mobilizes Ca2+ through two distinct mechanisms in rat hepatocytes
    • Sato H, Takeo T, Liu Q, et al. Hydrogen peroxide mobilizes Ca2+ through two distinct mechanisms in rat hepatocytes. Acta Pharmacol Sin 2009;30:78-89.
    • (2009) Acta Pharmacol Sin , vol.30 , pp. 78-89
    • Sato, H.1    Takeo, T.2    Liu, Q.3
  • 33
    • 0021874027 scopus 로고
    • Neutrophils adherent to a nonphagocytosable surface (glomerular basement membrane) produce oxidants only at the site of attachment
    • Vissers MC, Day WA, Winterbourn CC. Neutrophils adherent to a nonphagocytosable surface (glomerular basement membrane) produce oxidants only at the site of attachment. Blood 1985;66: 161-166. (Pubitemid 15004799)
    • (1985) Blood , vol.66 , Issue.1 , pp. 161-166
    • Vissers, M.C.M.1    Day, W.A.2    Winterbourn, C.C.3
  • 34
    • 0036901407 scopus 로고    scopus 로고
    • Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-β-catenin complexes from the cytoskeleton by oxidative stress
    • DOI 10.1042/BJ20011804
    • Rao RK, Basuroy S, Rao VU, et al. Tyrosine phosphorylation and dissociation of occludin-ZO-1 and E-cadherin-beta-catenin complexes from the cytoskeleton by oxidative stress. Biochem J 2002;368 (Part 2):471-481. (Pubitemid 35454525)
    • (2002) Biochemical Journal , vol.368 , Issue.2 , pp. 471-481
    • Rao, R.K.1    Basuroy, S.2    Rao, V.U.3    Karnaky Jr., K.J.4    Gupta, A.5
  • 35
    • 34249668828 scopus 로고    scopus 로고
    • Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer
    • DOI 10.1074/jbc.M610597200
    • Seth A, Sheth P, Elias BC, et al. Protein phosphatases 2A and 1 interact with occludin and negatively regulate the assembly of tight junctions in the CACO-2 cell monolayer. J Biol Chem 2007;282: 11487-11498. (Pubitemid 47100808)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.15 , pp. 11487-11498
    • Seth, A.1    Sheth, P.2    Elias, B.C.3    Rao, R.4
  • 37
    • 0038146915 scopus 로고    scopus 로고
    • 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
    • DOI 10.1074/jbc.M211710200
    • Basuroy S, Sheth P, Kuppuswamy D, et al. 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. J Biol Chem 2003;278:11916-11924. (Pubitemid 36800164)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.14 , pp. 11916-11924
    • Basuroy, S.1    Sheth, P.2    Kuppuswamy, D.3    Balasubramanian, S.4    Ray, R.M.5    Rao, R.K.6
  • 39
    • 0036697252 scopus 로고    scopus 로고
    • Emerging roles of the actin cytoskeleton in cholangiocyte function and disease
    • Doctor RB, Fouassier L. Emerging roles of the actin cytoskeleton in cholangiocyte function and disease. Semin Liver Dis 2002;22:263-276.
    • (2002) Semin Liver Dis , vol.22 , pp. 263-276
    • Doctor, R.B.1    Fouassier, L.2
  • 40
    • 61649106928 scopus 로고    scopus 로고
    • Inflammation and liver cancer: New molecular links
    • Berasain C, Castillo J, Perugorria MJ, et al. Inflammation and liver cancer: new molecular links. Ann N Y Acad Sci 2009;1155:206-221.
    • (2009) Ann N y Acad Sci , vol.1155 , pp. 206-221
    • Berasain, C.1    Castillo, J.2    Perugorria, M.J.3
  • 41
    • 44649116436 scopus 로고    scopus 로고
    • Growth factors as therapeutic targets in HCC
    • Furuse J. Growth factors as therapeutic targets in HCC. Crit Rev Oncol Hematol 2008;67:8-15.
    • (2008) Crit Rev Oncol Hematol , vol.67 , pp. 8-15
    • Furuse, J.1
  • 42
    • 0025122144 scopus 로고
    • Liver regeneration: Molecular mechanisms of growth control
    • Michalopoulos GK. Liver regeneration: molecular mechanisms of growth control. FASEB J 1990;4:176-187.
    • (1990) FASEB J , vol.4 , pp. 176-187
    • Michalopoulos, G.K.1
  • 43
    • 0024543241 scopus 로고
    • Biological effects of epidermal growth factor, with emphasis on the gastrointestinal tract and liver: An update
    • DOI 10.1002/hep.1840090122
    • Marti U, Burwen SJ, Jones AL. Biological effects of epidermal growth factor, with emphasis on the gastrointestinal tract and liver: an update. Hepatology 1989;9:126-138. (Pubitemid 19046315)
    • (1989) Hepatology , vol.9 , Issue.1 , pp. 126-138
    • Marti, U.1    Burwen, S.J.2    Jones, A.L.3


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