메뉴 건너뛰기




Volumn 318, Issue 9, 2012, Pages 973-978

The glomerular basement membrane

Author keywords

Alport syndrome; Collagen IV; Laminin; Pierson syndrome

Indexed keywords

AGRIN; COLLAGEN TYPE 4; ENTACTIN; ENTACTIN 1; ENTACTIN 2; EPIDERMAL GROWTH FACTOR; GLYCOSAMINOGLYCAN; HEPARAN SULFATE; LAMININ; LAMININ ALPHA5; LAMININ BETA1; LAMININ BETA2; MESSENGER RNA; PERLECAN; UNCLASSIFIED DRUG;

EID: 84859814741     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2012.02.031     Document Type: Review
Times cited : (235)

References (43)
  • 2
    • 40049093240 scopus 로고    scopus 로고
    • It's not all about nephrin
    • Simons M., Huber T.B. It's not all about nephrin. Kidney Int. 2008, 73:671-673.
    • (2008) Kidney Int. , vol.73 , pp. 671-673
    • Simons, M.1    Huber, T.B.2
  • 3
    • 0016563163 scopus 로고
    • Editorial: The primary glomerular filtration barrier-basement membrane or epithelial slits?
    • Farquhar M.G. Editorial: The primary glomerular filtration barrier-basement membrane or epithelial slits?. Kidney Int. 1975, 8:197-211.
    • (1975) Kidney Int. , vol.8 , pp. 197-211
    • Farquhar, M.G.1
  • 5
    • 0024558106 scopus 로고
    • Structure and biological activity of basement membrane proteins
    • Timpl R. Structure and biological activity of basement membrane proteins. Eur. J. Biochem. 1989, 180:487-502.
    • (1989) Eur. J. Biochem. , vol.180 , pp. 487-502
    • Timpl, R.1
  • 7
    • 78751526814 scopus 로고    scopus 로고
    • Characterization of the laminin gene family and evolution in zebrafish
    • Sztal T., Berger S., Currie P.D., Hall T.E. Characterization of the laminin gene family and evolution in zebrafish. Dev. Dyn. 2011, 240:422-431.
    • (2011) Dev. Dyn. , vol.240 , pp. 422-431
    • Sztal, T.1    Berger, S.2    Currie, P.D.3    Hall, T.E.4
  • 8
    • 34547093441 scopus 로고    scopus 로고
    • Role of laminin terminal globular domains in basement membrane assembly
    • McKee K.K., Harrison D., Capizzi S., Yurchenco P.D. Role of laminin terminal globular domains in basement membrane assembly. J. Biol. Chem. 2007, 282:21437-21447.
    • (2007) J. Biol. Chem. , vol.282 , pp. 21437-21447
    • McKee, K.K.1    Harrison, D.2    Capizzi, S.3    Yurchenco, P.D.4
  • 9
    • 0031963693 scopus 로고    scopus 로고
    • Developmental biology of glomerular basement membrane components
    • Miner J.H. Developmental biology of glomerular basement membrane components. Curr. Opin. Nephrol. Hypertens. 1998, 7:13-19.
    • (1998) Curr. Opin. Nephrol. Hypertens. , vol.7 , pp. 13-19
    • Miner, J.H.1
  • 10
    • 0030919488 scopus 로고    scopus 로고
    • The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform
    • Miner J.H., Patton B.L., Lentz S.I., Gilbert D.J., Snider W.D., Jenkins N.A., Copeland N.G., Sanes J.R. The laminin alpha chains: expression, developmental transitions, and chromosomal locations of alpha1-5, identification of heterotrimeric laminins 8-11, and cloning of a novel alpha3 isoform. J. Cell Biol. 1997, 137:685-701.
    • (1997) J. Cell Biol. , vol.137 , pp. 685-701
    • Miner, J.H.1    Patton, B.L.2    Lentz, S.I.3    Gilbert, D.J.4    Snider, W.D.5    Jenkins, N.A.6    Copeland, N.G.7    Sanes, J.R.8
  • 11
    • 0028171098 scopus 로고
    • Collagen IV α3, α4, and α5 chains in rodent basal laminae: sequence, distribution, association with laminins, and developmental switches
    • Miner J.H., Sanes J.R. Collagen IV α3, α4, and α5 chains in rodent basal laminae: sequence, distribution, association with laminins, and developmental switches. J. Cell Biol. 1994, 127:879-891.
    • (1994) J. Cell Biol. , vol.127 , pp. 879-891
    • Miner, J.H.1    Sanes, J.R.2
  • 12
    • 0034650304 scopus 로고    scopus 로고
    • Defective glomerulogenesis in the absence of laminin α5 demonstrates a developmental role for the kidney glomerular basement membrane
    • Miner J.H., Li C. Defective glomerulogenesis in the absence of laminin α5 demonstrates a developmental role for the kidney glomerular basement membrane. Dev. Biol. 2000, 217:278-289.
