메뉴 건너뛰기




Volumn 289, Issue 2 58-2, 2005, Pages

Ischemia-induced cleavage of cadherins in NRK cells: Evidence for a role of metalloproteinases

Author keywords

E cadherin; Matrix metalloproteinase; N cadherin; Normal rat kidney cells

Indexed keywords

ALPHA CATENIN; BETA CATENIN; CADHERIN; CALCIUM CHLORIDE; CALCIUM ION; CASPASE 3; CASPASE 9; EDETIC ACID; GLUCOSE TRANSPORTER 1; ILOMASTAT; IMMUNOGLOBULIN G; MAGNESIUM CHLORIDE; MAGNESIUM ION; MATRIX METALLOPROTEINASE INHIBITOR; METALLOPROTEINASE; NERVE CELL ADHESION MOLECULE; PLAKOGLOBIN; TISSUE INHIBITOR OF METALLOPROTEINASE 1; TISSUE INHIBITOR OF METALLOPROTEINASE 2; TISSUE INHIBITOR OF METALLOPROTEINASE 3; UVOMORULIN;

EID: 22344449179     PISSN: 1931857X     EISSN: 15221466     Source Type: Journal    
DOI: 10.1152/ajprenal.00351.2004     Document Type: Article
Times cited : (46)

References (46)
  • 1
    • 0032942210 scopus 로고    scopus 로고
    • Brefeldin A (BFA) disrupts the organization of the microtubule and the actin cytoskeletons
    • Alvarez C and Sztul ES. Brefeldin A (BFA) disrupts the organization of the microtubule and the actin cytoskeletons. Eur J Cell Biol 78: 1-14, 1999.
    • (1999) Eur J Cell Biol , vol.78 , pp. 1-14
    • Alvarez, C.1    Sztul, E.S.2
  • 2
    • 0032567463 scopus 로고    scopus 로고
    • Bacterial lipopolysaccharide disrupts endothelial monolayer integrity and survival signaling events through caspase cleavage of adherens junction proteins
    • Bannerman DD, Sathyamoorthy M, and Goldblum SE. Bacterial lipopolysaccharide disrupts endothelial monolayer integrity and survival signaling events through caspase cleavage of adherens junction proteins. J Biol Chem 273: 35371-35380, 1998.
    • (1998) J Biol Chem , vol.273 , pp. 35371-35380
    • Bannerman, D.D.1    Sathyamoorthy, M.2    Goldblum, S.E.3
  • 4
    • 0037087648 scopus 로고    scopus 로고
    • The Cdc42 and Rac1 GTPases are required for capillary lumen formation in three-dimensional extracellular matrices
    • Bayless KJ and Davis GE. The Cdc42 and Rac1 GTPases are required for capillary lumen formation in three-dimensional extracellular matrices. J Cell Sci 115: 1123-1136, 2002.
    • (2002) J Cell Sci , vol.115 , pp. 1123-1136
    • Bayless, K.J.1    Davis, G.E.2
  • 5
    • 0041842613 scopus 로고    scopus 로고
    • Recent advances in the pathohysiology of ischemic acute renal failure
    • 4a. Bonventre JV and Weinberg JM. Recent advances in the pathohysiology of ischemic acute renal failure. J Am Soc Nephrol 14: 2199-2210, 2003.
    • (2003) J Am Soc Nephrol , vol.14 , pp. 2199-2210
    • Bonventre, J.V.1    Weinberg, J.M.2
  • 6
    • 0034116268 scopus 로고    scopus 로고
    • Selective degradation of E-cadherin and dissolution of E-cadherin-catenin complexes in epithelial ischemia
    • Bush KT, Tsukamoto T, and Nigam SK. Selective degradation of E-cadherin and dissolution of E-cadherin-catenin complexes in epithelial ischemia. Am J Physiol Renal Physiol 278: F847-F852, 2000.
    • (2000) Am J Physiol Renal Physiol , vol.278
    • Bush, K.T.1    Tsukamoto, T.2    Nigam, S.K.3
  • 8
    • 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
  • 10
    • 0034637579 scopus 로고    scopus 로고
    • μ-protocadherin, a novel developmentally regulated protocadherin with mucin-like domains
