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Volumn 4, Issue 6, 2009, Pages

Ligation of α-dystroglycan on podocytes induces intracellular signaling: A new mechanism for podocyte effacement?

Author keywords

[No Author keywords available]

Indexed keywords

AGRIN; ALPHA DYSTROGLYCAN; BIGLYCAN; FIBRONECTIN; LAMININ; UTROPHIN; ACTIN; CALCIUM; DYSTROGLYCAN; GLYCOPROTEIN; LIGAND;

EID: 67650164846     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0005979     Document Type: Article
Times cited : (10)

References (65)
  • 1
    • 0037207471 scopus 로고    scopus 로고
    • Cell biology of the glomerular podocyte
    • Pavenstadt H, Kriz W, Kretzler M (2003) Cell biology of the glomerular podocyte. Physiol Rev 83: 1: 253-307.
    • (2003) Physiol Rev , vol.83 , Issue.1 , pp. 253-307
    • Pavenstadt, H.1    Kriz, W.2    Kretzler, M.3
  • 2
    • 0026543686 scopus 로고
    • Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix
    • Ibraghimov-Beskrovnaya O, Ervasti JM, Leveille CJ, Slaughter CA, Sernett SW, et al. (1992) Primary structure of dystrophin-associated glycoproteins linking dystrophin to the extracellular matrix. Nature 355: 6362: 696-702.
    • (1992) Nature , vol.355 , Issue.6362 , pp. 696-702
    • Ibraghimov-Beskrovnaya, O.1    Ervasti, J.M.2    Leveille, C.J.3    Slaughter, C.A.4    Sernett, S.W.5
  • 3
    • 0023906647 scopus 로고
    • Characterization of dystrophin in muscle-biopsy specimens from patients with Duchenne's or Becker's muscular dystrophy
    • Hoffman EP, Fischbeck KH, Brown RH, Johnson M, Medori R, et al. (1988) Characterization of dystrophin in muscle-biopsy specimens from patients with Duchenne's or Becker's muscular dystrophy. N Engl J Med 318: 21: 1363-1368.
    • (1988) N Engl J Med , vol.318 , Issue.21 , pp. 1363-1368
    • Hoffman, E.P.1    Fischbeck, K.H.2    Brown, R.H.3    Johnson, M.4    Medori, R.5
  • 6
    • 0033839003 scopus 로고    scopus 로고
    • Expression of agrin, dystroglycan, and utrophin in normal renal tissue and in experimental glomerulopathies
    • Raats CJ, van den Born J, Bakker MA, Oppers-Walgreen B, Pisa BJ, et al. (2000) Expression of agrin, dystroglycan, and utrophin in normal renal tissue and in experimental glomerulopathies. Am J Pathol 156: 5: 1749-1765.
    • (2000) Am J Pathol , vol.156 , Issue.5 , pp. 1749-1765
    • Raats, C.J.1    van den Born, J.2    Bakker, M.A.3    Oppers-Walgreen, B.4    Pisa, B.J.5
  • 8
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti JM, Campbell KP (1993) A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J Cell Biol 122: 4: 809-823.
    • (1993) J Cell Biol , vol.122 , Issue.4 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 9
    • 0034009952 scopus 로고    scopus 로고
    • Glomerular expression of dystroglycans is reduced in minimal change nephrosis but not in focal segmental glomerulosclerosis
    • Regele HM, Fillipovic E, Langer B, Poczewki H, Kraxberger I, et al. (2000) Glomerular expression of dystroglycans is reduced in minimal change nephrosis but not in focal segmental glomerulosclerosis. J Am Soc Nephrol 11: 3: 403-412.
    • (2000) J Am Soc Nephrol , vol.11 , Issue.3 , pp. 403-412
    • Regele, H.M.1    Fillipovic, E.2    Langer, B.3    Poczewki, H.4    Kraxberger, I.5
  • 11
    • 0034695928 scopus 로고    scopus 로고
    • The small leucine-rich repeat proteoglycan biglycan binds to alpha- dystroglycan and is upregulated in dystrophic muscle
    • Bowe MA, Mendis DB, Fallon JR (2000) The small leucine-rich repeat proteoglycan biglycan binds to alpha- dystroglycan and is upregulated in dystrophic muscle. J Cell Biol 148: 4: 801-810.
