메뉴 건너뛰기




Volumn 10, Issue 11, 1999, Pages 2297-2305

ATP depletion increases tyrosine phosphorylation of β-catenin and plakoglobin in renal tubular cells

Author keywords

[No Author keywords available]

Indexed keywords

ADENOSINE TRIPHOSPHATE; BETA CATENIN; GENISTEIN; OCCLUDIN; PLAKOGLOBIN; PROTEIN TYROSINE KINASE INHIBITOR; PROTEIN TYROSINE PHOSPHATASE INHIBITOR; TYROSINE; UVOMORULIN; VANADIC ACID;

EID: 0032711253     PISSN: 10466673     EISSN: None     Source Type: Journal    
DOI: 10.1681/asn.v10112297     Document Type: Article
Times cited : (33)

References (33)
  • 1
    • 0026346859 scopus 로고
    • Effect of reversible atp depletion on tight junction integrity
    • Canfield P, Geerdes A, Molitoris B: Effect of reversible ATP depletion on tight junction integrity. Am J Physiol 261: F1038-F1045, 1991
    • (1991) Am J Physiol , vol.261
    • Canfield, P.1    Geerdes, A.2    Molitoris, B.3
  • 2
    • 0028055171 scopus 로고
    • Functional and cytoskeletal changes induced by sublethal injury in proximal tubular epithelial cells
    • Kroshian VM, Sheridan A, Lieberthal W: Functional and cytoskeletal changes induced by sublethal injury in proximal tubular epithelial cells. Am J Physiol 266: F21-F30, 1994
    • (1994) Am J Physiol , vol.266
    • Kroshian, V.M.1    Sheridan, A.2    Lieberthal, W.3
  • 3
    • 0024439472 scopus 로고
    • Ischemia-induced loss of epithelial polarity: Role of the tight junction
    • Molitoris BA, Dahl RH, Falk SA: Ischemia-induced loss of epithelial polarity: Role of the tight junction. J Clin Invest 84: 1334-1339, 1989
    • (1989) J Clin Invest , vol.84 , pp. 1334-1339
    • Molitoris, B.A.1    Dahl, R.H.2    Falk, S.A.3
  • 4
    • 0025861527 scopus 로고
    • +-atpase from its surface membrane actin cytoskeletal complex during cellular atp depletion
    • +-ATPase from its surface membrane actin cytoskeletal complex during cellular ATP depletion. J Clin Invest 88: 462-469, 1991
    • (1991) J Clin Invest , vol.88 , pp. 462-469
    • Molitoris, B.1    Geerdes, A.2    McIntosh, J.3
  • 5
    • 33745345159 scopus 로고    scopus 로고
    • Putting the actin cytoskeleton into perspective: Pathophysiology of ischemic alterations
    • Molitoris BA: Putting the actin cytoskeleton into perspective: Pathophysiology of ischemic alterations. Am J Physiol 272: F430-F433, 1997
    • (1997) Am J Physiol , vol.272
    • Molitoris, B.A.1
  • 6
    • 0030808484 scopus 로고    scopus 로고
    • Heat stress ameliorates atp depletion-induced sublethal injury in mouse proximal tubule cells
    • Borkan SC, Wang Y-H, Lieberthal W, Burke PR, Schwartz JH: Heat stress ameliorates ATP depletion-induced sublethal injury in mouse proximal tubule cells. Am J Physiol 272: F347-F355, 1997
    • (1997) Am J Physiol , vol.272
    • Borkan, S.C.1    Wang, Y.-H.2    Lieberthal, W.3    Burke, P.R.4    Schwartz, J.H.5
  • 8
    • 0018142634 scopus 로고
    • Ischemic damage and repair in the rat proximal tubule: Differences among s1, s2 and s3 segments
    • Venkatachalam MA, Bernard DB, Donohoe J, Levinsky NG: Ischemic damage and repair in the rat proximal tubule: Differences among S1, S2 and S3 segments. Kidney Int 14: 31-49, 1978
    • (1978) Kidney Int , vol.14 , pp. 31-49
    • Venkatachalam, M.A.1    Bernard, D.B.2    Donohoe, J.3    Levinsky, N.G.4
  • 9
    • 0031838272 scopus 로고    scopus 로고
    • Biology of ischemic and toxic renal tubular cell injury: Role of nitric oxide and the inflammatory response
    • Lieberthal W: Biology of ischemic and toxic renal tubular cell injury: Role of nitric oxide and the inflammatory response. Curr Opin Nephrol Hypertens 7: 289-295, 1998
    • (1998) Curr Opin Nephrol Hypertens , vol.7 , pp. 289-295
    • Lieberthal, W.1
  • 10
    • 0000656242 scopus 로고    scopus 로고
    • Acute renal failure
    • edited by Brenner B. Philadelphia, Saunders