    • Goldberg M, Peshkovsky C, Shifteh A, and Al-Awqati Q. μ-Protocadherin, a novel developmentally regulated protocadherin with mucin-like domains. J Biol Chem 275: 24622-24629, 2000.
    • (2000) J Biol Chem , vol.275 , pp. 24622-24629
    • Goldberg, M.1    Peshkovsky, C.2    Shifteh, A.3    Al-Awqati, Q.4
  • 12
    • 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
  • 15
    • 0035946989 scopus 로고    scopus 로고
    • FK506, but not cyclosporin A, prevents mitochondrial dysfunction during hypoxia in rat hepatocytes
    • Kaibori M, Inoue T, Tu W, Oda M, Kwon AH, Kamiyama Y, and Okumura T. FK506, but not cyclosporin A, prevents mitochondrial dysfunction during hypoxia in rat hepatocytes. Life Sci 69: 17-26, 2001.
    • (2001) Life Sci , vol.69 , pp. 17-26
    • Kaibori, M.1    Inoue, T.2    Tu, W.3    Oda, M.4    Kwon, A.H.5    Kamiyama, Y.6    Okumura, T.7
  • 16
    • 0038352085 scopus 로고    scopus 로고
    • Biochemical processing of E-cadherin under cellular stress
    • Keller SH and Nigam SK. Biochemical processing of E-cadherin under cellular stress. Biochem Biophys Res Commun 307: 215-223, 2003.
    • (2003) Biochem Biophys Res Commun , vol.307 , pp. 215-223
    • Keller, S.H.1    Nigam, S.K.2
  • 18
    • 0031426654 scopus 로고    scopus 로고
    • Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells
    • Lochter A, Galosy S, Muschler J, Freedman N, Werb Z, and Bissell MJ. Matrix metalloproteinase stromelysin-1 triggers a cascade of molecular alterations that leads to stable epithelial-to-mesenchymal conversion and a premalignant phenotype in mammary epithelial cells. J Cell Biol 139: 1861-1872, 1997.
    • (1997) J Cell Biol , vol.139 , pp. 1861-1872
    • Lochter, A.1    Galosy, S.2    Muschler, J.3    Freedman, N.4    Werb, Z.5    Bissell, M.J.6
  • 20
    • 0037568364 scopus 로고    scopus 로고
    • Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium
    • McGuire JK, Li Q, and Parks WC. Matrilysin (matrix metalloproteinase-7) mediates E-cadherin ectodomain shedding in injured lung epithelium. Am J Pathol 162: 1831-1843, 2003.
    • (2003) Am J Pathol , vol.162 , pp. 1831-1843
    • McGuire, J.K.1    Li, Q.2    Parks, W.C.3
  • 21
    • 0037458926 scopus 로고    scopus 로고
    • Liposomal delivery of heat shock protein 72 into renal tubular cells blocks nuclear factor-κB activation, tumor necrosis factor-α production, and subsequent ischemia-induced apoptosis
    • Meldrum KK, Burnett AL, Meng X, Misseri R, Shaw MBK, Gearhart JP, and Meldrum DR. Liposomal delivery of heat shock protein 72 into renal tubular cells blocks nuclear factor-κB activation, tumor necrosis factor-α production, and subsequent ischemia-induced apoptosis. Circ Res 92: 293-299, 2003.
    • (2003) Circ Res , vol.92 , pp. 293-299
    • Meldrum, K.K.1    Burnett, A.L.2    Meng, X.3    Misseri, R.4    Shaw, M.B.K.5    Gearhart, J.P.6    Meldrum, D.R.7
  • 22
    • 0036285014 scopus 로고    scopus 로고
    • Simulated ischemia induces renal tubular cell apoptosis through a nuclear factor-κB dependent mechanism
    • Meldrum KK, Hile K, Meldrum DR, Crone JA, Gearhart JP, and Burnett AL. Simulated ischemia induces renal tubular cell apoptosis through a nuclear factor-κB dependent mechanism. J Urol 168: 248-252, 2002.
    • (2002) J Urol , vol.168 , pp. 248-252
    • Meldrum, K.K.1    Hile, K.2    Meldrum, D.R.3    Crone, J.A.4    Gearhart, J.P.5    Burnett, A.L.6
