메뉴 건너뛰기




Volumn 10, Issue 2, 2005, Pages 157-166

New insights into the molecular biology of the glomerular filtration barrier and associated disease

Author keywords

Endothelial cells; Glomerular basement membrane; Molecular biology; Podocytes; Proteinuria

Indexed keywords

ANATOMY; CHEMISTRY; ELECTRON MICROSCOPY; ENDOTHELIUM CELL; FATALITY; GLOMERULOPATHY; GLOMERULUS BASEMENT MEMBRANE; GLOMERULUS EPITHELIUM; GLOMERULUS FILTRATION; HUMAN; KIDNEY; MEDICAL GENETICS; MOLECULAR BIOLOGY; PODOCYTE; PRIORITY JOURNAL; PROTEINURIA; REVIEW;

EID: 20144376222     PISSN: 13205358     EISSN: None     Source Type: Journal    
DOI: 10.1111/j.1440-1797.2005.00385.x     Document Type: Review
Times cited : (27)

References (94)
  • 2
    • 0025908973 scopus 로고
    • Current status of the structural and functional basis of glomerular nitration and proteinuria
    • Kanwar YS, Liu ZZ, Kashihara N, Wallner EI. Current status of the structural and functional basis of glomerular nitration and proteinuria. Semin. Nephrol. 1991; 11: 390-413.
    • (1991) Semin. Nephrol. , vol.11 , pp. 390-413
    • Kanwar, Y.S.1    Liu, Z.Z.2    Kashihara, N.3    Wallner, E.I.4
  • 3
    • 0014138463 scopus 로고
    • Electron microscopic studies of normal glomerular basement membrane
    • Jorgensen F. Electron microscopic studies of normal glomerular basement membrane. Lab. Invest. 1967; 17: 416-24.
    • (1967) Lab. Invest. , vol.17 , pp. 416-424
    • Jorgensen, F.1
  • 4
    • 0014117562 scopus 로고
    • Electron microscopic studies of normal visceral epithelial cells
    • Jorgensen F. Electron microscopic studies of normal visceral epithelial cells. Lab. Invest. 1967b; 17: 225-42.
    • (1967) Lab. Invest. , vol.17 , pp. 225-242
    • Jorgensen, F.1
  • 5
    • 0014231725 scopus 로고
    • The ultastructure of the normal human glomerulus. Thickness of glomerular basement membrane
    • Jorgensen F, Bentzon MW. The ultastructure of the normal human glomerulus. Thickness of glomerular basement membrane. Lab. Invest. 1968; 18: 42-8.
    • (1968) Lab. Invest. , vol.18 , pp. 42-48
    • Jorgensen, F.1    Bentzon, M.W.2
  • 7
    • 0025001684 scopus 로고
    • Monoclonal antibodies against membrane proteins of the rat glomerulus. Immunochemical specificity and immunofluorescence distribution of the antigens
    • Miettinen A, Dekan G, Farquhar MG. Monoclonal antibodies against membrane proteins of the rat glomerulus. Immunochemical specificity and immunofluorescence distribution of the antigens. Am. J. Pathol. 1990; 137: 929-44.
    • (1990) Am. J. Pathol. , vol.137 , pp. 929-944
    • Miettinen, A.1    Dekan, G.2    Farquhar, M.G.3
  • 8
    • 0029127384 scopus 로고
    • The renal glomerulus of mice lacking s-laminin/laminin beta 2: Nephrosis despite molecular compensation by laminin beta 1
    • Noakes PG, Miner JH, Gautam M, Cunningham JM, Sanes JR, Merlie JP. The renal glomerulus of mice lacking s-laminin/laminin beta 2: nephrosis despite molecular compensation by laminin beta 1. Nat. Genet. 1995; 10: 400-6.
    • (1995) Nat. Genet. , vol.10 , pp. 400-406
    • Noakes, P.G.1    Miner, J.H.2    Gautam, M.3    Cunningham, J.M.4    Sanes, J.R.5    Merlie, J.P.6
  • 9
    • 0028802644 scopus 로고
    • Comparative distribution alphal(IV), alpha5(IV), and alpha6(IV) collagen chains in normal human adult and fetal tissues and in kidneys from X-linked Alport syndrome patients
    • Peissel B, Geng L, Kalluri R et al. Comparative distribution alphal(IV), alpha5(IV), and alpha6(IV) collagen chains in normal human adult and fetal tissues and in kidneys from X-linked Alport syndrome patients. J. Clin. Invest. 1995; 96: 1948-57.
    • (1995) J. Clin. Invest. , vol.96 , pp. 1948-1957
    • Peissel, B.1    Geng, L.2    Kalluri, R.3
  • 10
    • 0028168648 scopus 로고
    • Identification of mutations in the alpha3(IV) and alpha4(IV) collagen genes in autosomal recessive Alport syndrome
    • Mochizuki T, Lemmink HH, Mariyama M et al. Identification of mutations in the alpha3(IV) and alpha4(IV) collagen genes in autosomal recessive Alport syndrome. Nat. Genet. 1994; 8: 77-81.
    • (1994) Nat. Genet. , vol.8 , pp. 77-81
    • Mochizuki, T.1    Lemmink, H.H.2    Mariyama, M.3
  • 11
    • 0032823921 scopus 로고    scopus 로고
    • Alport syndrome. An inherited disorder of renal, ocular, and cochlear basement membranes
    • Kashtan CE. Alport syndrome. An inherited disorder of renal, ocular, and cochlear basement membranes. Medicine (Baltimore) 1999; 78: 338-60.
    • (1999) Medicine (Baltimore) , vol.78 , pp. 338-360
    • Kashtan, C.E.1
  • 12
    • 0031000529 scopus 로고    scopus 로고
    • Isoform switching of type IV collagen is developmentally arrested in X-linked Alport syndrome leading to increased susceptibility of renal basement membranes to endoproteolysis
    • Kalluri R, Shield CF, Todd P, Hudson BG, Neilson EG. Isoform switching of type IV collagen is developmentally arrested in X-linked Alport syndrome leading to increased susceptibility of renal basement membranes to endoproteolysis. J. Clin. Invest. 1997; 99: 2470-78.