    • (2000) J Cell Biol , vol.148 , Issue.4 , pp. 801-810
    • Bowe, M.A.1    Mendis, D.B.2    Fallon, J.R.3
  • 12
    • 0033797511 scopus 로고    scopus 로고
    • Small proteoglycans of normal adult human kidney: Distinct expression patterns of decorin, biglycan, fibromodulin, and lumican
    • 4
    • Schaefer L, Grone HJ, Raslik I, Robenek H, Ugorcakova J, et al. (2000) Small proteoglycans of normal adult human kidney: distinct expression patterns of decorin, biglycan, fibromodulin, and lumican. Kidney Int 58: 4: 1557-1568.
    • (2000) Kidney Int , vol.58 , pp. 1557-1568
    • Schaefer, L.1    Grone, H.J.2    Raslik, I.3    Robenek, H.4    Ugorcakova, J.5
  • 13
    • 0033934431 scopus 로고    scopus 로고
    • Expression of decorin, biglycan, and collagen type I in human renal fibrosing disease
    • Stokes MB, Holler S, Cui Y, Hudkins KL, Eitner F, et al. (2000) Expression of decorin, biglycan, and collagen type I in human renal fibrosing disease. Kidney Int 57: 2: 487-498.
    • (2000) Kidney Int , vol.57 , Issue.2 , pp. 487-498
    • Stokes, M.B.1    Holler, S.2    Cui, Y.3    Hudkins, K.L.4    Eitner, F.5
  • 14
    • 0032011197 scopus 로고    scopus 로고
    • An ultrastructural study of the colocalization of biglycan and decorin with AA amyloid fibrils in human renal glomeruli
    • Moss J, Shore I, Woodrow D (1998) An ultrastructural study of the colocalization of biglycan and decorin with AA amyloid fibrils in human renal glomeruli. Amyloid 5: 1: 43-48.
    • (1998) Amyloid , vol.5 , Issue.1 , pp. 43-48
    • Moss, J.1    Shore, I.2    Woodrow, D.3
  • 15
    • 0346505363 scopus 로고    scopus 로고
    • Glomerular expression of biglycan and decorin and urinary levels of decorin in primary glomerular disease
    • Kuroda M, Sasamura H, Kobayashi E, Shimizu-Hirota R, Nakazato Y, et al. (2004) Glomerular expression of biglycan and decorin and urinary levels of decorin in primary glomerular disease. Clin Nephrol 61: 1: 7-16.
    • (2004) Clin Nephrol , vol.61 , Issue.1 , pp. 7-16
    • Kuroda, M.1    Sasamura, H.2    Kobayashi, E.3    Shimizu-Hirota, R.4    Nakazato, Y.5
  • 16
    • 0035292906 scopus 로고    scopus 로고
    • Schaefer L, Raslik I, Grone HJ, Schonherr E, Macakova K, et al. (2001) Small proteoglycans in human diabetic nephropathy: discrepancy between glomerular expression and protein accumulation of decorin, biglycan, lumican, and fibromodulin. Faseb J 15: 3: 559-561.
    • Schaefer L, Raslik I, Grone HJ, Schonherr E, Macakova K, et al. (2001) Small proteoglycans in human diabetic nephropathy: discrepancy between glomerular expression and protein accumulation of decorin, biglycan, lumican, and fibromodulin. Faseb J 15: 3: 559-561.
  • 17
    • 0025102712 scopus 로고
    • Elevated expression of transforming growth factor-beta and proteoglycan production in experimental glomerulonephritis. Possible role in expansion of the mesangial extracellular matrix
    • Okuda S, Languino LR, Ruoslahti E, Border WA (1990) Elevated expression of transforming growth factor-beta and proteoglycan production in experimental glomerulonephritis. Possible role in expansion of the mesangial extracellular matrix. J Clin Invest 86: 2: 453-462.
    • (1990) J Clin Invest , vol.86 , Issue.2 , pp. 453-462
    • Okuda, S.1    Languino, L.R.2    Ruoslahti, E.3    Border, W.A.4
  • 19
    • 0036424227 scopus 로고    scopus 로고
    • Glucocorticoid regulation of proteoglycan synthesis in mesangial cells
    • Kuroda M, Sasamura H, Shimizu-Hirota R, Mifune M, Nakaya H, et al. (2002) Glucocorticoid regulation of proteoglycan synthesis in mesangial cells. Kidney Int 62: 3: 780-789.
