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Volumn 47, Issue 11, 2009, Pages 1561-1569

Remodeling of the tight junction during recovery from exposure to hydrogen peroxide in kidney epithelial cells

Author keywords

Barrier function; Free radicals; Kidney epithelium; Oxidative stress; Tight junction

Indexed keywords

CASPASE 3; CLAUDIN 1; CLAUDIN 2; HYDROGEN PEROXIDE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; MITOGEN ACTIVATED PROTEIN KINASE P38; OCCLUDIN;

EID: 70449109156     PISSN: 08915849     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.freeradbiomed.2009.08.024     Document Type: Article
Times cited : (48)

References (49)
  • 1
    • 0031944250 scopus 로고    scopus 로고
    • Molecular architecture of tight junctions
    • Mitic L.L., and Anderson J.M. Molecular architecture of tight junctions. Annu. Rev. Physiol. 60 (1998) 121-142
    • (1998) Annu. Rev. Physiol. , vol.60 , pp. 121-142
    • Mitic, L.L.1    Anderson, J.M.2
  • 5
    • 15244341423 scopus 로고    scopus 로고
    • Epithelial barrier dysfunction: a unifying theme to explain the pathogenesis of multiple organ dysfunction at the cellular level
    • Fink M.P., and Delude R.L. Epithelial barrier dysfunction: a unifying theme to explain the pathogenesis of multiple organ dysfunction at the cellular level. Crit. Care Clin. 21 (2005) 177-196
    • (2005) Crit. Care Clin. , vol.21 , pp. 177-196
    • Fink, M.P.1    Delude, R.L.2
  • 7
    • 0033970202 scopus 로고    scopus 로고
    • Acute renal failure. II. Experimental models of acute renal failure: imperfect but indispensable
    • Lieberthal W., and Nigam S.K. Acute renal failure. II. Experimental models of acute renal failure: imperfect but indispensable. Am. J. Physiol., Renal Physiol. 278 (2000) F1-F12
    • (2000) Am. J. Physiol., Renal Physiol. , vol.278
    • Lieberthal, W.1    Nigam, S.K.2
  • 8
    • 3242772187 scopus 로고    scopus 로고
    • Ischemic acute renal failure: an inflammatory disease?
    • Bonventre J.V., and Zuk A. Ischemic acute renal failure: an inflammatory disease?. Kidney Int. 66 (2004) 480-485
    • (2004) Kidney Int. , vol.66 , pp. 480-485
    • Bonventre, J.V.1    Zuk, A.2
  • 9
    • 33847050223 scopus 로고    scopus 로고
    • The inflammatory response to ischemic acute kidney injury: a result of the 'right stuff' in the 'wrong place'?
    • Lu C.Y., Hartono J., Senitko M., and Chen J. The inflammatory response to ischemic acute kidney injury: a result of the 'right stuff' in the 'wrong place'?. Curr. Opin. Nephrol. Hypertens. 16 (2007) 83-89
    • (2007) Curr. Opin. Nephrol. Hypertens. , vol.16 , pp. 83-89
    • Lu, C.Y.1    Hartono, J.2    Senitko, M.3    Chen, J.4
  • 10
    • 38649127552 scopus 로고    scopus 로고
    • Oxidant-mediated apoptosis in proximal tubular epithelial cells following ATP depletion and recovery
    • Maenpaa C.J., Shames B.D., Van Why S.K., Johnson C.P., and Nilakantan V. Oxidant-mediated apoptosis in proximal tubular epithelial cells following ATP depletion and recovery. Free Radic. Biol. Med. 44 (2008) 518-526
    • (2008) Free Radic. Biol. Med. , vol.44 , pp. 518-526
    • Maenpaa, C.J.1    Shames, B.D.2    Van Why, S.K.3    Johnson, C.P.4    Nilakantan, V.5
  • 11
    • 0022387826 scopus 로고
    • Oxidants increase paracellular permeability in a cultured epithelial cell line
    • Welsh M.J., Shasby D.M., and Husted R.M. Oxidants increase paracellular permeability in a cultured epithelial cell line. J. Clin. Invest. 76 (1985) 1155-1168
    • (1985) J. Clin. Invest. , vol.76 , pp. 1155-1168
    • Welsh, M.J.1    Shasby, D.M.2    Husted, R.M.3
  • 13
    • 33847010257 scopus 로고    scopus 로고
    • Effect of proinflammatory cytokines, tumor necrosis factor-alpha and interferon-gamma on epithelial barrier function and matrix metalloproteinase-9 in Madin Darby canine kidney cells