    • Brady HR, Brenner BM, Lieberthal W: Acute renal failure. In: The Kidney, edited by Brenner B. Philadelphia, Saunders, 1996, pp 1200-1252
    • (1996) The Kidney , pp. 1200-1252
    • Brady, H.R.1    Brenner, B.M.2    Lieberthal, W.3
  • 11
    • 0023612699 scopus 로고
    • Structure, biochemistry and assembly of epithelial tight junctions
    • Gumbiner B: Structure, biochemistry and assembly of epithelial tight junctions. Am J Physiol 253: C749-C758, 1987
    • (1987) Am J Physiol , vol.253
    • Gumbiner, B.1
  • 12
    • 0027207967 scopus 로고
    • The molecular organization of tight junctions
    • Citi S: The molecular organization of tight junctions. J Cell Biol 121: 485-489, 1993
    • (1993) J Cell Biol , vol.121 , pp. 485-489
    • Citi, S.1
  • 14
    • 0030000980 scopus 로고    scopus 로고
    • Cadherin-catenin complex: Protein interactions and their implications for cadherin function
    • Aberle H, Schwartz H, Kemler R: Cadherin-catenin complex: Protein interactions and their implications for cadherin function. J Cell Biochem 61: 514-523, 1996
    • (1996) J Cell Biochem , vol.61 , pp. 514-523
    • Aberle, H.1    Schwartz, H.2    Kemler, R.3
  • 15
    • 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 T, Ernst H, Zanin M, Hoffman S, 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: 801-812, 1996
    • (1996) J Cell Biol , vol.134 , pp. 801-812
    • Balsamo, J.1    Leung, T.2    Ernst, H.3    Zanin, M.4    Hoffman, S.5    Lilien, J.6
  • 16
    • 0029797378 scopus 로고    scopus 로고
    • Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex
    • Kypta RM, Su H, Reichardt LF: Association between a transmembrane protein tyrosine phosphatase and the cadherin-catenin complex. J Cell Biol 134: 1519-1529, 1996
    • (1996) J Cell Biol , vol.134 , pp. 1519-1529
    • Kypta, R.M.1    Su, H.2    Reichardt, L.F.3
  • 17
    • 0028931103 scopus 로고
    • Evidence that tyrosine phosphorylation may increase tight junction permeability
    • Staddon JM, Herrenknecht K, Rubin LL: Evidence that tyrosine phosphorylation may increase tight junction permeability. J Cell Sci 108: 609-619, 1995
    • (1995) J Cell Sci , vol.108 , pp. 609-619
    • Staddon, J.M.1    Herrenknecht, K.2    Rubin, L.L.3
  • 19
    • 0032568815 scopus 로고    scopus 로고
    • fak in differentiated ar4-2j pancreatic acinar cells
    • FAK in differentiated AR4-2J pancreatic acinar cells. J Biol Chem 273: 16366-16373, 1998
    • (1998) J Biol Chem , vol.273 , pp. 16366-16373
    • Feick, P.1    Gilhaus, S.2    Schultz, I.3
  • 20
    • 0023216941 scopus 로고
    • Selective modulation of calcium-dependent myosin phosphorylation by novel protein kinase inhibitors, isoquinoline-sulfonamide derivatives
    • Hagiwara M, Inagaki M, Watanabe M, Ito M, Onoda K, Tanaka T, Hidaka H: Selective modulation of calcium-dependent myosin phosphorylation by novel protein kinase inhibitors, isoquinoline-sulfonamide derivatives. Mol Pharm 32: 7-12, 1987
    • (1987) Mol Pharm , vol.32 , pp. 7-12
    • Hagiwara, M.1    Inagaki, M.2    Watanabe, M.3    Ito, M.4    Onoda, K.5    Tanaka, T.6    Hidaka, H.7
  • 21
    • 0029084127 scopus 로고
    • Dephosphorylation of ezrin as an early event in renal microvillar breakdown and anoxic injury
    • Chen JJ, Cohn A, Mandel LJ: Dephosphorylation of ezrin as an early event in renal microvillar breakdown and anoxic injury. Proc Natl Acad Sci USA 92: 7495-7499, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 7495-7499
    • Chen, J.J.1    Cohn, A.2    Mandel, L.J.3
  • 22
    • 0028141180 scopus 로고
    • Decreased protein phosphorylation induced by anoxia in proximal renal tubules
    • Kobryn C, Mandel L: Decreased protein phosphorylation induced by anoxia in proximal renal tubules. Am J Physiol 267: C1073-C1079, 1994
    • (1994) Am J Physiol , vol.267
    • Kobryn, C.1    Mandel, L.2
  • 23
    • 0027339375 scopus 로고