    • (2002) Kidney Int , vol.62 , Issue.3 , pp. 780-789
    • Kuroda, M.1    Sasamura, H.2    Shimizu-Hirota, R.3    Mifune, M.4    Nakaya, H.5
  • 20
    • 0345863398 scopus 로고    scopus 로고
    • N-terminal alpha-dystroglycan binds to different extracellular matrix molecules expressed in regenerating peripheral nerves in a protein-mediated manner and promotes neurite extension of PC12 cells
    • Hall H, Bozic D, Michel K, Hubbell JA (2003) N-terminal alpha-dystroglycan binds to different extracellular matrix molecules expressed in regenerating peripheral nerves in a protein-mediated manner and promotes neurite extension of PC12 cells. Mol Cell Neurosci 24: 4: 1062-1073.
    • (2003) Mol Cell Neurosci , vol.24 , Issue.4 , pp. 1062-1073
    • Hall, H.1    Bozic, D.2    Michel, K.3    Hubbell, J.A.4
  • 21
    • 0031753918 scopus 로고    scopus 로고
    • Alterations in the distribution of plasma fibronectin and the ultrastructure of podocytes in the peripheral glomerular loops in nephrotic rats
    • Kubosawa H, Kondo Y (1998) Alterations in the distribution of plasma fibronectin and the ultrastructure of podocytes in the peripheral glomerular loops in nephrotic rats. Virchows Arch 433: 5: 449-455.
    • (1998) Virchows Arch , vol.433 , Issue.5 , pp. 449-455
    • Kubosawa, H.1    Kondo, Y.2
  • 22
    • 33847056610 scopus 로고    scopus 로고
    • Deletion of protein kinase C-beta isoform in vivo reduces renal hypertrophy but not albuminuria in the streptozotocin-induced diabetic mouse model
    • Meier M, Park JK, Overheu D, Kirsch T, Lindschau C, et al. (2007) Deletion of protein kinase C-beta isoform in vivo reduces renal hypertrophy but not albuminuria in the streptozotocin-induced diabetic mouse model. Diabetes 56: 2: 346-354.
    • (2007) Diabetes , vol.56 , Issue.2 , pp. 346-354
    • Meier, M.1    Park, J.K.2    Overheu, D.3    Kirsch, T.4    Lindschau, C.5
  • 23
    • 33846677486 scopus 로고    scopus 로고
    • Renoprotective effect of COMP-angiopoietin-1 in db/db mice with type 2 diabetes
    • Lee S, Kim W, Moon SO, Sung MJ, Kim DH, et al. (2007) Renoprotective effect of COMP-angiopoietin-1 in db/db mice with type 2 diabetes. Nephrol Dial Transplant 22: 2: 396-408.
    • (2007) Nephrol Dial Transplant , vol.22 , Issue.2 , pp. 396-408
    • Lee, S.1    Kim, W.2    Moon, S.O.3    Sung, M.J.4    Kim, D.H.5
  • 24
    • 33846875250 scopus 로고    scopus 로고
    • Inhibiting albumin glycation attenuates dysregulation of VEGFR-1 and collagen IV subchain production and the development of renal insufficiency
    • Cohen MP, Lautenslager GT, Hud E, Shea E, Wang A, et al. (2007) Inhibiting albumin glycation attenuates dysregulation of VEGFR-1 and collagen IV subchain production and the development of renal insufficiency. Am J Physiol Renal Physiol 292: 2: F789-F795.
    • (2007) Am J Physiol Renal Physiol , vol.292 , Issue.2
    • Cohen, M.P.1    Lautenslager, G.T.2    Hud, E.3    Shea, E.4    Wang, A.5
  • 26
    • 0344628721 scopus 로고    scopus 로고
    • Urine activity of cathepsin B, collagenase and urine excretion of TGF-beta 1 and fibronectin in membranous glomerulonephritis
    • Senatorski G, Paczek L, Sulowicz W, Gradowska L, Bartlomiejczyk I (1998) Urine activity of cathepsin B, collagenase and urine excretion of TGF-beta 1 and fibronectin in membranous glomerulonephritis. Res Exp Med (Berl) 198: 4: 199-206.
