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Volumn 289, Issue 2 52-2, 2005, Pages

Acetaldehyde disrupts tight junctions and adherens junctions in human colonic mucosa: Protection by EGF and L-glutamine

Author keywords

Alcohol; Barrier function; Epidermal growth factor; Human colon

Indexed keywords

ACETALDEHYDE; ALCOHOL; BETA CATENIN; DETERGENT; EPIDERMAL GROWTH FACTOR; GAP JUNCTION PROTEIN; GLUTAMINE; OCCLUDIN; PROTEIN TYROSINE PHOSPHATASE; UNCLASSIFIED DRUG; UVOMORULIN; ZONULA OCCLUDENS 1;

EID: 22544451542     PISSN: 01931857     EISSN: None     Source Type: Journal    
DOI: 10.1152/ajpgi.00464.2004     Document Type: Article
Times cited : (119)

References (30)
  • 1
    • 0028799226 scopus 로고
    • Tight junctions and the molecular basis for regulation of paracelular permeability
    • Anderson JM and van Italie CM. Tight junctions and the molecular basis for regulation of paracelular permeability. Am J Physiol Gastrointest Liver Physiol 269: G467-G475, 1995.
    • (1995) Am J Physiol Gastrointest Liver Physiol , vol.269
    • Anderson, J.M.1    Van Italie, C.M.2
  • 2
    • 0034967963 scopus 로고    scopus 로고
    • Role of tyrosine phosphorylation in acetaldehyde mediated disruption of tight junctions
    • Atkinson KA and Rao RK. Role of tyrosine phosphorylation in acetaldehyde mediated disruption of tight junctions. Am J Physiol Gastrointest Liver Physiol 280: G1280-G1288, 2001.
    • (2001) Am J Physiol Gastrointest Liver Physiol , vol.280
    • Atkinson, K.A.1    Rao, R.K.2
  • 3
    • 0029782711 scopus 로고    scopus 로고
    • Regulated binding of a PTP1B-like phosphatase to N-cadherin: Control of cadherin-mediated adhesion by dephosphorylation of β-catenin
    • Balsamo J, Leung Ernst H T, Zanin MKB, Hoffman S, and Lilien J. Regulated binding of a PTP1B-like phosphatase to N-cadherin: control of cadherin-mediated adhesion by dephosphorylation of β-catenin. J Cell Biol 134: 801-813, 1996.
    • (1996) J Cell Biol , vol.134 , pp. 801-813
    • Balsamo, J.1    Leung Ernst, H.T.2    Zanin, M.K.B.3    Hoffman, S.4    Lilien, J.5
  • 4
    • 0025321157 scopus 로고
    • Epidermal growth factor
    • Carpenter G and Cohen S. Epidermal growth factor. J Biol Chem 265: 7709-7712, 1990.
    • (1990) J Biol Chem , vol.265 , pp. 7709-7712
    • Carpenter, G.1    Cohen, S.2
  • 5
    • 0030047838 scopus 로고    scopus 로고
    • Cytoskeleton-membrane interaction
    • Cowin P and Burke D. Cytoskeleton-membrane interaction. Curr Opin Cell Biol 8: 56-65, 1996.
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 56-65
    • Cowin, P.1    Burke, D.2
  • 7
    • 0028572556 scopus 로고
    • E-cadherin and APC compete for the interaction with β-catenin and the cytoskeleton
    • Hulsken J, Birchmeier W, and Beherens J. E-cadherin and APC compete for the interaction with β-catenin and the cytoskeleton. J Cell Biol 127: 2061-2091, 1994.
    • (1994) J Cell Biol , vol.127 , pp. 2061-2091
    • Hulsken, J.1    Birchmeier, W.2    Beherens, J.3
  • 8
    • 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. 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.
    • (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
  • 9
    • 0037428288 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of C-terminal tail of occludin prevents its interaction with ZO-1, ZO-2, ZO-3. B
