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Volumn 1043, Issue , 2005, Pages 609-616

Effects of advanced glycation end products on ezrin-dependent functions in LLC-PK1 proximal tubule cells

Author keywords

Advanced glycation end products; Diabetes; Diabetic complications; ERM proteins; Ezrin; Kidney; Nephropathy; Proximal tubule

Indexed keywords

ACTIN; ADVANCED GLYCATION END PRODUCT; CELL MEMBRANE PROTEIN; EPIDERMAL GROWTH FACTOR RECEPTOR; EZRIN; MOESIN; RADIXIN;

EID: 23744470202     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1196/annals.1338.069     Document Type: Conference Paper
Times cited : (5)

References (42)
  • 1
    • 0142089900 scopus 로고    scopus 로고
    • Evolving concepts in advanced glycation, diabetic nephropathy and diabetic vascular disease
    • JERUMS, G. et al. 2003. Evolving concepts in advanced glycation, diabetic nephropathy and diabetic vascular disease. Arch. Biochem. Biophys. 419: 55-62.
    • (2003) Arch. Biochem. Biophys. , vol.419 , pp. 55-62
    • Jerums, G.1
  • 2
    • 0028453652 scopus 로고
    • Glycation and diabetic complications
    • BROWNLEE, M. 1994. Glycation and diabetic complications. Diabetes 43: 836-841.
    • (1994) Diabetes , vol.43 , pp. 836-841
    • Brownlee, M.1
  • 3
    • 0242468729 scopus 로고    scopus 로고
    • Quantitative screening of AGEs in cellular and extracellular proteins by tandem mass spectrometry
    • THORNALLEY, P.J. et al. 2003. Quantitative screening of AGEs in cellular and extracellular proteins by tandem mass spectrometry. Biochem. J. 375: 581-592.
    • (2003) Biochem. J. , vol.375 , pp. 581-592
    • Thornalley, P.J.1
  • 4
    • 0029118168 scopus 로고
    • Formation of immunochemical AGEs precedes and correlates with early manifestations of renal and retinal disease in diabetes
    • BEISSWENGER, P.J. et al. 1995. Formation of immunochemical AGEs precedes and correlates with early manifestations of renal and retinal disease in diabetes. Diabetes 44: 824-829.
    • (1995) Diabetes , vol.44 , pp. 824-829
    • Beisswenger, P.J.1
  • 5
    • 0027970304 scopus 로고
    • AGEs induce glomerular sclerosis and albuminuria in normal rats
    • VLASSARA, H. et al. 1994. AGEs induce glomerular sclerosis and albuminuria in normal rats. Proc. Natl. Acad. Sci. USA 91: 11704-11708.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11704-11708
    • Vlassara, H.1
  • 6
    • 0035125966 scopus 로고    scopus 로고
    • Renoprotective effects of a novel inhibitor of advanced glycation
    • FORBES, J.M. et al. 2001. Renoprotective effects of a novel inhibitor of advanced glycation. Diabetologia 44: 108-114.
    • (2001) Diabetologia , vol.44 , pp. 108-114
    • Forbes, J.M.1
  • 7
    • 0030061699 scopus 로고    scopus 로고
    • Receptor-mediated endothelial cell dysfunction in diabetic vasculopathy. Soluble receptor for advanced glycation end products blocks hyperpermeability in diabetic rats
    • WAUTIER, J.L. et al. 1996. Receptor-mediated endothelial cell dysfunction in diabetic vasculopathy. Soluble receptor for advanced glycation end products blocks hyperpermeability in diabetic rats. J. Clin. Invest. 97: 238-243.