    • (1998) Res Exp Med (Berl) , vol.198 , Issue.4 , pp. 199-206
    • Senatorski, G.1    Paczek, L.2    Sulowicz, W.3    Gradowska, L.4    Bartlomiejczyk, I.5
  • 27
    • 1842834296 scopus 로고    scopus 로고
    • Analysis of collagen IV and fibronectin in blood and urine in evaluation of nephrotic fibrosis in children with chronic glomerulonephritis
    • Kilis-Pstrusinska K, Wikierα-Magott I, Zwolinska D, Kopec W, Rzeszutko M (2002) Analysis of collagen IV and fibronectin in blood and urine in evaluation of nephrotic fibrosis in children with chronic glomerulonephritis. Med Sci Monit 8: 10: CR713-CR719.
    • (2002) Med Sci Monit , vol.8 , Issue.10
    • Kilis-Pstrusinska, K.1    Wikierα-Magott, I.2    Zwolinska, D.3    Kopec, W.4    Rzeszutko, M.5
  • 28
    • 0028805790 scopus 로고
    • Identification and characterization of the dystrophin anchoring site on beta-dystroglycan
    • Jung D, Yang B, Meyer J, Chamberlain JS, Campbell KP (1995) Identification and characterization of the dystrophin anchoring site on beta-dystroglycan. J Biol Chem 270: 45: 27305-27310.
    • (1995) J Biol Chem , vol.270 , Issue.45 , pp. 27305-27310
    • Jung, D.1    Yang, B.2    Meyer, J.3    Chamberlain, J.S.4    Campbell, K.P.5
  • 29
    • 0032915455 scopus 로고    scopus 로고
    • The WW domain of dystrophin requires EF-hands region to interact with beta-dystroglycan
    • Rentschler S, Linn H, Deininger K, Bedford MT, Espanel X, et al. (1999) The WW domain of dystrophin requires EF-hands region to interact with beta-dystroglycan. Biol Chem 380: 4: 431-442.
    • (1999) Biol Chem , vol.380 , Issue.4 , pp. 431-442
    • Rentschler, S.1    Linn, H.2    Deininger, K.3    Bedford, M.T.4    Espanel, X.5
  • 30
    • 0034027602 scopus 로고    scopus 로고
    • Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin
    • James M, Nuttall A, Ilsley JL, Ottersbach K, Tinsley JM, et al. (2000) Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin. J Cell Sci 113(Pt 10): 1717-1726.
    • (2000) J Cell Sci , vol.113 , Issue.PART 10 , pp. 1717-1726
    • James, M.1    Nuttall, A.2    Ilsley, J.L.3    Ottersbach, K.4    Tinsley, J.M.5
  • 31
    • 0037138411 scopus 로고    scopus 로고
    • WW and SH3 domains, two different scaffolds to recognize proline-rich ligands
    • Macias MJ, Wiesner S, Sudol M (2002) WW and SH3 domains, two different scaffolds to recognize proline-rich ligands. FEBS Lett 513: 1: 30-37.
    • (2002) FEBS Lett , vol.513 , Issue.1 , pp. 30-37
    • Macias, M.J.1    Wiesner, S.2    Sudol, M.3
  • 32
    • 0343081091 scopus 로고    scopus 로고
    • Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan
    • Huang X, Poy F, Zhang R, Joachimiak A, Sudol M, et al. (2000) Structure of a WW domain containing fragment of dystrophin in complex with beta-dystroglycan. Nat Struct Biol 7: 8: 634-638.
    • (2000) Nat Struct Biol , vol.7 , Issue.8 , pp. 634-638
    • Huang, X.1    Poy, F.2    Zhang, R.3    Joachimiak, A.4    Sudol, M.5
  • 33
    • 0034903234 scopus 로고    scopus 로고
    • The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation
    • Ilsley JL, Sudol M, Winder SJ (2001) The interaction of dystrophin with beta-dystroglycan is regulated by tyrosine phosphorylation. Cell Signal 13: 9: 625-632.
    • (2001) Cell Signal , vol.13 , Issue.9 , pp. 625-632
    • Ilsley, J.L.1    Sudol, M.2    Winder, S.J.3
  • 34
    • 0035807788 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins
    • Sotgia F, Lee H, Bedford MT, Petrucci T, Sudol M, et al. (2001) Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins. Biochemistry 40: 48: 14585-14592.
    • (2001) Biochemistry , vol.40 , Issue.48 , pp. 14585-14592
    • Sotgia, F.1    Lee, H.2    Bedford, M.T.3    Petrucci, T.4    Sudol, M.5
  • 35
    • 0029013870 scopus 로고
    • SH3 domain-mediated interaction of dystroglycan and Grb2
    • Yang B, Jung D, Motto D, Meyer J, Koretzky G, et al. (1995) SH3 domain-mediated interaction of dystroglycan and Grb2. J Biol Chem 270: 20: 11711-11714.
