메뉴 건너뛰기




Volumn 183, Issue 3, 1997, Pages 272-280

A quantitative immunofluorescence study of glomerular cell adhesion proteins in proteinuric states

Author keywords

Adhesion; Cadherin; Catenin; FAK; Foot processes; Glomerulus; Integrin; Paxillin; Phosphotyrosine; Podocytes; Pp130CAS; Proteinuria; Talin; Vinculin

Indexed keywords

CADHERIN; CATENIN; CELL ADHESION MOLECULE; INTEGRIN; PHOSPHOTYROSINE; TALIN; VINCULIN;

EID: 0030659415     PISSN: 00223417     EISSN: None     Source Type: Journal    
DOI: 10.1002/(SICI)1096-9896(199711)183:3<272::AID-PATH914>3.0.CO;2-U     Document Type: Article
Times cited : (44)

References (47)
  • 1
    • 0024819933 scopus 로고
    • Glomerular epithelial detachment, not reduced charge density, correlates with proteinuria in adriamycin and puromycin nephrosis
    • Whiteside C, Prutis K, Cameron R, Thompson J. Glomerular epithelial detachment, not reduced charge density, correlates with proteinuria in adriamycin and puromycin nephrosis. Lab Invest 1989; 61: 650-660.
    • (1989) Lab Invest , vol.61 , pp. 650-660
    • Whiteside, C.1    Prutis, K.2    Cameron, R.3    Thompson, J.4
  • 2
    • 0027742857 scopus 로고
    • Podocytic cytoskeletal disaggregation and basement-membrane detachment in puromycin aminonucleoside nephrosis
    • Whiteside CI, Cameron R, Munk S, Levy J. Podocytic cytoskeletal disaggregation and basement-membrane detachment in puromycin aminonucleoside nephrosis. Am J Pathol 1993; 142: 1641-1653.
    • (1993) Am J Pathol , vol.142 , pp. 1641-1653
    • Whiteside, C.I.1    Cameron, R.2    Munk, S.3    Levy, J.4
  • 3
    • 0027511359 scopus 로고
    • Visceral glomerular epithelial cells can proliferate in vivo and synthesize platelet-derived growth factor B-chain
    • Floege J, Johnson RJ, Alpers CE, et al. Visceral glomerular epithelial cells can proliferate in vivo and synthesize platelet-derived growth factor B-chain. Am J Pathol 1993; 142: 637-650.
    • (1993) Am J Pathol , vol.142 , pp. 637-650
    • Floege, J.1    Johnson, R.J.2    Alpers, C.E.3
  • 4
    • 0029809045 scopus 로고    scopus 로고
    • Structural continuity of filtration slit (slit diaphragm) to plasma membrane of podocyte
    • Fujigaki Y, Morioka T, Matsui K, et al. Structural continuity of filtration slit (slit diaphragm) to plasma membrane of podocyte. Kidney Int 1996; 50: 54-62.
    • (1996) Kidney Int , vol.50 , pp. 54-62
    • Fujigaki, Y.1    Morioka, T.2    Matsui, K.3
  • 5
    • 0028107686 scopus 로고
    • The immunolocalisation and urinary quantitation of 7-5Q/A, a unique human renal antigen
    • Kittelberger R, Kerjaschki D, Neale T. The immunolocalisation and urinary quantitation of 7-5Q/A, a unique human renal antigen. Clin Nephrol 1994; 2: 72-82.
    • (1994) Clin Nephrol , vol.2 , pp. 72-82
    • Kittelberger, R.1    Kerjaschki, D.2    Neale, T.3
  • 6
    • 0027414695 scopus 로고
    • Two classes of tight junctions are revealed by ZO-1 isoforms
    • Balda MS, Anderson JM. Two classes of tight junctions are revealed by ZO-1 isoforms. Am J Physiol 1993; 264: C918-C924.
    • (1993) Am J Physiol , vol.264
    • Balda, M.S.1    Anderson, J.M.2
  • 8
    • 0026345292 scopus 로고
    • Identification of 160-kDa polypeptide that binds to the tight junction protein ZO-1
    • Gumbiner B, Lowenkopf T, Apatira D. Identification of 160-kDa polypeptide that binds to the tight junction protein ZO-1. Proc Natl Acad Sci USA 1991; 80: 3460-3464.
    • (1991) Proc Natl Acad Sci USA , vol.80 , pp. 3460-3464
    • Gumbiner, B.1    Lowenkopf, T.2    Apatira, D.3
  • 9
    • 0027744129 scopus 로고
    • Occludin: A novel integral membrane protein localizing at tight junctions
    • Furuse M, Hirase T, Itoh M, et al. Occludin: a novel integral membrane protein localizing at tight junctions. J Cell Biol 1993; 123: 1777-1788.