    • (1996) J. Clin. Invest. , vol.97 , pp. 238-243
    • Wautier, J.L.1
  • 8
    • 0026323337 scopus 로고
    • Aminoguanidine treatment inhibits the development of experimental diabetic retinopathy
    • HAMMES, H. et al. 1991. Aminoguanidine treatment inhibits the development of experimental diabetic retinopathy. Proc. Natl. Acad. Sci. USA 88: 11555-11558.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 11555-11558
    • Hammes, H.1
  • 9
    • 0025787122 scopus 로고
    • Aminoguanidine effects on nerve blood flow, vascular permeability, electrophysiology, and oxygen free radicals
    • KIHARA, M. et al. 1991. Aminoguanidine effects on nerve blood flow, vascular permeability, electrophysiology, and oxygen free radicals. Proc. Natl. Acad. Sci. USA 88: 6107-6111.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 6107-6111
    • Kihara, M.1
  • 10
    • 0030907178 scopus 로고    scopus 로고
    • Vascular hypertrophy in experimental diabetes: Role of advanced glycation end products
    • RUMBLE, J.R. et al. 1997. Vascular hypertrophy in experimental diabetes: role of advanced glycation end products. J. Clin. Invest. 99: 1016-1027.
    • (1997) J. Clin. Invest. , vol.99 , pp. 1016-1027
    • Rumble, J.R.1
  • 11
    • 3042704196 scopus 로고    scopus 로고
    • Advanced glycation end product interventions reduce diabetes-accelerated atherosclerosis
    • FORBES, J.M. et al. 2004. Advanced glycation end product interventions reduce diabetes-accelerated atherosclerosis. Diabetes 53: 1813-1823.
    • (2004) Diabetes , vol.53 , pp. 1813-1823
    • Forbes, J.M.1
  • 12
    • 0035856980 scopus 로고    scopus 로고
    • Biochemistry and molecular cell biology of diabetic complications
    • BROWNLEE, M. 2001. Biochemistry and molecular cell biology of diabetic complications. Nature 414: 813-820.
    • (2001) Nature , vol.414 , pp. 813-820
    • Brownlee, M.1
  • 13
    • 0028304845 scopus 로고
    • Nonenzymatic glycosylation in vitro and in bovine endothelial cells alters basic fibroblast growth factor activity
    • GIARDINO, I., D. EDELSTEIN & M. BROWNLEE. 1994. Nonenzymatic glycosylation in vitro and in bovine endothelial cells alters basic fibroblast growth factor activity. J. Clin. Invest. 94: 110-117.
    • (1994) J. Clin. Invest. , vol.94 , pp. 110-117
    • Giardino, I.1    Edelstein, D.2    Brownlee, M.3
  • 14
    • 0026659883 scopus 로고
    • Cloning and expression of a cell surface receptor for advanced glycosylation endproducts of proteins
    • NEEPER, M. et al. 1992. Cloning and expression of a cell surface receptor for advanced glycosylation endproducts of proteins. J. Biol. Chem. 267: 14998-15004.
    • (1992) J. Biol. Chem. , vol.267 , pp. 14998-15004
    • Neeper, M.1
  • 15
    • 0030811664 scopus 로고    scopus 로고
    • Advanced glycation end products and their receptors co-localise in rat organs susceptible to diabetic microvascular injury
    • SOULIS, T. et al. 1997. Advanced glycation end products and their receptors co-localise in rat organs susceptible to diabetic microvascular injury. Diabetologia 40: 619-628.
    • (1997) Diabetologia , vol.40 , pp. 619-628
    • Soulis, T.1
  • 16
    • 0028875176 scopus 로고
    • Antibacterial activity of lysozyme and lactoferrin is inhibited by binding of advanced glycation-modified proteins to a conserved motif
    • LI, Y.M., A.X. TAN & H. VLASSARA. 1995. Antibacterial activity of lysozyme and lactoferrin is inhibited by binding of advanced glycation-modified proteins to a conserved motif. Nat. Med. 1: 1057-1061.
    • (1995) Nat. Med. , vol.1 , pp. 1057-1061
    • Li, Y.M.1    Tan, A.X.2    Vlassara, H.3
  • 17
    • 0001263746 scopus 로고    scopus 로고
    • Molecular identity and distribution of advanced glycation endproducts receptors: Relationship of p60 to OST48 and p90 to 80K-H membrane proteins
    • LI, Y. et al. 1996. Molecular identity and distribution of advanced glycation endproducts receptors: Relationship of p60 to OST48 and p90 to 80K-H membrane proteins. Proc. Natl. Acad. Sci. USA. 93: 11047-11052.