    • Leone A.K., Chun J.A., Koehler C.L., Caranto J., and King J.M. Effect of proinflammatory cytokines, tumor necrosis factor-alpha and interferon-gamma on epithelial barrier function and matrix metalloproteinase-9 in Madin Darby canine kidney cells. Cell. Physiol. Biochem. 19 (2007) 99-112
    • (2007) Cell. Physiol. Biochem. , vol.19 , pp. 99-112
    • Leone, A.K.1    Chun, J.A.2    Koehler, C.L.3    Caranto, J.4    King, J.M.5
  • 14
    • 0038617335 scopus 로고    scopus 로고
    • Functional analysis of tight junctions
    • Matter K., and Balda M.S. Functional analysis of tight junctions. Methods 30 (2003) 228-234
    • (2003) Methods , vol.30 , pp. 228-234
    • Matter, K.1    Balda, M.S.2
  • 15
    • 0031425958 scopus 로고    scopus 로고
    • Phosphorylation of occludin correlates with occludin localization and function at the tight junction
    • Wong V. Phosphorylation of occludin correlates with occludin localization and function at the tight junction. Am. J. Physiol. 273 (1997) C1859-C1867
    • (1997) Am. J. Physiol. , vol.273
    • Wong, V.1
  • 16
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies S.P., Reddy H., Caivano M., and Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351 (2000) 95-105
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 17
    • 33748743740 scopus 로고    scopus 로고
    • Multiple activation mechanisms of p38alpha mitogen-activated protein kinase
    • Kang Y.J., Seit-Nebi A., Davis R.J., and Han J. Multiple activation mechanisms of p38alpha mitogen-activated protein kinase. J. Biol. Chem. 281 (2006) 26225-26234
    • (2006) J. Biol. Chem. , vol.281 , pp. 26225-26234
    • Kang, Y.J.1    Seit-Nebi, A.2    Davis, R.J.3    Han, J.4
  • 18
    • 33745631769 scopus 로고    scopus 로고
    • 2, a necessary evil for cell signaling
    • 2, a necessary evil for cell signaling. Science 312 (2006) 1882-1883
    • (2006) Science , vol.312 , pp. 1882-1883
    • Rhee, S.G.1
  • 19
    • 0036086130 scopus 로고    scopus 로고
    • Free radicals in the physiological control of cell function
    • Droge W. Free radicals in the physiological control of cell function. Physiol. Rev. 82 (2002) 47-95
    • (2002) Physiol. Rev. , vol.82 , pp. 47-95
    • Droge, W.1
  • 20
    • 55149107716 scopus 로고    scopus 로고
    • Radical-free biology of oxidative stress
    • Jones D.P. Radical-free biology of oxidative stress. Am. J. Physiol., Cell Physiol. 295 (2008) C849-868
    • (2008) Am. J. Physiol., Cell Physiol. , vol.295
    • Jones, D.P.1
  • 21
    • 20444400257 scopus 로고    scopus 로고
    • Redox redux: revisiting PTPs and the control of cell signaling
    • Tonks N.K. Redox redux: revisiting PTPs and the control of cell signaling. Cell 121 (2005) 667-670
    • (2005) Cell , vol.121 , pp. 667-670
    • Tonks, N.K.1
  • 23
    • 61949143204 scopus 로고    scopus 로고
    • Oxygen in health and disease: regulation of oxygen homeostasis-clinical implications
    • Maltepe E., and Saugstad O.D. Oxygen in health and disease: regulation of oxygen homeostasis-clinical implications. Pediatr. Res. 65 (2009) 261-268
    • (2009) Pediatr. Res. , vol.65 , pp. 261-268
    • Maltepe, E.1    Saugstad, O.D.2
  • 25
    • 0029799520 scopus 로고    scopus 로고
    • Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein
    • Balda M.S., Whitney J.A., Flores C., Gonzalez S., Cereijido M., and Matter K. Functional dissociation of paracellular permeability and transepithelial electrical resistance and disruption of the apical-basolateral intramembrane diffusion barrier by expression of a mutant tight junction membrane protein. J. Cell Biol. 134 (1996) 1031-1049
    • (1996) J. Cell Biol. , vol.134 , pp. 1031-1049
    • Balda, M.S.1    Whitney, J.A.2    Flores, C.3    Gonzalez, S.4    Cereijido, M.5    Matter, K.6
  • 26
    • 0035933894 scopus 로고    scopus 로고
    • Reassembly of the tight junction after oxidative stress depends on tyrosine kinase activity