    • (1995) J Biol Chem , vol.270 , Issue.20 , pp. 11711-11714
    • Yang, B.1    Jung, D.2    Motto, D.3    Meyer, J.4    Koretzky, G.5
  • 36
    • 0030991963 scopus 로고    scopus 로고
    • A role of dystroglycan in schwannoma cell adhesion to laminin
    • Matsumura K, Chiba A, Yamada H, Fukuta-Ohi H, Fujita S, et al. (1997) A role of dystroglycan in schwannoma cell adhesion to laminin. J Biol Chem 272: 21: 13904-13910.
    • (1997) J Biol Chem , vol.272 , Issue.21 , pp. 13904-13910
    • Matsumura, K.1    Chiba, A.2    Yamada, H.3    Fukuta-Ohi, H.4    Fujita, S.5
  • 37
    • 0037793365 scopus 로고    scopus 로고
    • Localization of phospho-beta-dystroglycan (pY892) to an intracellular vesicular compartment in cultured cells and skeletal muscle fibers in vivo
    • Sotgia F, Bonuccelli G, Bedford M, Brancaccio A, Mayer U, et al. (2003) Localization of phospho-beta-dystroglycan (pY892) to an intracellular vesicular compartment in cultured cells and skeletal muscle fibers in vivo. Biochemistry 42: 23: 7110-7123.
    • (2003) Biochemistry , vol.42 , Issue.23 , pp. 7110-7123
    • Sotgia, F.1    Bonuccelli, G.2    Bedford, M.3    Brancaccio, A.4    Mayer, U.5
  • 38
    • 0031563832 scopus 로고    scopus 로고
    • Rearrangements of the cytoskeleton and cell contacts induce process formation during differentiation of conditionally immortalized mouse podocyte cell lines
    • Mundel P, Reiser J, Zuniga Mejia Borja A, Pavenstadt H, Davidson GR, et al. (1997) Rearrangements of the cytoskeleton and cell contacts induce process formation during differentiation of conditionally immortalized mouse podocyte cell lines. Exp Cell Res 236: 1: 248-258.
    • (1997) Exp Cell Res , vol.236 , Issue.1 , pp. 248-258
    • Mundel, P.1    Reiser, J.2    Zuniga3    Mejia Borja, A.4    Pavenstadt, H.5    Davidson, G.R.6
  • 39
  • 40
    • 0029958839 scopus 로고    scopus 로고
    • Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor
    • Gesemann M, Cavalli V, Denzer AJ, Brancaccio A, Schumacher B, et al. (1996) Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor. Neuron 16: 4: 755-767.
    • (1996) Neuron , vol.16 , Issue.4 , pp. 755-767
    • Gesemann, M.1    Cavalli, V.2    Denzer, A.J.3    Brancaccio, A.4    Schumacher, B.5
  • 41
    • 0034600063 scopus 로고    scopus 로고
    • Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin
    • Tisi D, Talts JF, Timpl R, Hohenester E (2000) Structure of the C-terminal laminin G-like domain pair of the laminin alpha2 chain harbouring binding sites for alpha-dystroglycan and heparin. Embo J 19: 7: 1432-1440.
    • (2000) Embo J , vol.19 , Issue.7 , pp. 1432-1440
    • Tisi, D.1    Talts, J.F.2    Timpl, R.3    Hohenester, E.4
  • 42
    • 0034254083 scopus 로고    scopus 로고
    • Structure and function of laminin LG modules
    • Timpl R, Tisi D, Talts JF, Andac Z, Sasaki T, et al. (2000) Structure and function of laminin LG modules. Matrix Biol 19: 4: 309-317.
    • (2000) Matrix Biol , vol.19 , Issue.4 , pp. 309-317
    • Timpl, R.1    Tisi, D.2    Talts, J.F.3    Andac, Z.4    Sasaki, T.5
  • 43
    • 20844444136 scopus 로고    scopus 로고
    • Integrin-linked kinase in renal disease: Connecting cell-matrix interaction to the cytoskeleton
    • Blattner SM, Kretzler M (2005) Integrin-linked kinase in renal disease: connecting cell-matrix interaction to the cytoskeleton. Curr Opin Nephrol Hypertens 14: 4: 404-410.