    • (1996) Proc. Natl. Acad. Sci. USA. , vol.93 , pp. 11047-11052
    • Li, Y.1
  • 18
    • 0035918193 scopus 로고    scopus 로고
    • Scavenger receptor class B type I-mediated reverse cholesterol transport is inhibited by advanced glycation end products
    • OHGAMI, N. et al. 2001. Scavenger receptor class B type I-mediated reverse cholesterol transport is inhibited by advanced glycation end products. J. Biol. Chem. 276: 13348-13355.
    • (2001) J. Biol. Chem. , vol.276 , pp. 13348-13355
    • Ohgami, N.1
  • 19
    • 0009770755 scopus 로고    scopus 로고
    • Effect of diabetes and aminoguanidine therapy on renal advanced glycation endproduct binding
    • YOUSSEF, S. et al. 1999. Effect of diabetes and aminoguanidine therapy on renal advanced glycation endproduct binding. Kidney Int. 55: 907-916.
    • (1999) Kidney Int. , vol.55 , pp. 907-916
    • Youssef, S.1
  • 20
    • 0037477342 scopus 로고    scopus 로고
    • The amino terminal domains of ERM proteins bind advanced glycation endproducts: An interaction that may play a role in the development of diabetic complications
    • MCROBERT, E.A. et al. 2003. The amino terminal domains of ERM proteins bind advanced glycation endproducts: an interaction that may play a role in the development of diabetic complications. J. Biol. Chem. 278: 25783-25789.
    • (2003) J. Biol. Chem. , vol.278 , pp. 25783-25789
    • McRobert, E.A.1
  • 21
    • 0033521010 scopus 로고    scopus 로고
    • Cortical actin organization lessons from ERM (ezrin/radixin/moesin) proteins
    • TSUKITA, S. & S. YONEMURA. 1999. Cortical actin organization lessons from ERM (ezrin/radixin/moesin) proteins. J. Biol. Chem. 274: 34507-34510.
    • (1999) J. Biol. Chem. , vol.274 , pp. 34507-34510
    • Tsukita, S.1    Yonemura, S.2
  • 22
    • 0027933858 scopus 로고
    • Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family
    • TURUREN, O., T. WAHLSTROM & A. VAHERI. 1994. Ezrin has a COOH-terminal actin-binding site that is conserved in the ezrin protein family. J. Cell Biol. 126: 1445-1453.
    • (1994) J. Cell Biol. , vol.126 , pp. 1445-1453
    • Tururen, O.1    Wahlstrom, T.2    Vaheri, A.3
  • 23
    • 0029609581 scopus 로고
    • Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ERM association domains
    • BRETSCHER, A., R. GARY & M. BERRYMAN. 1995. Soluble ezrin purified from placenta exists as stable monomers and elongated dimers with masked C-terminal ERM association domains. Biochemistry 34: 16830-16837.
    • (1995) Biochemistry , vol.34 , pp. 16830-16837
    • Bretscher, A.1    Gary, R.2    Berryman, M.3
  • 24
    • 0032583447 scopus 로고    scopus 로고
    • C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical bilayer to the cytoskeleton
    • SIMONS, P. et al. 1998. C-terminal threonine phosphorylation activates ERM proteins to link the cell's cortical bilayer to the cytoskeleton. Biochem. Biophys. Res. Commun. 253: 561-565.
    • (1998) Biochem. Biophys. Res. Commun. , vol.253 , pp. 561-565
    • Simons, P.1
  • 25
    • 0027162182 scopus 로고
    • Ezrin-calpain 1 interactions in gastric parietal cells
    • YAO, X., A. THIBODEAU & J.G. FORTE. 1993. Ezrin-calpain 1 interactions in gastric parietal cells. Am. J. Physiol. 265: C36-C46.