    • (1997) J. Clin. Invest. , vol.99 , pp. 2470-2478
    • Kalluri, R.1    Shield, C.F.2    Todd, P.3    Hudson, B.G.4    Neilson, E.G.5
  • 13
    • 0024462827 scopus 로고
    • Goodpasture syndrome: Molecular architecture and function of basement membrane antigen
    • Hudson BG, Wieslander J, Wisdom BJ Jr, Noelken ME. Goodpasture syndrome: molecular architecture and function of basement membrane antigen. Lab. Invest. 1989; 61: 256-69.
    • (1989) Lab. Invest. , vol.61 , pp. 256-269
    • Hudson, B.G.1    Wieslander, J.2    Wisdom Jr., B.J.3    Noelken, M.E.4
  • 14
    • 11944275329 scopus 로고
    • The pathogenesis of Alport syndrome involves type IV collagen molecules containing the alpha 3 (IV) chain: Evidence from anti-GBM nephritis after renal transplantation
    • Hudson BG, Kalluri R, Gunwar S et al. The pathogenesis of Alport syndrome involves type IV collagen molecules containing the alpha 3 (IV) chain: evidence from anti-GBM nephritis after renal transplantation. Kidney Int. 1992; 42: 179-87.
    • (1992) Kidney Int. , vol.42 , pp. 179-187
    • Hudson, B.G.1    Kalluri, R.2    Gunwar, S.3
  • 15
    • 3042810092 scopus 로고    scopus 로고
    • DDR 1-deficient mice show localized subepithelial GBM thickening with focal loss of slit diaphragms and proteinuria
    • Gross O, Beirowski B, Harvey SJ et al. DDR 1-deficient mice show localized subepithelial GBM thickening with focal loss of slit diaphragms and proteinuria. Kidney Int. 2004; 66: 102-11.
    • (2004) Kidney Int. , vol.66 , pp. 102-111
    • Gross, O.1    Beirowski, B.2    Harvey, S.J.3
  • 16
    • 0025076791 scopus 로고
    • The alpha 1-alpha 6 subunits of integrins are characteristically expressed in distinct segments of developing and adult human nephron
    • Korhonen M, Ylanne J, Laitinen L, Virtanen I. The alpha 1-alpha 6 subunits of integrins are characteristically expressed in distinct segments of developing and adult human nephron. J. Cell Biol. 1990; 111: 1245-54.
    • (1990) J. Cell Biol. , vol.111 , pp. 1245-1254
    • Korhonen, M.1    Ylanne, J.2    Laitinen, L.3    Virtanen, I.4
  • 17
    • 0029855437 scopus 로고    scopus 로고
    • Alpha 3 beta 1 integrin has a crucial role in kidney and lung organogenesis
    • Kreidberg JA, Donovan MJ, Goldstein SL et al. Alpha 3 beta 1 integrin has a crucial role in kidney and lung organogenesis. Development 1996; 122: 3537-47.
    • (1996) Development , vol.122 , pp. 3537-3547
    • Kreidberg, J.A.1    Donovan, M.J.2    Goldstein, S.L.3
  • 18
    • 0028982596 scopus 로고
    • Beta 1 and beta 3 integrin upregulation in rapidly progressive glomerulonephritis
    • Bataldi A, Zambruno G, Furci L et al. Beta 1 and beta 3 integrin upregulation in rapidly progressive glomerulonephritis. Nephrol. Dial. Transplant. 1995; 10: 1155-61.
    • (1995) Nephrol. Dial. Transplant. , vol.10 , pp. 1155-1161
    • Bataldi, A.1    Zambruno, G.2    Furci, L.3
  • 19
    • 20144379752 scopus 로고    scopus 로고
    • Podocyte migration during nephrotic syndrome requires a coordinated interplay between cathepsin L and alpha3 integrin
    • Reiser J, Oh J, Shirato I et al. Podocyte migration during nephrotic syndrome requires a coordinated interplay between cathepsin L and alpha3 integrin. J. Biol. Chem. 2004; 13: 34 827-32.
    • (2004) J. Biol. Chem. , vol.13
    • Reiser, J.1    Oh, J.2    Shirato, I.3
  • 20
    • 0027286695 scopus 로고
    • A single EGF-like motif of laminin is responsible for high affinity nidogen binding
    • Mayer U, Nischt R, Poschl E et al. A single EGF-like motif of laminin is responsible for high affinity nidogen binding. EMBO J. 1993; 12: 1879-85.
    • (1993) EMBO J. , vol.12 , pp. 1879-1885
    • Mayer, U.1    Nischt, R.2    Poschl, E.3
  • 21
    • 0024460533 scopus 로고
    • Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV
    • Aumailley M, Wiedemann H, Mann K, Timpl R. Binding of nidogen and the laminin-nidogen complex to basement membrane collagen type IV. Eur. J. Biochem. 1989; 184: 241-8.
    • (1989) Eur. J. Biochem. , vol.184 , pp. 241-248
    • Aumailley, M.1    Wiedemann, H.2    Mann, K.3    Timpl, R.4
  • 22
    • 0032815533 scopus 로고    scopus 로고
    • Recent insights into the structure and functions of heparan sulfate proteoglycans in the human glomerular basement membrane
    • Groffen AJ, Veerkamp JH, Monnens LA, van den Heuvel LP. Recent insights into the structure and functions of heparan sulfate proteoglycans in the human glomerular basement membrane. Nephrol. Dial. Transplant. 1999; 14: 2119-29.
    • (1999) Nephrol. Dial. Transplant. , vol.14 , pp. 2119-2129
    • Groffen, A.J.1    Veerkamp, J.H.2    Monnens, L.A.3    Van Den Heuvel, L.P.4
  • 23
    • 0037631361 scopus 로고    scopus 로고
    • Neutralization of circulating vascular endothelial growth factor (VEGF) by anti-VEGF antibodies and soluble VEGF receptor 1 (sFlt-1) induces proteinuria
    • Sugimoto H, Hamano Y, Charytan D et al. Neutralization of circulating vascular endothelial growth factor (VEGF) by anti-VEGF antibodies and soluble VEGF receptor 1 (sFlt-1) induces proteinuria. J. Biol. Chem. 2003; 278: 12 605-8.