    • (1993) J Cell Biol , vol.123 , pp. 1777-1788
    • Furuse, M.1    Hirase, T.2    Itoh, M.3
  • 10
    • 0027393734 scopus 로고
    • Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2
    • Zhong Y, Saitoh T, Minase T, et al. Monoclonal antibody 7H6 reacts with a novel tight junction-associated protein distinct from ZO-1, cingulin and ZO-2. J Cell Biol 1993; 120: 477-483.
    • (1993) J Cell Biol , vol.120 , pp. 477-483
    • Zhong, Y.1    Saitoh, T.2    Minase, T.3
  • 11
    • 0026729987 scopus 로고
    • The altered glomerular filtration slits seen in puromycin aminonucleoside nephrosis and protamine sulfate-treated rats contain the tight junction protein ZO-1
    • Kurihara H, Anderson JM, Kerjaschki D, Farquhar MG. The altered glomerular filtration slits seen in puromycin aminonucleoside nephrosis and protamine sulfate-treated rats contain the tight junction protein ZO-1. Am J Pathol 1992; 141: 805-816.
    • (1992) Am J Pathol , vol.141 , pp. 805-816
    • Kurihara, H.1    Anderson, J.M.2    Kerjaschki, D.3    Farquhar, M.G.4
  • 12
    • 0026757674 scopus 로고
    • Characterization of glomerular epithelial cell matrix receptors
    • Adler S. Characterization of glomerular epithelial cell matrix receptors. Am J Pathol 1992; 141: 571-578.
    • (1992) Am J Pathol , vol.141 , pp. 571-578
    • Adler, S.1
  • 13
    • 0026497661 scopus 로고
    • Cytoskeletal-plasma membrane interactions
    • Luna EJ, Hitt AL. Cytoskeletal-plasma membrane interactions. Science 1992; 258: 955-964.
    • (1992) Science , vol.258 , pp. 955-964
    • Luna, E.J.1    Hitt, A.L.2
  • 14
    • 0026705661 scopus 로고
    • Suppression of tumorigenicity in transformed cells after transfection with vinculin cDNA
    • Rodriguez-Fernandez JL, Geiger B, Salomon D, et al. Suppression of tumorigenicity in transformed cells after transfection with vinculin cDNA. J Cell Biol 1992; 119: 427-438.
    • (1992) J Cell Biol , vol.119 , pp. 427-438
    • Rodriguez-Fernandez, J.L.1    Geiger, B.2    Salomon, D.3
  • 16
    • 0028306464 scopus 로고
    • Lysophosphatidic acid stimulates tyrosine phosphorylation of focal adhesion kinase, paxillin, and p 130. Signalling pathways and cross-talk with platelet-derived growth factor
    • Seufferlein T, Rozengurt E. Lysophosphatidic acid stimulates tyrosine phosphorylation of focal adhesion kinase, paxillin, and p 130. Signalling pathways and cross-talk with platelet-derived growth factor. J Biol Chem 1994; 269: 9345-9351.
    • (1994) J Biol Chem , vol.269 , pp. 9345-9351
    • Seufferlein, T.1    Rozengurt, E.2
  • 17
    • 0028986116 scopus 로고
    • pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high affinity binding site for Crk
    • Schaller M, Parsons J. pp125FAK-dependent tyrosine phosphorylation of paxillin creates a high affinity binding site for Crk. Mol Cell Biol 1995; 5: 2635-2645.
    • (1995) Mol Cell Biol , vol.5 , pp. 2635-2645
    • Schaller, M.1    Parsons, J.2
  • 18
    • 0026445719 scopus 로고
    • Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • Burridge K, Turner CE, Romer LH. Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: a role in cytoskeletal assembly. J Cell Biol 1992; 119: 893-903.
    • (1992) J Cell Biol , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 19
    • 0028940658 scopus 로고
    • Adhesion-induced tyrosine phosphorylation of the p130SRC substrate
    • Petch L, Bockholt S, Boulton A, Parsons J, Burridge K. Adhesion-induced tyrosine phosphorylation of the p130SRC substrate. J Cell Sci 1995; 108: 1371-1379.