  • 23
    • 0034894967 scopus 로고    scopus 로고
    • A novel model of ischemia in renal tubular cells which closely parallels in vivo injury
    • Meldrum KK, Meldrum DR, Hile KL, Burnett AL, and Harken AH. A novel model of ischemia in renal tubular cells which closely parallels in vivo injury. J Surg Res 99: 288-293, 2001.
    • (2001) J Surg Res , vol.99 , pp. 288-293
    • Meldrum, K.K.1    Meldrum, D.R.2    Hile, K.L.3    Burnett, A.L.4    Harken, A.H.5
  • 25
    • 0033135667 scopus 로고    scopus 로고
    • The role of cell adhesion molecules in ischemic acute renal failure
    • Molitoris BA and Marrs J. The role of cell adhesion molecules in ischemic acute renal failure. Am J Med 106: 583-592, 1999.
    • (1999) Am J Med , vol.106 , pp. 583-592
    • Molitoris, B.A.1    Marrs, J.2
  • 26
    • 0038047053 scopus 로고    scopus 로고
    • Temporal expression and activation of matrix metalloproteinases-2, -9, and membrane type 1-matrix metalloproteinase following acute hindlimb ischemia
    • Muhs BE, Plitas G, Delgado Y, Ianus I, Shaw JP, Adelman MA, Lamparello P, Shamamian P, and Gagne P. Temporal expression and activation of matrix metalloproteinases-2, -9, and membrane type 1-matrix metalloproteinase following acute hindlimb ischemia. J Surg Res 111: 8-15, 2003.
    • (2003) J Surg Res , vol.111 , pp. 8-15
    • Muhs, B.E.1    Plitas, G.2    Delgado, Y.3    Ianus, I.4    Shaw, J.P.5    Adelman, M.A.6    Lamparello, P.7    Shamamian, P.8    Gagne, P.9
  • 27
    • 9644267507 scopus 로고    scopus 로고
    • N-cadherin cleavage during activated hepatic stellate cell apoptosis is inhibited by tissue inhibitor of metalloproteinase-1
    • Murphy F, Waung J, Collins J, Arthur MJ, Nagase H, Mann D, Benyon RC, and Iredale JP. N-cadherin cleavage during activated hepatic stellate cell apoptosis is inhibited by tissue inhibitor of metalloproteinase-1 (Abstract). Comp Hepatol 3, Suppl 1: S8, 2004.
    • (2004) Comp Hepatol , vol.3 , Issue.SUPPL. 1
    • Murphy, F.1    Waung, J.2    Collins, J.3    Arthur, M.J.4    Nagase, H.5    Mann, D.6    Benyon, R.C.7    Iredale, J.P.8
  • 28
    • 0025799478 scopus 로고
    • The origin of matrix metalloproteinases and their familial relationships
    • Murphy GJ, Murphy G, and Reynolds JJ. The origin of matrix metalloproteinases and their familial relationships. FEBS Lett 289: 4-7, 1991.
    • (1991) FEBS Lett , vol.289 , pp. 4-7
    • Murphy, G.J.1    Murphy, G.2    Reynolds, J.J.3
  • 29
    • 0025752664 scopus 로고
    • The 102 kd cadherin-associated protein: Similarity to vinculin and posttranscriptional regulation of expression
    • Nagafuchi A, Takeichi M, and Tsukita S. The 102 kd cadherin-associated protein: similarity to vinculin and posttranscriptional regulation of expression. Cell 65: 849-857, 1991.
    • (1991) Cell , vol.65 , pp. 849-857
    • Nagafuchi, A.1    Takeichi, M.2    Tsukita, S.3
  • 30
    • 0033618337 scopus 로고    scopus 로고
    • Matrix metalloproteinases
    • Nagase H and Woessner JF Jr. Matrix metalloproteinases. J Biol Chem 274: 21491-21494, 1999.
    • (1999) J Biol Chem , vol.274 , pp. 21491-21494
    • Nagase, H.1    Woessner Jr., J.F.2
  • 32
    • 0036232486 scopus 로고    scopus 로고
    • ATP depletion of tubular cells causes dissociation of the zonula adherens and nuclear translocation of beta-catenin and LEF-1