    • (2003) J. Biol. Chem. , vol.278
    • Sugimoto, H.1    Hamano, Y.2    Charytan, D.3
  • 24
    • 0042343801 scopus 로고    scopus 로고
    • A randomized trial of bevacizumab, an anti-vascular endothelial growth factor antibody, for metastatic renal cancer
    • Yang JC, Haworth L, Sherry RM et al. A randomized trial of bevacizumab, an anti-vascular endothelial growth factor antibody, for metastatic renal cancer. N. Engl J. Med. 2003; 349: 427-34.
    • (2003) N. Engl J. Med. , vol.349 , pp. 427-434
    • Yang, J.C.1    Haworth, L.2    Sherry, R.M.3
  • 25
    • 0037370325 scopus 로고    scopus 로고
    • Glomerular-specific alterations of VEGF-A expression lead to distinct congenital and acquired renal diseases
    • Eremina V, Sood M, Haigh J et al. Glomerular-specific alterations of VEGF-A expression lead to distinct congenital and acquired renal diseases. J. Clin. Invest. 2003; 111: 707-16.
    • (2003) J. Clin. Invest. , vol.111 , pp. 707-716
    • Eremina, V.1    Sood, M.2    Haigh, J.3
  • 26
    • 0033662239 scopus 로고    scopus 로고
    • Perlecan, the major proteoglycan of basement membranes, is altered in patients with Schwartz-Jampel syndrome (chondrodystrophic myotonia)
    • Nicole S, Davoine CS, Topaloglu H et al. Perlecan, the major proteoglycan of basement membranes, is altered in patients with Schwartz-Jampel syndrome (chondrodystrophic myotonia). Nat. Genet. 2000; 26: 480-83.
    • (2000) Nat. Genet. , vol.26 , pp. 480-483
    • Nicole, S.1    Davoine, C.S.2    Topaloglu, H.3
  • 27
    • 0035068499 scopus 로고    scopus 로고
    • Dyssegmental dysplasia, Silverman-Handmaker type, is caused by functional null mutations of the perlecan gene
    • Arikawa-Hirasawa E, Wilcox WR, Le AH et al. Dyssegmental dysplasia, Silverman-Handmaker type, is caused by functional null mutations of the perlecan gene. Nat. Genet. 2001; 27: 431-4.
    • (2001) Nat. Genet. , vol.27 , pp. 431-434
    • Arikawa-Hirasawa, E.1    Wilcox, W.R.2    Le, A.H.3
  • 28
    • 0031837107 scopus 로고    scopus 로고
    • The putative tumour suppressor EXT1 alters the expression of cell-surface heparan sulfate
    • McCormick C, Leduc Y, Martindale D et al. The putative tumour suppressor EXT1 alters the expression of cell-surface heparan sulfate. Nat. Genet. 1998; 19: 158-61.
    • (1998) Nat. Genet. , vol.19 , pp. 158-161
    • McCormick, C.1    Leduc, Y.2    Martindale, D.3
  • 29
    • 0035093836 scopus 로고    scopus 로고
    • Glypicans and the biology of renal malformations
    • Grisaru S, Rosenblum ND. Glypicans and the biology of renal malformations. Pediatr. Nephrol. 2001; 16: 302-6.
    • (2001) Pediatr. Nephrol. , vol.16 , pp. 302-306
    • Grisaru, S.1    Rosenblum, N.D.2
  • 30
    • 0033946278 scopus 로고    scopus 로고
    • Glomerular heparan sulfate alterations: Mechanisms and relevance for proteinuria
    • Raats CJ, Van Den Born J, Berden JH. Glomerular heparan sulfate alterations: mechanisms and relevance for proteinuria. Kidney Int. 2000; 57: 385-400.
    • (2000) Kidney Int. , vol.57 , pp. 385-400
    • Raats, C.J.1    Van Den Born, J.2    Berden, J.H.3
  • 31
    • 0025187262 scopus 로고
    • Cross-reactivity of monoclonal anti-DNA antibodies with heparan sulfate is mediated via bound DNA/histone complexes
    • Termaat RM, Brinkman K, van Compel F et al. Cross-reactivity of monoclonal anti-DNA antibodies with heparan sulfate is mediated via bound DNA/histone complexes. J. Autoimmun. 1990; 3: 531-45.
    • (1990) J. Autoimmun. , vol.3 , pp. 531-545
    • Termaat, R.M.1    Brinkman, K.2    Van Compel, F.3
  • 32
    • 0028015572 scopus 로고
    • Anti-nucleosome antibodies complexed to nucleosomal antigens show anti-DNA reactivity and bind to rat glomerular basement membrane in vivo
    • Kramers C, Hylkema MN, van Bruggen MC et al. Anti-nucleosome antibodies complexed to nucleosomal antigens show anti-DNA reactivity and bind to rat glomerular basement membrane in vivo. J. Clin. Invest. 1994; 94: 568-77.
    • (1994) J. Clin. Invest. , vol.94 , pp. 568-577
    • Kramers, C.1    Hylkema, M.N.2    Van Bruggen, M.C.3
  • 33
    • 0024403795 scopus 로고
    • Histones have high affinity for the glomerular basement membrane. Relevance for immune complex formation in lupus nephritis
    • Schmiedeke TM, Stockl FW, Weber R, Sugisaki Y, Batsford SR, Vogt A. Histones have high affinity for the glomerular basement membrane. Relevance for immune complex formation in lupus nephritis. J. Exp. Med. 1989; 169: 1879-94.
    • (1989) J. Exp. Med. , vol.169 , pp. 1879-1894
    • Schmiedeke, T.M.1    Stockl, F.W.2    Weber, R.3    Sugisaki, Y.4    Batsford, S.R.5    Vogt, A.6
  • 34
    • 0026737572 scopus 로고
    • Multiple mechanisms for doxorubicin cytotoxicity on glomerular epithelial cells 'in vitro'
    • Ghiggeri GM, Bertelli R, Ginevri F et al. Multiple mechanisms for doxorubicin cytotoxicity on glomerular epithelial cells 'in vitro'. Eur J. Pharmacol. 1992; 228: 77-83.