    • (1995) J Cell Sci , vol.108 , pp. 1371-1379
    • Petch, L.1    Bockholt, S.2    Boulton, A.3    Parsons, J.4    Burridge, K.5
  • 20
    • 0029034873 scopus 로고
    • Integrin-mediated cell adhesion promotes tyrosine phosphorylation of p130(CAS). An SRC homology 3-containing molecule having multiple SRC homology-2 binding motifs
    • Nojima Y, Morino N, Mimura T, et al. Integrin-mediated cell adhesion promotes tyrosine phosphorylation of p130(CAS). an SRC homology 3-containing molecule having multiple SRC homology-2 binding motifs. J Biol Chem 1995; 270: 15398-15402.
    • (1995) J Biol Chem , vol.270 , pp. 15398-15402
    • Nojima, Y.1    Morino, N.2    Mimura, T.3
  • 21
    • 0028236960 scopus 로고
    • The RhoA-dependent assembly of focal adhesions in Swiss 3T3 cells is associated with increased tyrosine phosphorylation and recruitment of both pp125FAK and protein kinase C-δ to focal adhesions
    • Barry S, Critchley DR. The RhoA-dependent assembly of focal adhesions in Swiss 3T3 cells is associated with increased tyrosine phosphorylation and recruitment of both pp125FAK and protein kinase C-δ to focal adhesions. J Cell Sci 1994; 107: 2033-2045.
    • (1994) J Cell Sci , vol.107 , pp. 2033-2045
    • Barry, S.1    Critchley, D.R.2
  • 22
    • 0030585376 scopus 로고    scopus 로고
    • Src kinase plays an essential role in integrin mediated tyrosine phosphorylation of Crc-associated substate p130(Cas)
    • Hamasaki K, Mimura T, Morino N, et al. Src kinase plays an essential role in integrin mediated tyrosine phosphorylation of Crc-associated substate p130(Cas) Biochem Biophys Res Commun 1996; 222: 338-343.
    • (1996) Biochem Biophys Res Commun , vol.222 , pp. 338-343
    • Hamasaki, K.1    Mimura, T.2    Morino, N.3
  • 23
    • 0029120440 scopus 로고
    • Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice
    • Illc D, Furuta Y, Kanazawa S, et al. Reduced cell motility and enhanced focal adhesion contact formation in cells from FAK-deficient mice. Nature 1995; 377: 539-544.
    • (1995) Nature , vol.377 , pp. 539-544
    • Illc, D.1    Furuta, Y.2    Kanazawa, S.3
  • 24
    • 0027242121 scopus 로고
    • Tyrosine phosphorylation and cytoskeletal reorganization in platelets are triggered by interaction of integrin receptors with their immobilized ligands
    • Haimovich B, Lipfert L, Brugge JS, Shattil SJ. Tyrosine phosphorylation and cytoskeletal reorganization in platelets are triggered by interaction of integrin receptors with their immobilized ligands. J Biol Chem 1993; 268: 15868-15877.
    • (1993) J Biol Chem , vol.268 , pp. 15868-15877
    • Haimovich, B.1    Lipfert, L.2    Brugge, J.S.3    Shattil, S.J.4
  • 25
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark E, Brugge J. Integrins and signal transduction pathways: the road taken. Science 1995; 268: 233-239.
    • (1995) Science , vol.268 , pp. 233-239
    • Clark, E.1    Brugge, J.2
  • 26
    • 0029135105 scopus 로고
    • Cell-matrix adhesion: Structure and regulation
    • Hemmings L, Barry S, Critchley D. Cell-matrix adhesion: structure and regulation. Biochem Soc Trans 1995; 23: 617-623.
    • (1995) Biochem Soc Trans , vol.23 , pp. 617-623
    • Hemmings, L.1    Barry, S.2    Critchley, D.3
  • 27
    • 0026772018 scopus 로고
    • Hormonal regulation of paracellular permeability in isolated rat hepatocyte couplets
    • Nathanson MH, Gautam A, Ng OC, Bruck R, Boyer JL. Hormonal regulation of paracellular permeability in isolated rat hepatocyte couplets. Am J Physiol 1992; 262: G1079-G1086.
    • (1992) Am J Physiol , vol.262
    • Nathanson, M.H.1    Gautam, A.2    Ng, O.C.3    Bruck, R.4    Boyer, J.L.5
  • 28
    • 0028931103 scopus 로고
    • Evidence that tyrosine phosphorylation may increase tight junction permeability
    • Staddon J, Herrenknecht K, Smales C, Rubin L. Evidence that tyrosine phosphorylation may increase tight junction permeability. J Cell Sci 1995; 108: 609-619.
    • (1995) J Cell Sci , vol.108 , pp. 609-619
    • Staddon, J.1    Herrenknecht, K.2    Smales, C.3    Rubin, L.4
  • 29
    • 0029002719 scopus 로고
    • Distribution of extracellular matrix receptors in various forms of glomerulonephritis
    • Shikata K, Makino H, Morioka S, et al. Distribution of extracellular matrix receptors in various forms of glomerulonephritis. Am J Kidney Dis 1995; 25: 680-688.