    • (2000) Dev. Biol. , vol.217 , pp. 278-289
    • Miner, J.H.1    Li, C.2
  • 13
    • 0033545239 scopus 로고    scopus 로고
    • Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation
    • Smyth N., Vatansever H.S., Murray P., Meyer M., Frie C., Paulsson M., Edgar D. Absence of basement membranes after targeting the LAMC1 gene results in embryonic lethality due to failure of endoderm differentiation. J. Cell Biol. 1999, 144:151-160.
    • (1999) J. Cell Biol. , vol.144 , pp. 151-160
    • Smyth, N.1    Vatansever, H.S.2    Murray, P.3    Meyer, M.4    Frie, C.5    Paulsson, M.6    Edgar, D.7
  • 14
    • 33745866295 scopus 로고    scopus 로고
    • A hypomorphic mutation in the mouse laminin alpha5 gene (Lama5) causes polycystic kidney disease
    • Shannon M.B., Patton B.L., Harvey S.J., Miner J.H. A hypomorphic mutation in the mouse laminin alpha5 gene (Lama5) causes polycystic kidney disease. J. Am. Soc. Nephrol. 2006, 17:1913-1922.
    • (2006) J. Am. Soc. Nephrol. , vol.17 , pp. 1913-1922
    • Shannon, M.B.1    Patton, B.L.2    Harvey, S.J.3    Miner, J.H.4
  • 16
    • 0029127384 scopus 로고
    • The renal glomerulus of mice lacking s-laminin/laminin beta2: nephrosis despite molecular compensation by laminin beta1
    • Noakes P.G., Miner J.H., Gautam M., Cunningham J.M., Sanes J.R., Merlie J.P. The renal glomerulus of mice lacking s-laminin/laminin beta2: nephrosis despite molecular compensation by laminin beta1. Nat. Genet. 1995, 10:400-406.
    • (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
  • 17
    • 33746730496 scopus 로고    scopus 로고
    • Proteinuria precedes podocyte abnormalities in Lamb2-/- mice, implicating the glomerular basement membrane as an albumin barrier
    • Jarad G., Cunningham J., Shaw A.S., Miner J.H. Proteinuria precedes podocyte abnormalities in Lamb2-/- mice, implicating the glomerular basement membrane as an albumin barrier. J. Clin. Invest. 2006, 116:2272-2279.
    • (2006) J. Clin. Invest. , vol.116 , pp. 2272-2279
    • Jarad, G.1    Cunningham, J.2    Shaw, A.S.3    Miner, J.H.4
  • 18
    • 80053057998 scopus 로고    scopus 로고
    • Forced expression of laminin {beta}1 in podocytes prevents nephrotic syndrome in mice lacking laminin {beta}2, a model for Pierson syndrome
    • Suh J.H., Jarad G., Vandevoorde R.G., Miner J.H. Forced expression of laminin {beta}1 in podocytes prevents nephrotic syndrome in mice lacking laminin {beta}2, a model for Pierson syndrome. Proc. Natl. Acad. Sci. U. S. A. 2011, 108:15348-15353.
    • (2011) Proc. Natl. Acad. Sci. U. S. A. , vol.108 , pp. 15348-15353
    • Suh, J.H.1    Jarad, G.2    Vandevoorde, R.G.3    Miner, J.H.4
  • 19
    • 1842482987 scopus 로고    scopus 로고
    • Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development
    • Poschl E., Schlotzer-Schrehardt U., Brachvogel B., Saito K., Ninomiya Y., Mayer U. Collagen IV is essential for basement membrane stability but dispensable for initiation of its assembly during early development. Development 2004, 131:1619-1628.
    • (2004) Development , vol.131 , pp. 1619-1628
    • Poschl, E.1    Schlotzer-Schrehardt, U.2    Brachvogel, B.3    Saito, K.4    Ninomiya, Y.5    Mayer, U.6
  • 23
    • 0027378858 scopus 로고
    • The alpha 1 beta 1 integrin recognition site of the basement membrane collagen molecule [alpha 1(IV)]2 alpha 2(IV)
    • Eble J.A., Golbik R., Mann K., Kuhn K. The alpha 1 beta 1 integrin recognition site of the basement membrane collagen molecule [alpha 1(IV)]2 alpha 2(IV). EMBO J. 1993, 12:4795-4802.
    • (1993) EMBO J. , vol.12 , pp. 4795-4802
    • Eble, J.A.1    Golbik, R.2    Mann, K.3    Kuhn, K.4
  • 29
    • 0036785584 scopus 로고    scopus 로고
    • Gene structure and functional analysis of the mouse nidogen-2 gene: nidogen-2 is not essential for basement membrane formation in mice
    • Schymeinsky J., Nedbal S., Miosge N., Poschl E., Rao C., Beier D.R., Skarnes W.C., Timpl R., Bader B.L. Gene structure and functional analysis of the mouse nidogen-2 gene: nidogen-2 is not essential for basement membrane formation in mice. Mol. Cell. Biol. 2002, 22:6820-6830.