    • (1992) Eur J. Pharmacol. , vol.228 , pp. 77-83
    • Ghiggeri, G.M.1    Bertelli, R.2    Ginevri, F.3
  • 35
    • 0021076614 scopus 로고
    • Reactive oxygen production by cultured rat glomerular mesangial cells during phagocytosis is associated with stimulation of lipoxygenase activity
    • Baud L, Hagege J, Sraer J, Rondeau E, Perez J, Ardaillou R. Reactive oxygen production by cultured rat glomerular mesangial cells during phagocytosis is associated with stimulation of lipoxygenase activity. J. Exp. Med. 1983; 158: 1836-52.
    • (1983) J. Exp. Med. , vol.158 , pp. 1836-1852
    • Baud, L.1    Hagege, J.2    Sraer, J.3    Rondeau, E.4    Perez, J.5    Ardaillou, R.6
  • 36
    • 0022539964 scopus 로고
    • Complement membrane attack complex stimulates production of reactive oxygen metabolites by cultured rat mesangial cells
    • Adler S, Baker PJ, Johnson RJ, Ochi RF, Pritzl P, Couser WG. Complement membrane attack complex stimulates production of reactive oxygen metabolites by cultured rat mesangial cells. J. Clin. Invest. 1986; 11: 762-7.
    • (1986) J. Clin. Invest. , vol.11 , pp. 762-767
    • Adler, S.1    Baker, P.J.2    Johnson, R.J.3    Ochi, R.F.4    Pritzl, P.5    Couser, W.G.6
  • 37
    • 0025069960 scopus 로고
    • Interleukin 1-alpha and tumor necrosis factor-alpha induce oxygen radical production in mesangial cells
    • Radeke HH, Meier B, Topley N, Fioge J, Habermehl GG, Resch K. Interleukin 1-alpha and tumor necrosis factor-alpha induce oxygen radical production in mesangial cells. Kidney Int. 1990; 37: 767-75.
    • (1990) Kidney Int. , vol.37 , pp. 767-775
    • Radeke, H.H.1    Meier, B.2    Topley, N.3    Fioge, J.4    Habermehl, G.G.5    Resch, K.6
  • 38
    • 0023266398 scopus 로고
    • Immune complexes bind to cultured rat glomerular mesangial cells to stimulate superoxide release. Evidence for an Fc receptor
    • Sedor JR, Carey SW, Emancipator SN. Immune complexes bind to cultured rat glomerular mesangial cells to stimulate superoxide release. Evidence for an Fc receptor. J. Immunol. 1987; 138: 3751-7.
    • (1987) J. Immunol. , vol.138 , pp. 3751-3757
    • Sedor, J.R.1    Carey, S.W.2    Emancipator, S.N.3
  • 39
    • 0029069047 scopus 로고
    • The chemical modification of glycosaminoglycan structure by oxygen-derived species in vitro
    • Moseley R, Waddington R, Evans P, Halliwell B, Embery G. The chemical modification of glycosaminoglycan structure by oxygen-derived species in vitro. Biochim. Biophys. Acta 1995; 1244: 245-52.
    • (1995) Biochim. Biophys. Acta , vol.1244 , pp. 245-252
    • Moseley, R.1    Waddington, R.2    Evans, P.3    Halliwell, B.4    Embery, G.5
  • 40
    • 0025373721 scopus 로고
    • The inhibitory action of oxygen radical scavengers on proteinuria and glomerular heparan sulphate loss in the isolated perfused kidney
    • Tay M, Comper WD, Vassiliou P, Glasgow EF, Baker MS, Pratt L. The inhibitory action of oxygen radical scavengers on proteinuria and glomerular heparan sulphate loss in the isolated perfused kidney. Biochem. Int. 1990; 20: 767-78.
    • (1990) Biochem. Int. , vol.20 , pp. 767-778
    • Tay, M.1    Comper, W.D.2    Vassiliou, P.3    Glasgow, E.F.4    Baker, M.S.5    Pratt, L.6
  • 41
    • 0030664773 scopus 로고    scopus 로고
    • Hydroxyl radicals depolymerize glomerular heparan sulfate in vitro and in experimental nephrotic syndrome
    • Raats CJ, Bakker MA, van den Born J, Berden JH. Hydroxyl radicals depolymerize glomerular heparan sulfate in vitro and in experimental nephrotic syndrome. J. Biol. Chem. 1997; 272: 26 734-41.
    • (1997) J. Biol. Chem. , vol.272
    • Raats, C.J.1    Bakker, M.A.2    Van Den Born, J.3    Berden, J.H.4
  • 42
    • 0025314928 scopus 로고
    • Heparin protects cultured arterial endothelial cells from damage by toxic oxygen metabolites
    • Hiebert LM, Liu JM. Heparin protects cultured arterial endothelial cells from damage by toxic oxygen metabolites. Atherosclerosis 1990; 83: 47-51.
    • (1990) Atherosclerosis , vol.83 , pp. 47-51
    • Hiebert, L.M.1    Liu, J.M.2
  • 43
    • 0029855958 scopus 로고    scopus 로고
    • Heparin and heparinoids prevent the binding of immune complexes containing nucleosomal antigens to the GBM and delay nephritis in MRL/lpr mice
    • van Bruggen MC, Walgreen B, Rijke TP et al. Heparin and heparinoids prevent the binding of immune complexes containing nucleosomal antigens to the GBM and delay nephritis in MRL/lpr mice. Kidney Int. 1996; 50: 1555-64.
    • (1996) Kidney Int. , vol.50 , pp. 1555-1564
    • Van Bruggen, M.C.1    Walgreen, B.2    Rijke, T.P.3
  • 44
    • 0026699401 scopus 로고
    • Effect of heparin on the anionic sites of glomerular basement membrane in adriamycin nephrosis in rats
    • Chen ZY, Jiang XY, Fei L. Effect of heparin on the anionic sites of glomerular basement membrane in adriamycin nephrosis in rats. Chin. Med. J. (Engl.) 1992; 105: 671-5.
    • (1992) Chin. Med. J. (Engl.) , vol.105 , pp. 671-675
    • Chen, Z.Y.1    Jiang, X.Y.2    Fei, L.3
  • 45
    • 0028092966 scopus 로고
    • Treatment with a glycosaminoglycan formulation ameliorates experimental diabetic nephropathy
    • Gambaro G, Venturini AP, Noonan DM et al. Treatment with a glycosaminoglycan formulation ameliorates experimental diabetic nephropathy. Kidney Int. 1994; 46: 797-806.