    • (1995) Am J Kidney Dis , vol.25 , pp. 680-688
    • Shikata, K.1    Makino, H.2    Morioka, S.3
  • 30
    • 0028831889 scopus 로고
    • Podocytes lose their adhesive phenotype in focal segmental glomerulosclerosis
    • Kemeny E, Mihatsch M, Durmuller U, Gudat F. Podocytes lose their adhesive phenotype in focal segmental glomerulosclerosis. Clin Nephrol 1995; 2: 71-83.
    • (1995) Clin Nephrol , vol.2 , pp. 71-83
    • Kemeny, E.1    Mihatsch, M.2    Durmuller, U.3    Gudat, F.4
  • 31
    • 0026476115 scopus 로고
    • Very late activation-3 integrin is the dominant beta 1-integrin on the glomerular capillary wall: An immunofluorescence study in nephrotic syndrome
    • Baraldi A, Furci L, Zambruno G, et al. Very late activation-3 integrin is the dominant beta 1-integrin on the glomerular capillary wall: an immunofluorescence study in nephrotic syndrome. Nephron 1992; 62: 382-388.
    • (1992) Nephron , vol.62 , pp. 382-388
    • Baraldi, A.1    Furci, L.2    Zambruno, G.3
  • 32
    • 0001402991 scopus 로고
    • Patterns of membranous nephropathy
    • Ehrenreich T, Churg J. Patterns of membranous nephropathy. Path Annual 1968; 3: 145-186.
    • (1968) Path Annual , vol.3 , pp. 145-186
    • Ehrenreich, T.1    Churg, J.2
  • 33
    • 0028120461 scopus 로고
    • Modulation of cytoskeletal organization of podocytes during the course of aminonucleoside nephrosis in rats
    • Kubosawa H, Kondo Y. Modulation of cytoskeletal organization of podocytes during the course of aminonucleoside nephrosis in rats. Path Int 1994; 8: 578-586.
    • (1994) Path Int , vol.8 , pp. 578-586
    • Kubosawa, H.1    Kondo, Y.2
  • 34
    • 0027972232 scopus 로고
    • Puromycin aminonucleoside and adriamycin disturb cytoskeletal and extracellular matrix protein organization, but not protein synthesis of cultured glomerular epithelial cells
    • Coers W, Huitema S, van-der-Horst M, Weening J. Puromycin aminonucleoside and adriamycin disturb cytoskeletal and extracellular matrix protein organization, but not protein synthesis of cultured glomerular epithelial cells. Exp Nephrol 1994; 1: 40-50.
    • (1994) Exp Nephrol , vol.1 , pp. 40-50
    • Coers, W.1    Huitema, S.2    Van-der-Horst, M.3    Weening, J.4
  • 35
    • 0027732572 scopus 로고
    • Temporal expression of VLA-2 and modulation of its ligand specificity by rat glomerular epithelial cells in vitro
    • Mendrick DL, Kelly DM. Temporal expression of VLA-2 and modulation of its ligand specificity by rat glomerular epithelial cells in vitro. Lab Invest 1993; 69: 690-702.
    • (1993) Lab Invest , vol.69 , pp. 690-702
    • Mendrick, D.L.1    Kelly, D.M.2
  • 36
    • 0028069635 scopus 로고
    • Glomerular cells in virto versus the glomerulus in vivo
    • Floege J, Radeke HR, Johnson RJ. Glomerular cells in virto versus the glomerulus in vivo. Kidney Int 1994; 45: 360-368.
    • (1994) Kidney Int , vol.45 , pp. 360-368
    • Floege, J.1    Radeke, H.R.2    Johnson, R.J.3
  • 37
    • 0029026697 scopus 로고
    • Convergent signalling in the action of integrins, neuropeptides, growth factors and oncogenes
    • Rozengurt E. Convergent signalling in the action of integrins, neuropeptides, growth factors and oncogenes. Cancer Sirv 1995; 24: 81-96.