    • (2005) Curr Opin Nephrol Hypertens , vol.14 , Issue.4 , pp. 404-410
    • Blattner, S.M.1    Kretzler, M.2
  • 44
    • 0037093539 scopus 로고    scopus 로고
    • Regulation of adhesive interaction between podocytes and glomerular basement membrane
    • Kretzler M (2002) Regulation of adhesive interaction between podocytes and glomerular basement membrane. Microsc Res Tech 57: 4: 247-253.
    • (2002) Microsc Res Tech , vol.57 , Issue.4 , pp. 247-253
    • Kretzler, M.1
  • 45
    • 0034532164 scopus 로고    scopus 로고
    • Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members
    • Sotgia F, Lee JK, Das K, Bedford M, Petrucci TC, et al. (2000) Caveolin-3 directly interacts with the C-terminal tail of beta -dystroglycan. Identification of a central WW-like domain within caveolin family members. J Biol Chem 275: 48: 38048-38058.
    • (2000) J Biol Chem , vol.275 , Issue.48 , pp. 38048-38058
    • Sotgia, F.1    Lee, J.K.2    Das, K.3    Bedford, M.4    Petrucci, T.C.5
  • 46
    • 0033037910 scopus 로고    scopus 로고
    • Association of the dystroglycan complex isolated from bovine brain synaptosomes with proteins involved in signal transduction
    • Cavaldesi M, Macchia G, Barca S, Defilippi P, Tarone G, et al. (1999) Association of the dystroglycan complex isolated from bovine brain synaptosomes with proteins involved in signal transduction. J Neurochem 72: 4: 1648-1655.
    • (1999) J Neurochem , vol.72 , Issue.4 , pp. 1648-1655
    • Cavaldesi, M.1    Macchia, G.2    Barca, S.3    Defilippi, P.4    Tarone, G.5
  • 47
    • 27744607526 scopus 로고    scopus 로고
    • Src-family kinases stabilize the neuromuscular synapse in vivo via protein interactions, phosphorylation, and cytoskeletal linkage of acetylcholine receptors
    • Sadasivam G, Willmann R, Lin S, Erb-Vogtli S, Kong XC, et al. (2005) Src-family kinases stabilize the neuromuscular synapse in vivo via protein interactions, phosphorylation, and cytoskeletal linkage of acetylcholine receptors. J Neurosci 25: 45: 10479-10493.
    • (2005) J Neurosci , vol.25 , Issue.45 , pp. 10479-10493
    • Sadasivam, G.1    Willmann, R.2    Lin, S.3    Erb-Vogtli, S.4    Kong, X.C.5
  • 48
    • 4344717288 scopus 로고    scopus 로고
    • Ezrin-dependent regulation of the actin cytoskeleton by beta-dystroglycan
    • Spence HJ, Chen YJ, Batchelor CL, Higginson JR, Suila H, et al. (2004) Ezrin-dependent regulation of the actin cytoskeleton by beta-dystroglycan. Hum Mol Genet 13: 15: 1657-1668.
    • (2004) Hum Mol Genet , vol.13 , Issue.15 , pp. 1657-1668
    • Spence, H.J.1    Chen, Y.J.2    Batchelor, C.L.3    Higginson, J.R.4    Suila, H.5
  • 49
    • 12444289493 scopus 로고    scopus 로고
    • Opposing roles of integrin alpha6-beta1 and dystroglycan in laminin-mediated extracellular signal-regulated kinase activation
    • Ferletta M, Kikkawa Y, Yu H, Talts JF, Durbeej M, et al. (2003) Opposing roles of integrin alpha6-beta1 and dystroglycan in laminin-mediated extracellular signal-regulated kinase activation. Mol Biol Cell 14: 5: 2088-20103.
    • (2003) Mol Biol Cell , vol.14 , Issue.5 , pp. 2088-20103
    • Ferletta, M.1    Kikkawa, Y.2    Yu, H.3    Talts, J.F.4    Durbeej, M.5
  • 50
    • 2942604709 scopus 로고    scopus 로고
    • Dystroglycan, a scaffold for the ERK-MAP kinase cascade
    • Spence HJ, Dhillon AS, James M, Winder SJ (2004) Dystroglycan, a scaffold for the ERK-MAP kinase cascade. EMBO Rep 5: 5: 484-489.