    • (1994) Kidney Int. , vol.46 , pp. 797-806
    • Gambaro, G.1    Venturini, A.P.2    Noonan, D.M.3
  • 46
    • 0027312478 scopus 로고
    • Distribution of GBM heparan sulfate proteoglycan core protein and side chains in human glomerular diseases
    • van den Bom J, van den Heuvel LP, Bakker MA et al. Distribution of GBM heparan sulfate proteoglycan core protein and side chains in human glomerular diseases. Kidney Int. 1993; 43: 454-63.
    • (1993) Kidney Int. , vol.43 , pp. 454-463
    • Van Den Bom, J.1    Van Den Heuvel, L.P.2    Bakker, M.A.3
  • 47
    • 0029071294 scopus 로고
    • Reduction of heparan sulphate-associated anionic sites in the glomerular basement membrane of rats with streptozotocin-induced diabetic nephropathy
    • van den Born J, van Kraats AA, Bakker MA et al. Reduction of heparan sulphate-associated anionic sites in the glomerular basement membrane of rats with streptozotocin-induced diabetic nephropathy. Diabetologia 1995a; 38: 1169-75.
    • (1995) Diabetologia , vol.38 , pp. 1169-1175
    • Van Den Born, J.1    Van Kraats, A.A.2    Bakker, M.A.3
  • 48
    • 0028891176 scopus 로고
    • Selective proteinuria in diabetic nephropathy in the rat is associated with a relative decrease in glomerular basement membrane heparan sulphate
    • van den Born J, van Kraats AA, Bakker MA et al. Selective proteinuria in diabetic nephropathy in the rat is associated with a relative decrease in glomerular basement membrane heparan sulphate. Diabetologia 1995; 38: 161-72.
    • (1995) Diabetologia , vol.38 , pp. 161-172
    • Van Den Born, J.1    Van Kraats, A.A.2    Bakker, M.A.3
  • 49
    • 0029093903 scopus 로고
    • Is microalbuminuria in diabetes due to changes in glomerular heparan sulphate?
    • Editorial
    • van den Born J, Berden JH. Is microalbuminuria in diabetes due to changes in glomerular heparan sulphate? (Editorial) Nephrol. Dial. Transplant. 1995; 10: 1277-9.
    • (1995) Nephrol. Dial. Transplant. , vol.10 , pp. 1277-1279
    • Van Den Born, J.1    Berden, J.H.2
  • 50
    • 2442748185 scopus 로고
    • Decreased de novo synthesis of glomerular proteoglycans in diabetes: Biochemical and autotadiographic evidence
    • Kanwar YS, Rosenzweig LJ, Linker A, Jakubowski ML. Decreased de novo synthesis of glomerular proteoglycans in diabetes: biochemical and autotadiographic evidence. Proc. Natl Acad. Sci. USA 1983; 80: 2272-7.
    • (1983) Proc. Natl Acad. Sci. USA , vol.80 , pp. 2272-2277
    • Kanwar, Y.S.1    Rosenzweig, L.J.2    Linker, A.3    Jakubowski, M.L.4
  • 51
    • 0021723019 scopus 로고
    • Evidence for diabetes-induced alterations in the sulfation of heparin sulfate intestinal epithelial cells
    • Levy P, Picard J, Bruel A. Evidence for diabetes-induced alterations in the sulfation of heparin sulfate intestinal epithelial cells. Life Sci. 1984; 35; 2613-20.
    • (1984) Life Sci. , vol.35 , pp. 2613-2620
    • Levy, P.1    Picard, J.2    Bruel, A.3
  • 52
    • 0030662123 scopus 로고    scopus 로고
    • Immunohistochemical quantification of heparan sulfate proteoglycan and collagen IV in skeletal muscle capillary basement membranes of patients with diabetic nephropathy
    • Yokoyama H, Hoyer PE, Hansen PM et al. Immunohistochemical quantification of heparan sulfate proteoglycan and collagen IV in skeletal muscle capillary basement membranes of patients with diabetic nephropathy. Diabetes 1997; 46: 1875-80.
    • (1997) Diabetes , vol.46 , pp. 1875-1880
    • Yokoyama, H.1    Hoyer, P.E.2    Hansen, P.M.3
  • 53
    • 15444355265 scopus 로고    scopus 로고
    • Extracellular matrix in human diabetic nephropathy: Reduced expression of heparan sulphate in skin basement membrane
    • van der Pijl JW, Daha MR, van den Born J et al. Extracellular matrix in human diabetic nephropathy: reduced expression of heparan sulphate in skin basement membrane. Diabetoiogia 1998; 41: 791-8.
    • (1998) Diabetoiogia , vol.41 , pp. 791-798
    • Van Der Pijl, J.W.1    Daha, M.R.2    Van Den Born, J.3
  • 54
    • 0034791187 scopus 로고    scopus 로고
    • Increased expression of heparanase in puromycin aminonucleoside nephrosis
    • Levidiotis V, Kanellis J, Ierino FL, Power DA. Increased expression of heparanase in puromycin aminonucleoside nephrosis. Kidney Int. 2001; 60: 1287-96.
    • (2001) Kidney Int. , vol.60 , pp. 1287-1296
    • Levidiotis, V.1    Kanellis, J.2    Ierino, F.L.3    Power, D.A.4
  • 55
    • 0023801387 scopus 로고
    • The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo
    • Johnson RJ, Couser WG, Alpers CE, Vissers M, Schuhe M, Klebanoff SJ. The human neutrophil serine proteinases, elastase and cathepsin G, can mediate glomerular injury in vivo. J. Exp. Med. 1988; 168: 1169-74.
    • (1988) J. Exp. Med. , vol.168 , pp. 1169-1174
    • Johnson, R.J.1    Couser, W.G.2    Alpers, C.E.3    Vissers, M.4    Schuhe, M.5    Klebanoff, S.J.6
  • 56
    • 8944225501 scopus 로고    scopus 로고
    • Elastase, hut not proteinase 3 (PR3), induces proteinuria associated with loss of glomerular basement membrane heparan sulphate after in vivo renal perfusion in rats
    • Heeringa P, Van den Born J, Brouwer E et al. Elastase, hut not proteinase 3 (PR3), induces proteinuria associated with loss of glomerular basement membrane heparan sulphate after in vivo renal perfusion in rats. Clin. Exp Immunol. 1996; 105: 321-9.