    • (1993) Am. J. Physiol. , vol.265
    • Yao, X.1    Thibodeau, A.2    Forte, J.G.3
  • 26
    • 17944372904 scopus 로고    scopus 로고
    • Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility
    • NG, T. et al. 2001. Ezrin is a downstream effector of trafficking PKC-integrin complexes involved in the control of cell motility. EMBO J. 20: 2723-2741.
    • (2001) EMBO J. , vol.20 , pp. 2723-2741
    • Ng, T.1
  • 27
    • 0028987905 scopus 로고
    • 2-terminal domain inhibits the cell extension activity of the COOH-terminal domain
    • 2-terminal domain inhibits the cell extension activity of the COOH-terminal domain. J. Cell Biol. 128: 1081-1093.
    • (1995) J. Cell Biol. , vol.128 , pp. 1081-1093
    • Martin, M.1
  • 28
    • 0033593481 scopus 로고    scopus 로고
    • Normal development of mice and unimpaired cell adhesion/cell motility/actin-based cytoskeleton without compensatory up-regulation of ezrin or radixin in moesin gene knockout
    • DOI, Y. et al. 1999. Normal development of mice and unimpaired cell adhesion/cell motility/actin-based cytoskeleton without compensatory up-regulation of ezrin or radixin in moesin gene knockout. J. Biol. Chem. 274: 2315-2321.
    • (1999) J. Biol. Chem. , vol.274 , pp. 2315-2321
    • Doi, Y.1
  • 29
    • 0028247080 scopus 로고
    • Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members
    • TAKEUCHI, K. et al. 1994. Perturbation of cell adhesion and microvilli formation by antisense oligonucleotides to ERM family members. J. Cell Biol. 125: 1371-1384.
    • (1994) J. Cell Biol. , vol.125 , pp. 1371-1384
    • Takeuchi, K.1
  • 30
    • 0033542725 scopus 로고    scopus 로고
    • Identification of a 55-kDa ezrin-related protein that induces cytoskeletal changes and localizes to the nucleolus
    • KAUL, S.C. et al. 1999. Identification of a 55-kDa ezrin-related protein that induces cytoskeletal changes and localizes to the nucleolus. Exp. Cell Res. 250: 51-61.
    • (1999) Exp. Cell Res. , vol.250 , pp. 51-61
    • Kaul, S.C.1
  • 31
    • 0032949862 scopus 로고    scopus 로고
    • Disruption of dynamic cell surface architecture of NIH3T3 fibroblasts by the N-terminal domains of moesin and ezrin: In vivo imaging with GFP fusion proteins
    • AMIEVA, M.R. et al. 1999. Disruption of dynamic cell surface architecture of NIH3T3 fibroblasts by the N-terminal domains of moesin and ezrin: in vivo imaging with GFP fusion proteins. J. Cell Sci. 112: 111-125.
    • (1999) J. Cell Sci. , vol.112 , pp. 111-125
    • Amieva, M.R.1
  • 32
    • 0034918560 scopus 로고    scopus 로고
    • The glomerular epithelial cell anti-adhesion podocalyxin associates with the actin cytoskeleton through interactions with ezrin
    • ORLANDO, R.A. et al. 2001. The glomerular epithelial cell anti-adhesion podocalyxin associates with the actin cytoskeleton through interactions with ezrin. J. Am. Soc. Nephrol. 12: 1589-1598.
    • (2001) J. Am. Soc. Nephrol. , vol.12 , pp. 1589-1598
    • Orlando, R.A.1
  • 33
    • 0034126357 scopus 로고    scopus 로고
    • Getting a foothold in nephrotic syndrome
    • SOMLO, S. & P. MUNDEL. 2000. Getting a foothold in nephrotic syndrome. Nat. Genet. 24: 333-335.
    • (2000) Nat. Genet. , vol.24 , pp. 333-335
    • Somlo, S.1    Mundel, P.2
  • 34
    • 0034954343 scopus 로고    scopus 로고
    • Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton
    • TAKEDA, T. et al. 2001. Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton. J. Clin. Invest. 108: 289-301.