    • Kale G, Naren AP, Sheth P, and Rao RK. Tyrosine phosphorylation of C-terminal tail of occludin prevents its interaction with ZO-1, ZO-2, ZO-3. Biochem Biophys Res Commun 302: 324-329, 2003.
    • (2003) Iochem Biophys Res Commun , vol.302 , pp. 324-329
    • Kale, G.1    Naren, A.P.2    Sheth, P.3    Rao, R.K.4
  • 10
    • 0029925516 scopus 로고    scopus 로고
    • Aldehyde dehydrogenases of the rat colon: Comparison with other tissues of the alimentary tract and the liver
    • Koivisto T and Salaspuro M. Aldehyde dehydrogenases of the rat colon: comparison with other tissues of the alimentary tract and the liver. Alcohol Clin Exp Res 20: 551-555, 1996.
    • (1996) Alcohol Clin Exp Res , vol.20 , pp. 551-555
    • Koivisto, T.1    Salaspuro, M.2
  • 11
    • 0031446151 scopus 로고    scopus 로고
    • Effects of acetaldehyde on brush border enzyme activities in human colon adenocarcinoma cell line Caco-2
    • Koivisto T and Salaspuro M. Effects of acetaldehyde on brush border enzyme activities in human colon adenocarcinoma cell line Caco-2. Alcohol Clin Exp Res 21: 1599-1605, 1997.
    • (1997) Alcohol Clin Exp Res , vol.21 , pp. 1599-1605
    • Koivisto, T.1    Salaspuro, M.2
  • 12
    • 0029089328 scopus 로고
    • Cytoskeletal regulation of Caco-2 intestinal monolayer paracellular permeability
    • Ma TY, Hollander D, Tran LT, Nguyen D, Hoa N, and Bhalla D. Cytoskeletal regulation of Caco-2 intestinal monolayer paracellular permeability. J Cell Physiol 164: 533-545, 1995.
    • (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
  • 13
    • 0025376471 scopus 로고
    • Identification of an additional member of the protein-tyrosine- phosphatase family: Evidence for alternative splicing in the tyrosine phosphatase domain
    • Matthews RJ, Cahir ED, Thomas ML. Identification of an additional member of the protein-tyrosine-phosphatase family: evidence for alternative splicing in the tyrosine phosphatase domain. Proc Natl Acad Sci USA 87: 4444-4448, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 4444-4448
    • Matthews, R.J.1    Cahir, E.D.2    Thomas, M.L.3
  • 14
    • 0024755646 scopus 로고
    • Transmembrane control of cadherin-mediated cytoplasmic domain of E-cadherin
    • Nagafuchi A and Takeichi M. Transmembrane control of cadherin-mediated cytoplasmic domain of E-cadherin. Cell Regul 1: 37-44, 1989.
    • (1989) Cell Regul , vol.1 , pp. 37-44
    • Nagafuchi, A.1    Takeichi, M.2
  • 16
    • 0025859096 scopus 로고
    • Biologically active peptides in the gastrointestinal lumen
    • Rao RK. Biologically active peptides in the gastrointestinal lumen. Life Sci 48: 1685-1704, 1991.
    • (1991) Life Sci , vol.48 , pp. 1685-1704
    • Rao, R.K.1
  • 17
    • 0031761303 scopus 로고    scopus 로고
    • Acetaldehyde-induced increase in paracellular permeability in Caco-2 cell monolayer
    • Rao RK. Acetaldehyde-induced increase in paracellular permeability in Caco-2 cell monolayer. Alcohol Clin Exp Res 22: 1724-1730, 1998.
    • (1998) Alcohol Clin Exp Res , vol.22 , pp. 1724-1730
    • Rao, R.K.1
  • 18
    • 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
    • Rao RK, Rao VU, Karnaky KJ, and Gupta A. Tyrosine phosphorylation and dissociation of occludin/ZO-1 and E-cadherin/β-catenin complexes from the cytoskeleton by oxidative stress. Biochem J 368: 471-481, 2002.
    • (2002) Biochem J , vol.368 , pp. 471-481
    • Rao, R.K.1    Rao, V.U.2    Karnaky, K.J.3    Gupta, A.4