    • (1996) Clin. Exp. Immunol. , vol.105 , pp. 321-329
    • Heeringa, P.1    Van Den Born, J.2    Brouwer, E.3
  • 57
    • 10744232455 scopus 로고    scopus 로고
    • Transgenic expression of mammalian heparanase uncovers physiological functions of heparan sulfate in tissue morphogenesis, vascularization, and feeding behavior
    • Zcharia E, Metzger S, Chajek-Shaul T et al. Transgenic expression of mammalian heparanase uncovers physiological functions of heparan sulfate in tissue morphogenesis, vascularization, and feeding behavior. FASEB J. 2004; 18: 252-63.
    • (2004) FASEB J. , vol.18 , pp. 252-263
    • Zcharia, E.1    Metzger, S.2    Chajek-Shaul, T.3
  • 58
    • 0346734139 scopus 로고    scopus 로고
    • Heparanase is involved in the pathogenesis of proteinuria as a result of glomerulonephritis
    • Levidiotis V, Freeman C, Tikellis C, Cooper ME, Power DA. Heparanase is involved in the pathogenesis of proteinuria as a result of glomerulonephritis. J. Am. Soc. Nephrol. 2004; 15: 68-78.
    • (2004) J. Am. Soc. Nephrol. , vol.15 , pp. 68-78
    • Levidiotis, V.1    Freeman, C.2    Tikellis, C.3    Cooper, M.E.4    Power, D.A.5
  • 59
    • 16644385848 scopus 로고    scopus 로고
    • A synthetic heparanase inhibitor reduces proteinuria in passive Heymann nephritis
    • Levidiotis V, Freeman C, Punler M et al. A synthetic heparanase inhibitor reduces proteinuria in passive Heymann nephritis. J. Am. Soc. Nephrol. 2004; 15: 2882-92.
    • (2004) J. Am. Soc. Nephrol. , vol.15 , pp. 2882-2892
    • Levidiotis, V.1    Freeman, C.2    Punler, M.3
  • 60
    • 0035413616 scopus 로고    scopus 로고
    • Cyclin-dependent kinases
    • Harper JW, Adams PD. Cyclin-dependent kinases. Chem. Rev. 2001; 101: 2511-26.
    • (2001) Chem. Rev. , vol.101 , pp. 2511-2526
    • Harper, J.W.1    Adams, P.D.2
  • 61
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: Positive and negative regulators of G1-phase progression
    • Sherr CJ, Roberts JM. CDK inhibitors: positive and negative regulators of G1-phase progression. Genes Dev. 1999; 13: 1501-12.
    • (1999) Genes Dev. , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 62
    • 0032410285 scopus 로고    scopus 로고
    • Cip/Kip cyclin-dependent kinase inhibitors: Brakes of the cell cycle engine during development
    • Nakayama K. Cip/Kip cyclin-dependent kinase inhibitors: brakes of the cell cycle engine during development. Bioessays 1998; 20: 1020-29.
    • (1998) Bioessays , vol.20 , pp. 1020-1029
    • Nakayama, K.1
  • 63
    • 0036460334 scopus 로고    scopus 로고
    • Glomerular differentiation in p27 and p57 double-mutant metanephrol
    • Tomari S, Nagahama H, Shu Y et al. Glomerular differentiation in p27 and p57 double-mutant metanephrol. Anat. Embryol. 2002; 206: 31-6.
    • (2002) Anat. Embryol. , vol.206 , pp. 31-36
    • Tomari, S.1    Nagahama, H.2    Shu, Y.3
  • 64
    • 8544282400 scopus 로고    scopus 로고
    • Cyclin kinase inhibitors are increased during experimental membranous nephropathy: Potential role in limiting glomerular epithelial cell proliferation in vivo
    • Shankland SJ, Floege J, Thomas SE et al. Cyclin kinase inhibitors are increased during experimental membranous nephropathy: potential role in limiting glomerular epithelial cell proliferation in vivo. Kidney Int. 1997; 52: 404-13.
    • (1997) Kidney Int. , vol.52 , pp. 404-413
    • Shankland, S.J.1    Floege, J.2    Thomas, S.E.3
  • 66
    • 0035205183 scopus 로고    scopus 로고
    • Suppression of HIV-1 expression by inhibitors of cyclin-dependent kinases promotes differentiation of infected podocytes
    • Nelson PJ, Gelman IH, Klotman PE. Suppression of HIV-1 expression by inhibitors of cyclin-dependent kinases promotes differentiation of infected podocytes. J. Am. Soc. Nephrol. 2001; 12: 2827-31.
    • (2001) J. Am. Soc. Nephrol. , vol.12 , pp. 2827-2831
    • Nelson, P.J.1    Gelman, I.H.2    Klotman, P.E.3
  • 67
    • 0036149007 scopus 로고    scopus 로고
    • Mechanical stress reduces podocyte proliferation in vitro
    • Petermann AT, Hiromura K, Blonski M et al. Mechanical stress reduces podocyte proliferation in vitro. Kidney Int. 2002; 61: 40-50.
    • (2002) Kidney Int. , vol.61 , pp. 40-50
    • Petermann, A.T.1    Hiromura, K.2    Blonski, M.3
  • 69
    • 0030826607 scopus 로고    scopus 로고
    • Immunohistochemical localization of ANG II AT1 receptor in adult rat kidney using a monoclonal antibody
    • Harrison-Bernard LM, Navar LO, Ho MM, Vinson GP, el-Dahr SS. Immunohistochemical localization of ANG II AT1 receptor in adult rat kidney using a monoclonal antibody. Am. J. Physiol. 1997; 273: F170-77.