    • (2001) J. Clin. Invest. , vol.108 , pp. 289-301
    • Takeda, T.1
  • 35
    • 0034945789 scopus 로고    scopus 로고
    • Podocyte foot process broadening in experimental diabetic nephropathy: Amelioration with renin-angiotensin blockade
    • MIFSUD, S.A. et al. 2001. Podocyte foot process broadening in experimental diabetic nephropathy: amelioration with renin-angiotensin blockade. Diabetologia 44: 878-882.
    • (2001) Diabetologia , vol.44 , pp. 878-882
    • Mifsud, S.A.1
  • 36
    • 0030659415 scopus 로고    scopus 로고
    • A quantitative immunofluorescence study of glomerular cell adhesion proteins in proteinuric states
    • BAINS, R., P.N. FURNESS & D.R. CRITCHLEY. 1997. A quantitative immunofluorescence study of glomerular cell adhesion proteins in proteinuric states. J. Pathol. 183: 272-280.
    • (1997) J. Pathol. , vol.183 , pp. 272-280
    • Bains, R.1    Furness, P.N.2    Critchley, D.R.3
  • 37
    • 0033667398 scopus 로고    scopus 로고
    • F-actin fiber distribution in glomerular cells: Structural and functional implications
    • CORTES, P. et al. 2000. F-actin fiber distribution in glomerular cells: structural and functional implications. Kidney Int. 58: 2452-2461.
    • (2000) Kidney Int. , vol.58 , pp. 2452-2461
    • Cortes, P.1
  • 38
    • 0029088469 scopus 로고
    • High glucose alters actin assembly in glomerular mesangial and epithelial cells
    • ZHOU, X. et al. 1995. High glucose alters actin assembly in glomerular mesangial and epithelial cells. Lab. Invest. 73: 372-383.
    • (1995) Lab. Invest. , vol.73 , pp. 372-383
    • Zhou, X.1
  • 39
    • 0026640556 scopus 로고
    • Corneal endothelial cytoskeletal changes in F-actin with aging, diabetes and after cytochalasin exposure
    • KlM, E.K. et al. 1992. Corneal endothelial cytoskeletal changes in F-actin with aging, diabetes and after cytochalasin exposure. Am. J. Ophthalmol. 114: 329-335.
    • (1992) Am. J. Ophthalmol. , vol.114 , pp. 329-335
    • Klm, E.K.1
  • 40
    • 0030763919 scopus 로고    scopus 로고
    • Ezrin is an effector of HGF-mediated migration and morphogenesis in epithelial cells
    • CREPALDI, T. et al. 1997. Ezrin is an effector of HGF-mediated migration and morphogenesis in epithelial cells. J. Cell Biol. 138: 423-434.
    • (1997) J. Cell Biol. , vol.138 , pp. 423-434
    • Crepaldi, T.1
  • 41
    • 0029084127 scopus 로고
    • Dephosphorylation of ezrin as an early event in renal microvillar breakdown and anoxic injury
    • CHEN, J., J.A. COHN & L.J. MANDEL. 1995. Dephosphorylation of ezrin as an early event in renal microvillar breakdown and anoxic injury. Proc. Natl. Acad. Sci. USA 92: 7495-7499.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 7495-7499
    • Chen, J.1    Cohn, J.A.2    Mandel, L.J.3
  • 42
    • 0035892765 scopus 로고    scopus 로고
    • Ovarian epithelial carcinoma tyrosine phosphorylation, cell proliferation, and ezrin translocation are stimulated by IL-1 alpha and EGF
    • CHEN, Z. et al. 2001. Ovarian epithelial carcinoma tyrosine phosphorylation, cell proliferation, and ezrin translocation are stimulated by IL-1 alpha and EGF. Cancer 92: 3068-3075.
    • (2001) Cancer , vol.92 , pp. 3068-3075
    • Chen, Z.1


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