    • (2004) EMBO Rep , vol.5 , Issue.5 , pp. 484-489
    • Spence, H.J.1    Dhillon, A.S.2    James, M.3    Winder, S.J.4
  • 51
    • 48749089967 scopus 로고    scopus 로고
    • Genetic modifier screens reveal new components that interact with the Drosophila dystroglycan-dystrophin complex
    • Kucherenko MM, Pantoja M, Yatsenko AS, Shcherbata HR, Fischer KA, et al. (2008) Genetic modifier screens reveal new components that interact with the Drosophila dystroglycan-dystrophin complex. PLoS ONE 3: 6: e2418.
    • (2008) PLoS ONE , vol.3 , Issue.6
    • Kucherenko, M.M.1    Pantoja, M.2    Yatsenko, A.S.3    Shcherbata, H.R.4    Fischer, K.A.5
  • 52
    • 26944498336 scopus 로고    scopus 로고
    • Cultured podocytes establish a size-selective barrier regulated by specific signaling pathways and demonstrate synchronized barrier assembly in a calcium switch model of junction formation
    • Hunt JL, Pollak MR, Denker BM (2005) Cultured podocytes establish a size-selective barrier regulated by specific signaling pathways and demonstrate synchronized barrier assembly in a calcium switch model of junction formation. J Am Soc Nephrol 16: 6: 1593-1602.
    • (2005) J Am Soc Nephrol , vol.16 , Issue.6 , pp. 1593-1602
    • Hunt, J.L.1    Pollak, M.R.2    Denker, B.M.3
  • 53
    • 22844436647 scopus 로고    scopus 로고
    • TRPC6 is a glomerular slit diaphragm-associated channel required for normal renal function
    • Reiser J, Polu KR, Moller CC, Kenlan P, Altintas MM, et al. (2005) TRPC6 is a glomerular slit diaphragm-associated channel required for normal renal function. Nat Genet 37: 7: 739-744.
    • (2005) Nat Genet , vol.37 , Issue.7 , pp. 739-744
    • Reiser, J.1    Polu, K.R.2    Moller, C.C.3    Kenlan, P.4    Altintas, M.M.5
  • 54
    • 20844461826 scopus 로고    scopus 로고
    • A mutation in the TRPC6 cation channel causes familial focal segmental glomerulosclerosis
    • Winn MP, Conlon PJ, Lynn KL, Farrington MK, Creazzo T, et al. (2005) A mutation in the TRPC6 cation channel causes familial focal segmental glomerulosclerosis. Science 308: 5729: 1801-1804.
    • (2005) Science , vol.308 , Issue.5729 , pp. 1801-1804
    • Winn, M.P.1    Conlon, P.J.2    Lynn, K.L.3    Farrington, M.K.4    Creazzo, T.5
  • 55
    • 0034954343 scopus 로고    scopus 로고
    • Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton
    • Takeda T, McQuistan T, Orlando RA, Farquhar MG (2001) Loss of glomerular foot processes is associated with uncoupling of podocalyxin from the actin cytoskeleton. J Clin Invest 108: 2: 289-301.
    • (2001) J Clin Invest , vol.108 , Issue.2 , pp. 289-301
    • Takeda, T.1    McQuistan, T.2    Orlando, R.A.3    Farquhar, M.G.4
  • 56
    • 0032730835 scopus 로고    scopus 로고
    • Polycations induce calcium signaling in glomerular podocytes
    • Rudiger F, Greger R, Nitschke R, Henger A, Mundel P, et al. (1999) Polycations induce calcium signaling in glomerular podocytes. Kidney Int 56: 5: 1700-1709.
    • (1999) Kidney Int , vol.56 , Issue.5 , pp. 1700-1709
    • Rudiger, F.1    Greger, R.2    Nitschke, R.3    Henger, A.4    Mundel, P.5
  • 57
    • 3543098648 scopus 로고    scopus 로고
    • Podocyte flattening and disorder of glomerular basement membrane are associated with splitting of dystroglycan-matrix interaction
    • Kojima K, Davidovits A, Poczewski H, Langer B, Uchida S, et al. (2004) Podocyte flattening and disorder of glomerular basement membrane are associated with splitting of dystroglycan-matrix interaction. J Am Soc Nephrol 15: 8: 2079-2089.