    • (1997) Am. J. Physiol. , vol.273
    • Harrison-Bernard, L.M.1    Navar, L.O.2    Ho, M.M.3    Vinson, G.P.4    El-Dahr, S.S.5
  • 70
    • 15844368318 scopus 로고    scopus 로고
    • Effect of the angiotensin-converting-enzyme inhibitor benazepril on the progression of chronic renal insufficiency
    • The Angiotensin-Converting-Enzyme Inhibition in Progressive Renal Insufficiency Study Group
    • Maschio G, Alberti D, Janin G et al. Effect of the angiotensin- converting-enzyme inhibitor benazepril on the progression of chronic renal insufficiency. The Angiotensin-Converting-Enzyme Inhibition in Progressive Renal Insufficiency Study Group. N. Engl. J. Med. 1996; 334; 939-45.
    • (1996) N. Engl. J. Med. , vol.334 , pp. 939-945
    • Maschio, G.1    Alberti, D.2    Janin, G.3
  • 71
    • 0029954482 scopus 로고    scopus 로고
    • Effect of ramipril, nifedipine, and moxonidine on glomerular morphology and podocyte structure in experimental renal failure
    • Amann K, Nichols C, Tornig J et al. Effect of ramipril, nifedipine, and moxonidine on glomerular morphology and podocyte structure in experimental renal failure. Nephrol. Dial. Transplant. 1996; 11: 1003-11.
    • (1996) Nephrol. Dial. Transplant. , vol.11 , pp. 1003-1011
    • Amann, K.1    Nichols, C.2    Tornig, J.3
  • 72
    • 0026504525 scopus 로고
    • Homeobox genes and axial patterning
    • McGinnis W, Krumlauf R. Homeobox genes and axial patterning. Cell 1992; 68: 283-302.
    • (1992) Cell , vol.68 , pp. 283-302
    • McGinnis, W.1    Krumlauf, R.2
  • 73
    • 0031893838 scopus 로고    scopus 로고
    • Molecular structure and assembly of the tight junction
    • Denker BM, Nigatn SK. Molecular structure and assembly of the tight junction. Am. J. Physiol. 1998; 274: F1-9.
    • (1998) Am. J. Physiol. , vol.274
    • Denker, B.M.1    Nigatn, S.K.2
  • 74
    • 0344541695 scopus 로고    scopus 로고
    • Nephrin localizes at the podocyte filtration slit area and is characteristically spliced in the human kidney
    • Holthofer H, Ahola H, Solin ML et al. Nephrin localizes at the podocyte filtration slit area and is characteristically spliced in the human kidney. Am. J. Pathol. 1999; 155: 1681-7.
    • (1999) Am. J. Pathol. , vol.155 , pp. 1681-1687
    • Holthofer, H.1    Ahola, H.2    Solin, M.L.3
  • 75
    • 0033634789 scopus 로고    scopus 로고
    • Role of nephrin in cell junction formation in human nephrogenesis
    • Ruotsalainen V, Patrakka J, Tissari P et al. Role of nephrin in cell junction formation in human nephrogenesis. Am. J. Pathol. 2000; 157: 1905-16.
    • (2000) Am. J. Pathol. , vol.157 , pp. 1905-1916
    • Ruotsalainen, V.1    Patrakka, J.2    Tissari, P.3
  • 76
  • 78
    • 0026025505 scopus 로고
    • Contrasting expression patterns of three members of the myc family of protooncogenes in the developing and adult mouse kidney
    • Mugrauer G, Ekblom P. Contrasting expression patterns of three members of the myc family of protooncogenes in the developing and adult mouse kidney. J. Cell Biol 1991; 112: 13-25.
    • (1991) J. Cell Biol. , vol.112 , pp. 13-25
    • Mugrauer, G.1    Ekblom, P.2
  • 79
    • 0031728156 scopus 로고    scopus 로고
    • Epitope-specific antibodies to the 43-kD glomerular membrane protein podoplanin cause ptoteinuria and rapid flattening of podocytes
    • Matsui K, Breiteneder-Geleff S, Kerjaschki D. Epitope-specific antibodies to the 43-kD glomerular membrane protein podoplanin cause ptoteinuria and rapid flattening of podocytes. J. Am. Soc. Nephrol. 1998; 9: 2013-26.
    • (1998) J. Am. Soc. Nephrol. , vol.9 , pp. 2013-2026
    • Matsui, K.1    Breiteneder-Geleff, S.2    Kerjaschki, D.3
  • 80
    • 4744375611 scopus 로고    scopus 로고
    • Role of truncating mutations in MME gene in fetomaternal alloimmunisation and antenatal glomerulopathies
    • Debiec H, Nauta J, Coulet F et al. Role of truncating mutations in MME gene in fetomaternal alloimmunisation and antenatal glomerulopathies. Lancet 2004; 364: 1252-9.
    • (2004) Lancet , vol.364 , pp. 1252-1259
    • Debiec, H.1    Nauta, J.2    Coulet, F.3
  • 81
    • 0032929050 scopus 로고    scopus 로고
    • The dysregulated podocyte phenotype: A novel concept in the pathogenesis of collapsing idiopathic focal segmental glomerulosclerosis and HIV-associated nephropathy
    • Barisoni L, Kriz W, Mundel P, D'Agati V. The dysregulated podocyte phenotype: a novel concept in the pathogenesis of collapsing idiopathic focal segmental glomerulosclerosis and HIV-associated nephropathy. J. Am. Soc. Nephrol. 1999; 10: 51-61.
    • (1999) J. Am. Soc. Nephrol. , vol.10 , pp. 51-61
    • Barisoni, L.1    Kriz, W.2    Mundel, P.3    D'Agati, V.4
  • 82
    • 0029940563 scopus 로고    scopus 로고
    • Cytoskeletal changes in podocytes associated with foot process effacement in Masugi nephritis
    • Shirato I, Sakai T, Kimura K, Tomino Y, Kriz W. Cytoskeletal changes in podocytes associated with foot process effacement in Masugi nephritis. Am. J. Pathol. 1996; 148: 1283-96.
    • (1996) Am. J. Pathol. , vol.148 , pp. 1283-1296
    • Shirato, I.1    Sakai, T.2    Kimura, K.3    Tomino, Y.4    Kriz, W.5
  • 83
    • 0030764235 scopus 로고    scopus 로고
    • Podocyte alpha-actinin induction precedes foot process effacement in experimental nephrotic syndrome
    • Smoyer WE, Mundel P, Gupta A, Welsh MJ. Podocyte alpha-actinin induction precedes foot process effacement in experimental nephrotic syndrome. Am. J. Physiol. 1997; 273: F150-57.