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 6820-6830
    • Schymeinsky, J.1    Nedbal, S.2    Miosge, N.3    Poschl, E.4    Rao, C.5    Beier, D.R.6    Skarnes, W.C.7    Timpl, R.8    Bader, B.L.9
  • 30
    • 0036860601 scopus 로고    scopus 로고
    • Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice
    • Miosge N., Sasaki T., Timpl R. Evidence of nidogen-2 compensation for nidogen-1 deficiency in transgenic mice. Matrix Biol. 2002, 21:611-621.
    • (2002) Matrix Biol. , vol.21 , pp. 611-621
    • Miosge, N.1    Sasaki, T.2    Timpl, R.3
  • 33
    • 0033137032 scopus 로고    scopus 로고
    • Alternatively spliced isoforms of nerve- and muscle-derived agrin: their roles at the neuromuscular junction
    • Burgess R.W., Nguyen Q.T., Son Y.J., Lichtman J.W., Sanes J.R. Alternatively spliced isoforms of nerve- and muscle-derived agrin: their roles at the neuromuscular junction. Neuron 1999, 23:33-44.
    • (1999) Neuron , vol.23 , pp. 33-44
    • Burgess, R.W.1    Nguyen, Q.T.2    Son, Y.J.3    Lichtman, J.W.4    Sanes, J.R.5
  • 34
    • 0034597091 scopus 로고    scopus 로고
    • Agrin isoforms with distinct amino termini: differential expression, localization, and function
    • Burgess R.W., Skarnes W.C., Sanes J.R. Agrin isoforms with distinct amino termini: differential expression, localization, and function. J. Cell Biol. 2000, 151:41-52.
    • (2000) J. Cell Biol. , vol.151 , pp. 41-52
    • Burgess, R.W.1    Skarnes, W.C.2    Sanes, J.R.3
  • 35
    • 65549164330 scopus 로고    scopus 로고
    • Transmembrane form agrin-induced process formation requires lipid rafts and the activation of Fyn and MAPK
    • Ramseger R., White R., Kroger S. Transmembrane form agrin-induced process formation requires lipid rafts and the activation of Fyn and MAPK. J. Biol. Chem. 2009, 284:7697-7705.
    • (2009) J. Biol. Chem. , vol.284 , pp. 7697-7705
    • Ramseger, R.1    White, R.2    Kroger, S.3
  • 36
    • 34547669237 scopus 로고    scopus 로고
    • Contribution of proteoglycans towards the integrated functions of renal glomerular capillaries. A historical perspective
    • Kanwar Y.S., Danesh F.R., Chugh S.S. Contribution of proteoglycans towards the integrated functions of renal glomerular capillaries. A historical perspective. Am. J. Pathol. 2007, 171:9-13.
    • (2007) Am. J. Pathol. , vol.171 , pp. 9-13
    • Kanwar, Y.S.1    Danesh, F.R.2    Chugh, S.S.3
  • 39
    • 67651089928 scopus 로고    scopus 로고
    • Glomerular filtration is normal in the absence of both agrin and perlecan-heparan sulfate from the glomerular basement membrane
    • Goldberg S., Harvey S.J., Cunningham J., Tryggvason K., Miner J.H. Glomerular filtration is normal in the absence of both agrin and perlecan-heparan sulfate from the glomerular basement membrane. Nephrol. Dial. Transplant. 2009, 24:2044-2051.
    • (2009) Nephrol. Dial. Transplant. , vol.24 , pp. 2044-2051
    • Goldberg, S.1    Harvey, S.J.2    Cunningham, J.3    Tryggvason, K.4    Miner, J.H.5
  • 41
    • 80053376935 scopus 로고    scopus 로고
    • Reduced diffusion of charge modified, conformationally intact anionic Ficoll relative to neutral Ficoll across the rat glomerular filtration barrier in vivo
    • Axelsson J., Sverrisson K., Rippe A., Fissell W., Rippe B. Reduced diffusion of charge modified, conformationally intact anionic Ficoll relative to neutral Ficoll across the rat glomerular filtration barrier in vivo. Am. J. Physiol. Renal Physiol. 2011, 301:F708-F712.
    • (2011) Am. J. Physiol. Renal Physiol. , vol.301
    • Axelsson, J.1    Sverrisson, K.2    Rippe, A.3    Fissell, W.4    Rippe, B.5
  • 42
    • 42149122041 scopus 로고    scopus 로고
    • Properties of the glomerular barrier and mechanisms of proteinuria
    • Haraldsson B., Nystrom J., Deen W.M. Properties of the glomerular barrier and mechanisms of proteinuria. Physiol. Rev. 2008, 88:451-487.
    • (2008) Physiol. Rev. , vol.88 , pp. 451-487
    • Haraldsson, B.1    Nystrom, J.2    Deen, W.M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.