    • Uncoupling of the molecular "fence" and paracellular "gate" functions in epithelial tight junctions
    • Mandel L, Bacallao R, Zampighi G: Uncoupling of the molecular "fence" and paracellular "gate" functions in epithelial tight junctions. Nature 361: 552-555, 1993
    • (1993) Nature , vol.361 , pp. 552-555
    • Mandel, L.1    Bacallao, R.2    Zampighi, G.3
  • 25
    • 0030056968 scopus 로고    scopus 로고
    • Cell adhesion: The molecular basis of tissue architecture and morphogenesis
    • Gumbiner BM: Cell adhesion: The molecular basis of tissue architecture and morphogenesis. Cell 84: 345-357, 1996
    • (1996) Cell , vol.84 , pp. 345-357
    • Gumbiner, B.M.1
  • 26
    • 0021166319 scopus 로고
    • Zonulae occludentes in junctional complex-enriched fractions from mouse liver: Preliminary morphological and biochemical characterization
    • Stevenson B, Siciliano J, Mooseker M, Goodenough D: Zonulae occludentes in junctional complex-enriched fractions from mouse liver: Preliminary morphological and biochemical characterization. J Cell Biol 98: 1209-1221, 1984
    • (1984) J Cell Biol , vol.98 , pp. 1209-1221
    • Stevenson, B.1    Siciliano, J.2    Mooseker, M.3    Goodenough, D.4
  • 27
    • 0029125639 scopus 로고
    • Protein tyrosine phosphatases as adhesion receptors
    • Brady-Kalnay S, Tonks N: Protein tyrosine phosphatases as adhesion receptors. Curr Opin Cell Biol 7: 650-657, 1995
    • (1995) Curr Opin Cell Biol , vol.7 , pp. 650-657
    • Brady-Kalnay, S.1    Tonks, N.2
  • 28
    • 0030297552 scopus 로고    scopus 로고
    • From form to function: Signalling by protein tyrosine phosphatases
    • Tonks N, Neel B: From form to function: Signalling by protein tyrosine phosphatases. Cell 87: 365-368, 1996
    • (1996) Cell , vol.87 , pp. 365-368
    • Tonks, N.1    Neel, B.2
  • 29
    • 0030297891 scopus 로고    scopus 로고
    • Form and function in protein phosphorylation
    • Denu J, Stuckey J, Saper M, Dixon J: Form and function in protein phosphorylation. Cell 87: 361-364, 1996
    • (1996) Cell , vol.87 , pp. 361-364
    • Denu, J.1    Stuckey, J.2    Saper, M.3    Dixon, J.4
  • 30
    • 0031026047 scopus 로고    scopus 로고
    • Hepatocyte growth factor alters the polarity of mdck cell monolayers
    • Balkovetz DF, Pollack AL, Mostov KE: Hepatocyte growth factor alters the polarity of MDCK cell monolayers. J Biol Chem 272: 3471-3477, 1997
    • (1997) J Biol Chem , vol.272 , pp. 3471-3477
    • Balkovetz, D.F.1    Pollack, A.L.2    Mostov, K.E.3
  • 31
    • 0029896163 scopus 로고    scopus 로고
    • Regulation, substrates and function of src
    • Brown MT, Cooper JC: Regulation, substrates and function of Src. Biochim Biophys Acta 1287: 121-149, 1996
    • (1996) Biochim Biophys Acta , vol.1287 , pp. 121-149
    • Brown, M.T.1    Cooper, J.C.2
  • 32
    • 0029068339 scopus 로고
    • Hypoxic induction of human vascular endothelial growth factor expression through c-src activation
    • Tsokias L, Zhou XM, Foster D, Brugge JS, Sukhatme VP: Hypoxic induction of human vascular endothelial growth factor expression through c-Src activation. Nature 375: 577-581, 1995
    • (1995) Nature , vol.375 , pp. 577-581
    • Tsokias, L.1    Zhou, X.M.2    Foster, D.3    Brugge, J.S.4    Sukhatme, V.P.5
  • 33
    • 0030582381 scopus 로고    scopus 로고
    • Hypoxia and hypoxia/regeneration activate src family tyrosine kinases and p21ras in cultured rat cardiac myocytes
    • Seko Y, Tobe K, Takahashi N, Kaburagi Y, Kadowaki T, Yazaki Y: Hypoxia and hypoxia/regeneration activate Src family tyrosine kinases and p21ras in cultured rat cardiac myocytes. Biochem Biophys Res Commun 226: 520-535, 1996
    • (1996) Biochem Biophys Res Commun , vol.226 , pp. 520-535
    • Seko, Y.1    Tobe, K.2    Takahashi, N.3    Kaburagi, Y.4    Kadowaki, T.5    Yazaki, Y.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.