    • Price VR, Reed CA, Lieberthal W, and Schwartz JH. ATP depletion of tubular cells causes dissociation of the zonula adherens and nuclear translocation of beta-catenin and LEF-1. J Am Soc Nephrol 13: 1152-1161, 2002.
    • (2002) J Am Soc Nephrol , vol.13 , pp. 1152-1161
    • Price, V.R.1    Reed, C.A.2    Lieberthal, W.3    Schwartz, J.H.4
  • 33
    • 0037841983 scopus 로고    scopus 로고
    • Imbalance between tissue inhibitor of metalloproteinase-4 and matrix metalloproteinases during acute myocardial ischemia-reperfusion injury
    • Schulze CJ, Wang W, Suarez-Pinzon WL, Sawicka J, Sawicki G, and Schulz R. Imbalance between tissue inhibitor of metalloproteinase-4 and matrix metalloproteinases during acute myocardial ischemia-reperfusion injury. Circulation 107: 2487-2492, 2003.
    • (2003) Circulation , vol.107 , pp. 2487-2492
    • Schulze, C.J.1    Wang, W.2    Suarez-Pinzon, W.L.3    Sawicka, J.4    Sawicki, G.5    Schulz, R.6
  • 35
    • 0029148192 scopus 로고
    • Cadherin 11 expression marks the mesenchymal phenotype: Towards new functions for cadherins?
    • Simonneau L, Kitagawa M, Suzuki S, and Thiery JP. Cadherin 11 expression marks the mesenchymal phenotype: towards new functions for cadherins? Cell Adhes Commun 3: 115-130, 1995.
    • (1995) Cell Adhes Commun , vol.3 , pp. 115-130
    • Simonneau, L.1    Kitagawa, M.2    Suzuki, S.3    Thiery, J.P.4
  • 37
    • 1842510647 scopus 로고    scopus 로고
    • Activation of matrix metalloproteinase-3 and agrin cleavage in cerebral ischemia/reperfusion
    • Sole S, Petegnief V, Gorina R, Chamorro A, and Planas AM. Activation of matrix metalloproteinase-3 and agrin cleavage in cerebral ischemia/reperfusion. J Neuropathol Exp Neurol 63: 338-349, 2004.
    • (2004) J Neuropathol Exp Neurol , vol.63 , pp. 338-349
    • Sole, S.1    Petegnief, V.2    Gorina, R.3    Chamorro, A.4    Planas, A.M.5
  • 39
    • 0032842426 scopus 로고    scopus 로고
    • Structural and signalling molecules come together at tight junctions
    • Tsukita S, Furuse M, and Itoh M. Structural and signalling molecules come together at tight junctions. Curr Opin Cell Biol 11: 628-633, 1999.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 628-633
    • Tsukita, S.1    Furuse, M.2    Itoh, M.3
  • 42
    • 0041633505 scopus 로고    scopus 로고
    • Novel approaches to the treatment of acute renal failure
    • Venkataraman R and Kellum JA. Novel approaches to the treatment of acute renal failure. Expert Opin Investig Drugs 12: 1353-1366, 2003.
    • (2003) Expert Opin Investig Drugs , vol.12 , pp. 1353-1366
    • Venkataraman, R.1    Kellum, J.A.2
  • 43
    • 0031888098 scopus 로고    scopus 로고
    • Beta-catenin: A key mediator of Wnt signaling
    • Willert K and Nusse R. Beta-catenin: a key mediator of Wnt signaling. Curr Opin Genet Dev 8: 95-102, 1998.
    • (1998) Curr Opin Genet Dev , vol.8 , pp. 95-102
    • Willert, K.1    Nusse, R.2
  • 44
    • 0033063445 scopus 로고    scopus 로고
    • A striking organization of a large family of human neural cadherin-like cell adhesion genes
    • Wu Q and Maniatis T. A striking organization of a large family of human neural cadherin-like cell adhesion genes. Cell 97: 779-790, 1999.
    • (1999) Cell , vol.97 , pp. 779-790
    • Wu, Q.1    Maniatis, T.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.