    • (2004) J Am Soc Nephrol , vol.15 , Issue.8 , pp. 2079-2089
    • Kojima, K.1    Davidovits, A.2    Poczewski, H.3    Langer, B.4    Uchida, S.5
  • 58
    • 34548324281 scopus 로고    scopus 로고
    • Synaptopodin protects against proteinuria by disrupting Cdc42:IRSp53:-Mena signaling complexes in kidney podocytes
    • Yanagida-Asanuma E, Asanuma K, Kim K, Donnelly M, Young Choi H, et al. (2007) Synaptopodin protects against proteinuria by disrupting Cdc42:IRSp53:-Mena signaling complexes in kidney podocytes. Am J Pathol 171: 2: 415-427.
    • (2007) Am J Pathol , vol.171 , Issue.2 , pp. 415-427
    • Yanagida-Asanuma, E.1    Asanuma, K.2    Kim, K.3    Donnelly, M.4    Young Choi, H.5
  • 59
    • 0026067790 scopus 로고
    • Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma
    • Ohlendieck K, Ervasti JM, Snook JB, Campbell KP (1991) Dystrophin-glycoprotein complex is highly enriched in isolated skeletal muscle sarcolemma. J Cell Biol 112: 1: 135-148.
    • (1991) J Cell Biol , vol.112 , Issue.1 , pp. 135-148
    • Ohlendieck, K.1    Ervasti, J.M.2    Snook, J.B.3    Campbell, K.P.4
  • 60
    • 0037173670 scopus 로고    scopus 로고
    • Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies
    • Michele DE, Barresi R, Kanagawa M, Saito F, Cohn RD, et al. (2002) Post-translational disruption of dystroglycan-ligand interactions in congenital muscular dystrophies. Nature 418: 6896: 417-422.
    • (2002) Nature , vol.418 , Issue.6896 , pp. 417-422
    • Michele, D.E.1    Barresi, R.2    Kanagawa, M.3    Saito, F.4    Cohn, R.D.5
  • 61
    • 0021343351 scopus 로고
    • Measurement of cell numbers by means of the endogenous enzyme hexosaminidase. Applications to detection of lymphokines and cell surface antigens
    • Landegren U (1984) Measurement of cell numbers by means of the endogenous enzyme hexosaminidase. Applications to detection of lymphokines and cell surface antigens. J Immunol Methods 67: 2: 379-388.
    • (1984) J Immunol Methods , vol.67 , Issue.2 , pp. 379-388
    • Landegren, U.1
  • 62
    • 4644326685 scopus 로고    scopus 로고
    • Inhibition of mitochondrial Na+-Ca2+ exchange restores agonist-induced ATP production and Ca2+ handling in human complex I deficiency
    • Visch HJ, Rutter GA, Koopman WJ, Koenderink JB, Verkaart S, et al. (2004) Inhibition of mitochondrial Na+-Ca2+ exchange restores agonist-induced ATP production and Ca2+ handling in human complex I deficiency. J Biol Chem 279: 39: 40328-40336.
    • (2004) J Biol Chem , vol.279 , Issue.39 , pp. 40328-40336
    • Visch, H.J.1    Rutter, G.A.2    Koopman, W.J.3    Koenderink, J.B.4    Verkaart, S.5
  • 63
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 259: 680-685.
    • (1970) Nature , vol.227 , Issue.259 , pp. 680-685
    • Laemmli, U.K.1
  • 64
    • 0036667931 scopus 로고    scopus 로고
    • Inclusion of phosphatase inhibitors during Western blotting enhances signal detection with phospho-specific antibodies
    • Sharma SK, Carew TJ (2002) Inclusion of phosphatase inhibitors during Western blotting enhances signal detection with phospho-specific antibodies. Anal Biochem 307: 1: 187-189.
    • (2002) Anal Biochem , vol.307 , Issue.1 , pp. 187-189
    • Sharma, S.K.1    Carew, T.J.2
  • 65
    • 33744969296 scopus 로고    scopus 로고
    • Synaptopodin orchestrates actin organization and cell motility via regulation of RhoA signalling
    • Asanuma K, Yanagida-Asanuma E, Faul C, Tomino Y, Kim K, et al. (2006) Synaptopodin orchestrates actin organization and cell motility via regulation of RhoA signalling. Nat Cell Biol 8: 5: 485-491.
    • (2006) Nat Cell Biol , vol.8 , Issue.5 , pp. 485-491
    • Asanuma, K.1    Yanagida-Asanuma, E.2    Faul, C.3    Tomino, Y.4    Kim, K.5


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