    • (1997) Am. J. Physiol. , vol.273
    • Smoyer, W.E.1    Mundel, P.2    Gupta, A.3    Welsh, M.J.4
  • 84
    • 0025944870 scopus 로고
    • Transient and locally restricted expression of the rosl protooncogene during mouse development
    • Sonnenberg E, Godecke A, Walter B, Bladt F, Birchmeier C. Transient and locally restricted expression of the rosl protooncogene during mouse development. EMBO J. 1991; 10: 3693-702.
    • (1991) EMBO J. , vol.10 , pp. 3693-3702
    • Sonnenberg, E.1    Godecke, A.2    Walter, B.3    Bladt, F.4    Birchmeier, C.5
  • 85
    • 0344120816 scopus 로고    scopus 로고
    • CD2-associated protein and glomerular disease
    • Wolf G, Stahl RA. CD2-associated protein and glomerular disease. Lancet 2003; 362: 1746-8.
    • (2003) Lancet , vol.362 , pp. 1746-1748
    • Wolf, G.1    Stahl, R.A.2
  • 86
    • 0038136885 scopus 로고    scopus 로고
    • CD2-associated protein haploin-sufficiency is linked to glomerular disease susceptibility
    • Kim JM, Wu H, Green G et al. CD2-associated protein haploin-sufficiency is linked to glomerular disease susceptibility. Science 2003; 300: 1298-300.
    • (2003) Science , vol.300 , pp. 1298-1300
    • Kim, J.M.1    Wu, H.2    Green, G.3
  • 87
    • 0035164681 scopus 로고    scopus 로고
    • The murine nephrin gene is specifically expressed in kidney, brain and pancreas: Inactivation of the gene leads to massive proteinuria and neonatal death
    • Putaala H, Soininen R, Kilpelainen P, Wartiovaara J, Tryggvason K. The murine nephrin gene is specifically expressed in kidney, brain and pancreas: inactivation of the gene leads to massive proteinuria and neonatal death. Hum. Mol. Genet. 2001; 10: 18.
    • (2001) Hum. Mol. Genet. , vol.10 , pp. 18
    • Putaala, H.1    Soininen, R.2    Kilpelainen, P.3    Wartiovaara, J.4    Tryggvason, K.5
  • 88
    • 0033431774 scopus 로고    scopus 로고
    • Nephritogenic mAb 5-1-6 is directed at the extracellular domain of rat nephrin
    • Topham PS, Kawachi H, Haydar SA et al. Nephritogenic mAb 5-1-6 is directed at the extracellular domain of rat nephrin. J. Clin. Invest. 1999; 104: 1559-66.
    • (1999) J. Clin. Invest. , vol.104 , pp. 1559-1566
    • Topham, P.S.1    Kawachi, H.2    Haydar, S.A.3
  • 89
    • 0035028772 scopus 로고    scopus 로고
    • Blocking angiotensin 11 synthesis/activity preserves glomerular nephrin in rats with severe nephrosis
    • Benigni A, Tomasoni S, Gagliardini E et al. Blocking angiotensin 11 synthesis/activity preserves glomerular nephrin in rats with severe nephrosis. J. Am. Soc. Nephrol. 2001; 12: 941-8.
    • (2001) J. Am. Soc. Nephrol. , vol.12 , pp. 941-948
    • Benigni, A.1    Tomasoni, S.2    Gagliardini, E.3
  • 90
    • 4744360704 scopus 로고    scopus 로고
    • Nephrin expression is increased in anti-Thy1.1-induced glomerulonephritis in rats
    • Schaefer L, Ren S, Schaefer RM et al. Nephrin expression is increased in anti-Thy1.1-induced glomerulonephritis in rats. Biochem. Biophys. Res. Commun. 2004; 324: 247-54.
    • (2004) Biochem. Biophys. Res. Commun. , vol.324 , pp. 247-254
    • Schaefer, L.1    Ren, S.2    Schaefer, R.M.3
  • 91
    • 0035023678 scopus 로고    scopus 로고
    • Nephrin redistribution on podocytes is a potential mechanism for proteinuria in patients with primary acquired nephrotic syndrome
    • Doublier S, Ruotsalainen V, Salvidio G et al. Nephrin redistribution on podocytes is a potential mechanism for proteinuria in patients with primary acquired nephrotic syndrome. Am. J. Pathol. 2001; 158: 1723-31.
    • (2001) Am. J. Pathol. , vol.158 , pp. 1723-1731
    • Doublier, S.1    Ruotsalainen, V.2    Salvidio, G.3
  • 92
    • 0037083989 scopus 로고    scopus 로고
    • Recurrence of nephrotic syndrome in kidney grafts of patients with congenital nephrotic syndrome of the Finnish type: Role of nephrin
    • Patrakka J, Ruotsalainen V, Reponen P et al. Recurrence of nephrotic syndrome in kidney grafts of patients with congenital nephrotic syndrome of the Finnish type: role of nephrin. Transplantation 2002; 73: 394-403.
    • (2002) Transplantation , vol.73 , pp. 394-403
    • Patrakka, J.1    Ruotsalainen, V.2    Reponen, P.3
  • 93
    • 0036144232 scopus 로고    scopus 로고
    • Podocin localizes in the kidney to the slit diaphragm area
    • Roselli S, Gribouval O, Boute N et al. Podocin localizes in the kidney to the slit diaphragm area. Am. J. Pathol. 2002; 160: 131-9.
    • (2002) Am. J. Pathol. , vol.160 , pp. 131-139
    • Roselli, S.1    Gribouval, O.2    Boute, N.3
  • 94
    • 0034051681 scopus 로고    scopus 로고
    • Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis
    • Kaplan JM, Kim SH, North KN et al. Mutations in ACTN4, encoding alpha-actinin-4, cause familial focal segmental glomerulosclerosis. Nat. Genet. 2000; 24: 251-6.
    • (2000) Nat. Genet. , vol.24 , pp. 251-256
    • Kaplan, J.M.1    Kim, S.H.2    North, K.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.