    • (1995) Cancer Sirv , vol.24 , pp. 81-96
    • Rozengurt, E.1
  • 38
    • 0028889436 scopus 로고
    • Interaction between focal adhesion kinase and Crk-assocrated tyrosine kinase substrate p130(Cas)
    • Polte T, Hanks S. Interaction between focal adhesion kinase and Crk-assocrated tyrosine kinase substrate p130(Cas). Proc Natl Acad Sci USA 1995; 92: 10678-10682.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 10678-10682
    • Polte, T.1    Hanks, S.2
  • 39
    • 0029666251 scopus 로고    scopus 로고
    • p130(Cas), a substrate associated with v-Src and v-Crk, localises to focal adhesions and binds to focal adhesion kinase
    • Harte M, Hildebrand J, Burnham M, Boulton A, Parsons J. p130(Cas), a substrate associated with v-Src and v-Crk, localises to focal adhesions and binds to focal adhesion kinase. J Biol Chem 1996; 271: 13649-13665.
    • (1996) J Biol Chem , vol.271 , pp. 13649-13665
    • Harte, M.1    Hildebrand, J.2    Burnham, M.3    Boulton, A.4    Parsons, J.5
  • 40
    • 0029665446 scopus 로고    scopus 로고
    • The identification of p130(Cas)-binding proteins and their role in cellular transformation
    • Burnham M, Harte M, Richardson A, Parsons J, Boulton A. The identification of p130(Cas)-binding proteins and their role in cellular transformation. Oncogene 1996; 12: 2467-2472.
    • (1996) Oncogene , vol.12 , pp. 2467-2472
    • Burnham, M.1    Harte, M.2    Richardson, A.3    Parsons, J.4    Boulton, A.5
  • 41
    • 0029948080 scopus 로고    scopus 로고
    • Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn
    • Cary L, Chang J, Guan J. Stimulation of cell migration by overexpression of focal adhesion kinase and its association with Src and Fyn. J Cell Sci 1996; 109: 1787-1794.
    • (1996) J Cell Sci , vol.109 , pp. 1787-1794
    • Cary, L.1    Chang, J.2    Guan, J.3
  • 42
    • 0028953668 scopus 로고
    • Increased tyrosine phosphorylation during modification of tight junctions between glomerular foot processes
    • Kurihara H, Anderson J, Farquhar M. Increased tyrosine phosphorylation during modification of tight junctions between glomerular foot processes. Am J Physiol 1995; 3(Part 2): F514-F524.
    • (1995) Am J Physiol , vol.3 , Issue.2 PART
    • Kurihara, H.1    Anderson, J.2    Farquhar, M.3
  • 43
    • 0015953201 scopus 로고
    • Porous substructure of the glomerular slit diaphragm in the rat and the mouse
    • Rodewald R, Karnovsky MJ. Porous substructure of the glomerular slit diaphragm in the rat and the mouse. J Cell Biol 1974; 60: 423-433.
    • (1974) J Cell Biol , vol.60 , pp. 423-433
    • Rodewald, R.1    Karnovsky, M.J.2
  • 44
    • 0016686024 scopus 로고
    • A stereological study of the glomerular filter in the rat. Morphometry of the slit diaphragm and basement membrane
    • Shea SM, Morrison AB. A stereological study of the glomerular filter in the rat. Morphometry of the slit diaphragm and basement membrane. J Cell Biol 1975; 67: 436-443.
    • (1975) J Cell Biol , vol.67 , pp. 436-443
    • Shea, S.M.1    Morrison, A.B.2
  • 45
    • 0029824927 scopus 로고    scopus 로고
    • Re-evaluation of foot process effacement in acute puromycin aminonucleoside nephrosis
    • Inokuchi S, Shirato I, Kobayashi N, et al Re-evaluation of foot process effacement in acute puromycin aminonucleoside nephrosis. Kidney Int 1996; 50: 1278-1287.
    • (1996) Kidney Int , vol.50 , pp. 1278-1287
    • Inokuchi, S.1    Shirato, I.2    Kobayashi, N.3
  • 46
    • 0028066825 scopus 로고
    • Structural basis for reduced filtration capacity in nephrotic humans
    • Drumond M, Kristal B, Myers B, Deen W. Structural basis for reduced filtration capacity in nephrotic humans. J Clin Invest 1994; 94: 1187-1194.
    • (1994) J Clin Invest , vol.94 , pp. 1187-1194
    • Drumond, M.1    Kristal, B.2    Myers, B.3    Deen, W.4
  • 47
    • 0028334836 scopus 로고
    • Spatiotemporal expression of molecules associated with junctional complexes during the in vivo maturation of renal podocytes
    • Tassin M, Beziau A, Gubler M, Boyer B. Spatiotemporal expression of molecules associated with junctional complexes during the in vivo maturation of renal podocytes. Int J Dev Biol 1994; 1: 45-54.
    • (1994) Int J Dev Biol , vol.1 , pp. 45-54
    • Tassin, M.1    Beziau, A.2    Gubler, M.3    Boyer, B.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.