    • Meyer T.N., Schwesinger C., Ye J., Denker B.M., and Nigam S.K. Reassembly of the tight junction after oxidative stress depends on tyrosine kinase activity. J. Biol. Chem. 276 (2001) 22048-22055
    • (2001) J. Biol. Chem. , vol.276 , pp. 22048-22055
    • Meyer, T.N.1    Schwesinger, C.2    Ye, J.3    Denker, B.M.4    Nigam, S.K.5
  • 27
    • 25444507662 scopus 로고    scopus 로고
    • Development of tight junction molecules in blood vessels of germinal matrix, cerebral cortex, and white matter
    • Ballabh P., Hu F., Kumarasiri M., Braun A., and Nedergaard M. Development of tight junction molecules in blood vessels of germinal matrix, cerebral cortex, and white matter. Pediatr. Res. 58 (2005) 791-798
    • (2005) Pediatr. Res. , vol.58 , pp. 791-798
    • Ballabh, P.1    Hu, F.2    Kumarasiri, M.3    Braun, A.4    Nedergaard, M.5
  • 28
    • 33751190327 scopus 로고    scopus 로고
    • A death-promoting role for extracellular signal-regulated kinase
    • Zhuang S., and Schnellmann R.G. A death-promoting role for extracellular signal-regulated kinase. J. Pharmacol. Exp. Ther. 319 (2006) 991-997
    • (2006) J. Pharmacol. Exp. Ther. , vol.319 , pp. 991-997
    • Zhuang, S.1    Schnellmann, R.G.2
  • 30
    • 44249090447 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinase activation mediates mitochondrial dysfunction and necrosis induced by hydrogen peroxide in renal proximal tubular cells
    • Zhuang S., Kinsey G.R., Yan Y., Han J., and Schnellmann R.G. Extracellular signal-regulated kinase activation mediates mitochondrial dysfunction and necrosis induced by hydrogen peroxide in renal proximal tubular cells. J. Pharmacol. Exp. Ther. 325 (2008) 732-740
    • (2008) J. Pharmacol. Exp. Ther. , vol.325 , pp. 732-740
    • Zhuang, S.1    Kinsey, G.R.2    Yan, Y.3    Han, J.4    Schnellmann, R.G.5
  • 31
  • 33
    • 33645963995 scopus 로고    scopus 로고
    • Claudins and epithelial paracellular transport
    • Van Itallie C.M., and Anderson J.M. Claudins and epithelial paracellular transport. Annu. Rev. Physiol. 68 (2006) 403-429
    • (2006) Annu. Rev. Physiol. , vol.68 , pp. 403-429
    • Van Itallie, C.M.1    Anderson, J.M.2
  • 36
    • 30044442771 scopus 로고    scopus 로고
    • MAPK interacts with occludin and mediates EGF-induced prevention of tight junction disruption by hydrogen peroxide
    • Basuroy S., Seth A., Elias B., Naren A.P., and Rao R. MAPK interacts with occludin and mediates EGF-induced prevention of tight junction disruption by hydrogen peroxide. Biochem. J. 393 (2006) 69-77
    • (2006) Biochem. J. , vol.393 , pp. 69-77
    • Basuroy, S.1    Seth, A.2    Elias, B.3    Naren, A.P.4    Rao, R.5
  • 37
    • 0037337817 scopus 로고    scopus 로고
    • Modulation of renal epithelial barrier function by mitogen-activated protein kinases (MAPKs): mechanism of cyclosporine A-induced increase in transepithelial resistance
    • Kiely B., Feldman G., and Ryan M.P. Modulation of renal epithelial barrier function by mitogen-activated protein kinases (MAPKs): mechanism of cyclosporine A-induced increase in transepithelial resistance. Kidney Int. 63 (2003) 908-916
    • (2003) Kidney Int. , vol.63 , pp. 908-916
    • Kiely, B.1    Feldman, G.2    Ryan, M.P.3
  • 38
    • 13544266585 scopus 로고    scopus 로고
    • Extracellular signal-regulated kinases 1/2 control claudin-2 expression in Madin-Darby canine kidney strain I and II cells
    • Lipschutz J.H., Li S., Arisco A., and Balkovetz D.F. Extracellular signal-regulated kinases 1/2 control claudin-2 expression in Madin-Darby canine kidney strain I and II cells. J. Biol. Chem. 280 (2005) 3780-3788
    • (2005) J. Biol. Chem. , vol.280 , pp. 3780-3788
    • Lipschutz, J.H.1    Li, S.2    Arisco, A.3    Balkovetz, D.F.4
  • 39
    • 21444450963 scopus 로고    scopus 로고
    • 2 induces paracellular permeability of porcine brain-derived microvascular endothelial cells by activation of the p44/42 MAP kinase pathway