  • 19
    • 0033559765 scopus 로고    scopus 로고
    • Epidermal growth factor delays oxidant-induced disruption of the intestinal epithelial barrier function
    • Rao RK, Baker RD, and Baker SS. Epidermal growth factor delays oxidant-induced disruption of the intestinal epithelial barrier function. Biochem Pharmacol 57: 685-697, 1999.
    • (1999) Biochem Pharmacol , vol.57 , pp. 685-697
    • Rao, R.K.1    Baker, R.D.2    Baker, S.S.3
  • 21
    • 0034853126 scopus 로고    scopus 로고
    • Glutamine and the bowel
    • Reeds PJ and Burrin DG. Glutamine and the bowel. J Nutr 131: 2505S-2508S, 2001.
    • (2001) J Nutr , vol.131
    • Reeds, P.J.1    Burrin, D.G.2
  • 22
    • 0029898316 scopus 로고    scopus 로고
    • Bacteriocolonic pathway for ethanol oxidation: Characteristics and implications
    • Salaspuro M. Bacteriocolonic pathway for ethanol oxidation: characteristics and implications. Ann Med 28: 195-200, 1996.
    • (1996) Ann Med , vol.28 , pp. 195-200
    • Salaspuro, M.1
  • 23
    • 0037623310 scopus 로고    scopus 로고
    • Acetaldehyde, microbes, and cancer of the digestive tract
    • Salaspuro M. Acetaldehyde, microbes, and cancer of the digestive tract. Crit Rev Clin Lab Sci 40: 183-208, 2003.
    • (2003) Crit Rev Clin Lab Sci , vol.40 , pp. 183-208
    • Salaspuro, M.1
  • 25
    • 4143100246 scopus 로고    scopus 로고
    • L-Glutamine ameliorates acetaldehyde-induced paracellular permeability in Caco-2 cell monolayer
    • Seth A, Sheth P, Basuroy S, and Rao RK. L-Glutamine ameliorates acetaldehyde-induced paracellular permeability in Caco-2 cell monolayer. Am J Physiol Gastrointest Liver Physiol 287: G510-G517, 2004.
    • (2004) Am J Physiol Gastrointest Liver Physiol , vol.287
    • Seth, A.1    Sheth, P.2    Basuroy, S.3    Rao, R.K.4
  • 26
    • 2442640463 scopus 로고    scopus 로고
    • Epidermal growth factor prevents acetaldehyde-induced disruption of tight junctions in Caco-2 cell monolayer
    • Sheth P, Seth A, Thangavel M, Basuroy S, and Rao RK. Epidermal growth factor prevents acetaldehyde-induced disruption of tight junctions in Caco-2 cell monolayer. Alcohol Clin Exp Res 28: 797-804, 2004.
    • (2004) Alcohol Clin Exp Res , vol.28 , pp. 797-804
    • Sheth, P.1    Seth, A.2    Thangavel, M.3    Basuroy, S.4    Rao, R.K.5
  • 28
    • 0033168966 scopus 로고    scopus 로고
    • Occludin and claudins in tight junction strands: Leading or supporting players?
    • Tsukita S and Furuse M. Occludin and claudins in tight junction strands: leading or supporting players? Trends Cell Biol 9: 268-273, 1999.
    • (1999) Trends Cell Biol , vol.9 , pp. 268-273
    • Tsukita, S.1    Furuse, M.2
  • 29
    • 0036312492 scopus 로고    scopus 로고
    • Microbes and mucosa in the regulation of intracolonic concentration during ethanol challenge
    • Visapaa JP, Tillonen J, and Salaspuro M. Microbes and mucosa in the regulation of intracolonic concentration during ethanol challenge. Alcohol Alcohol 37: 322-326, 2002.
    • (2002) Alcohol Alcohol , vol.37 , pp. 322-326
    • Visapaa, J.P.1    Tillonen, J.2    Salaspuro, M.3
  • 30
    • 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 ES, Haskins J, and Stevenson BR. 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.
    • (1999) J Biol Chem , vol.49 , pp. 35179-35185
    • Wittchen, E.S.1    Haskins, J.2    Stevenson, B.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.