    • 2 induces paracellular permeability of porcine brain-derived microvascular endothelial cells by activation of the p44/42 MAP kinase pathway. Eur. J. Cell Biol. 84 (2005) 687-697
    • (2005) Eur. J. Cell Biol. , vol.84 , pp. 687-697
    • Fischer, S.1    Wiesnet, M.2    Renz, D.3    Schaper, W.4
  • 41
    • 33645014120 scopus 로고    scopus 로고
    • Proinflammatory cytokines tumor necrosis factor-alpha and interferon-gamma modulate epithelial barrier function in Madin-Darby canine kidney cells through mitogen activated protein kinase signaling
    • Patrick D.M., Leone A.K., Shellenberger J.J., Dudowicz K.A., and King J.M. Proinflammatory cytokines tumor necrosis factor-alpha and interferon-gamma modulate epithelial barrier function in Madin-Darby canine kidney cells through mitogen activated protein kinase signaling. BMC Physiol. 6 (2006) 2
    • (2006) BMC Physiol. , vol.6 , pp. 2
    • Patrick, D.M.1    Leone, A.K.2    Shellenberger, J.J.3    Dudowicz, K.A.4    King, J.M.5
  • 42
    • 0942287209 scopus 로고    scopus 로고
    • Epidermal growth factor receptor activation differentially regulates claudin expression and enhances transepithelial resistance in Madin-Darby canine kidney cells
    • Singh A.B., and Harris R.C. Epidermal growth factor receptor activation differentially regulates claudin expression and enhances transepithelial resistance in Madin-Darby canine kidney cells. J. Biol. Chem. 279 (2004) 3543-3552
    • (2004) J. Biol. Chem. , vol.279 , pp. 3543-3552
    • Singh, A.B.1    Harris, R.C.2
  • 43
    • 0027936755 scopus 로고
    • A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells
    • Han J., Lee J.D., Bibbs L., and Ulevitch R.J. A MAP kinase targeted by endotoxin and hyperosmolarity in mammalian cells. Science 265 (1994) 808-811
    • (1994) Science , vol.265 , pp. 808-811
    • Han, J.1    Lee, J.D.2    Bibbs, L.3    Ulevitch, R.J.4
  • 46
    • 0034844097 scopus 로고    scopus 로고
    • The role of p38 MAP kinase in hydrogen peroxide mediated endothelial solute permeability
    • Kevil C.G., Oshima T., and Alexander J.S. The role of p38 MAP kinase in hydrogen peroxide mediated endothelial solute permeability. Endothelium 8 (2001) 107-116
    • (2001) Endothelium , vol.8 , pp. 107-116
    • Kevil, C.G.1    Oshima, T.2    Alexander, J.S.3
  • 47
    • 38549181147 scopus 로고    scopus 로고
    • Wip1 protects hydrogen peroxide-induced colonic epithelial barrier dysfunction
    • Oshima T., Sasaki M., Kataoka H., Miwa H., Takeuchi T., and Joh T. Wip1 protects hydrogen peroxide-induced colonic epithelial barrier dysfunction. Cell. Mol. Life Sci. 64 (2007) 3139-3147
    • (2007) Cell. Mol. Life Sci. , vol.64 , pp. 3139-3147
    • Oshima, T.1    Sasaki, M.2    Kataoka, H.3    Miwa, H.4    Takeuchi, T.5    Joh, T.6
  • 48
    • 42449141549 scopus 로고    scopus 로고
    • Regulation of dedifferentiation and redifferentiation in renal proximal tubular cells by the epidermal growth factor receptor
    • Hallman M.A., Zhuang S., and Schnellmann R.G. Regulation of dedifferentiation and redifferentiation in renal proximal tubular cells by the epidermal growth factor receptor. J. Pharmacol. Exp. Ther. 325 (2008) 520-528
    • (2008) J. Pharmacol. Exp. Ther. , vol.325 , pp. 520-528
    • Hallman, M.A.1    Zhuang, S.2    Schnellmann, R.G.3
  • 49
    • 20444417067 scopus 로고    scopus 로고
    • p38 kinase-mediated transactivation of the epidermal growth factor receptor is required for dedifferentiation of renal epithelial cells after oxidant injury
    • Zhuang S., Yan Y., Han J., and Schnellmann R.G. p38 kinase-mediated transactivation of the epidermal growth factor receptor is required for dedifferentiation of renal epithelial cells after oxidant injury. J. Biol. Chem. 280 (2005) 21036-21042
    • (2005) J. Biol. Chem. , vol.280 , pp. 21036-21042
    • Zhuang, S.1    Yan, Y.2    Han, J.3    Schnellmann, R.G.4


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