메뉴 건너뛰기




Volumn 20, Issue 23, 2011, Pages 4617-4633

A valid mouse model of AGRIN-associated congenital myasthenic syndrome

Author keywords

[No Author keywords available]

Indexed keywords

AGRIN; CHOLINERGIC RECEPTOR; MUTANT PROTEIN; PHENYLALANINE; PROTEOGLYCAN; SERINE;

EID: 81255209222     PISSN: 09646906     EISSN: 14602083     Source Type: Journal    
DOI: 10.1093/hmg/ddr396     Document Type: Article
Times cited : (36)

References (69)
  • 1
    • 13844290518 scopus 로고    scopus 로고
    • Chapter: 66 Congenital Myasthenic Syndrome
    • Engel, A.G. and Franzini-Armstrong, C. (eds), 3rd edn. McGraw-Hill, New York
    • Engel, A.G., Ohno, K. and Sine, S.M. (2004) Chapter 66: Congenital Myasthenic Syndrome. In Engel, A.G. and Franzini-Armstrong, C. (eds), Myology. 3rd edn. McGraw-Hill, New York, Vol. 2, pp. 1801-1854.
    • (2004) Myology , vol.2 , pp. 1801-1854
    • Engel, A.G.1    Ohno, K.2    Sine, S.M.3
  • 2
    • 0032936983 scopus 로고    scopus 로고
    • Development of the vertebrate neuromuscular junction
    • Sanes, J.R. and Lichtman, J.W. (1999) Development of the vertebrate neuromuscular junction. Ann. Rev. Neurosci., 22, 389-442.
    • (1999) Ann. Rev. Neurosci. , vol.22 , pp. 389-442
    • Sanes, J.R.1    Lichtman, J.W.2
  • 3
    • 0036891517 scopus 로고    scopus 로고
    • Building the vertebrate neuromuscular synapse
    • Burden, S.J. (2002) Building the vertebrate neuromuscular synapse. J. Neurobiol., 53, 501-511.
    • (2002) J. Neurobiol. , vol.53 , pp. 501-511
    • Burden, S.J.1
  • 4
    • 32344447256 scopus 로고    scopus 로고
    • Assembly of the postsynaptic membrane at the neuromuscular junction: paradigm lost
    • Kummer, T.T., Misgeld, T. and Sanes, J.R. (2006) Assembly of the postsynaptic membrane at the neuromuscular junction: paradigm lost. Curr. Opin. Neurobiol., 16, 74-82.
    • (2006) Curr. Opin. Neurobiol. , vol.16 , pp. 74-82
    • Kummer, T.T.1    Misgeld, T.2    Sanes, J.R.3
  • 6
    • 0030854507 scopus 로고    scopus 로고
    • Agrin-induced postsynaptic-like apparatus in skeletal muscle fibers in vivo
    • Cohen, I., Rimer, M., Lomo, T. and McMahan, U.J. (1997) Agrin-induced postsynaptic-like apparatus in skeletal muscle fibers in vivo. Mol. Cell Neurosci., 9, 237-253.
    • (1997) Mol. Cell Neurosci. , vol.9 , pp. 237-253
    • Cohen, I.1    Rimer, M.2    Lomo, T.3    McMahan, U.J.4
  • 7
    • 0026652948 scopus 로고
    • RNA splicing regulates agrin-mediated acetylcholine receptor clustering activity on cultured myotubes
    • Ferns, M., Hoch, W., Campanelli, J.T., Rupp, F., Hall, Z.W. and Scheller, R.H. (1992) RNA splicing regulates agrin-mediated acetylcholine receptor clustering activity on cultured myotubes. Neuron, 8, 1079-1086.
    • (1992) Neuron , vol.8 , pp. 1079-1086
    • Ferns, M.1    Hoch, W.2    Campanelli, J.T.3    Rupp, F.4    Hall, Z.W.5    Scheller, R.H.6
  • 8
    • 0027369903 scopus 로고
    • Developmental regulation of highly active alternatively spliced forms of agrin
    • Hoch, W., Ferns, M., Campanelli, J.T., Hall, Z.W. and Scheller, R.H. (1993) Developmental regulation of highly active alternatively spliced forms of agrin. Neuron, 11, 479-490.
    • (1993) Neuron , vol.11 , pp. 479-490
    • Hoch, W.1    Ferns, M.2    Campanelli, J.T.3    Hall, Z.W.4    Scheller, R.H.5
  • 9
    • 0027517961 scopus 로고
    • The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans
    • Ferns, M.J., Campanelli, J.T., Hoch, W., Scheller, R.H. and Hall, Z. (1993) The ability of agrin to cluster AChRs depends on alternative splicing and on cell surface proteoglycans. Neuron, 11, 491-502.
    • (1993) Neuron , vol.11 , pp. 491-502
    • Ferns, M.J.1    Campanelli, J.T.2    Hoch, W.3    Scheller, R.H.4    Hall, Z.5
  • 13
  • 14
    • 0035154191 scopus 로고    scopus 로고
    • An alternative amino-terminus expressed in the central nervous system converts agrin to a type II transmembrane protein
    • Neumann, F.R., Bittcher, G., Annies, M., Schumacher, B., Kroger, S. and Ruegg, M.A. (2001) An alternative amino-terminus expressed in the central nervous system converts agrin to a type II transmembrane protein. Mol. Cell Neurosci., 17, 208-225.
    • (2001) Mol. Cell Neurosci. , vol.17 , pp. 208-225
    • Neumann, F.R.1    Bittcher, G.2    Annies, M.3    Schumacher, B.4    Kroger, S.5    Ruegg, M.A.6
  • 15
    • 0034597091 scopus 로고    scopus 로고
    • Agrin isoforms with distinct amino termini: differential expression, localization, and function
    • Burgess, R.W., Skarnes, W.C. and Sanes, J.R. (2000) Agrin isoforms with distinct amino termini: differential expression, localization, and function. J. Cell Biol., 151, 41-52.
    • (2000) J. Cell Biol. , vol.151 , pp. 41-52
    • Burgess, R.W.1    Skarnes, W.C.2    Sanes, J.R.3
  • 16
    • 0035953645 scopus 로고    scopus 로고
    • Distinct roles of nerve and muscle in postsynaptic differentiation of the neuromuscular synapse
    • Lin, W., Burgess, R.W., Dominguez, B., Pfaff, S.L., Sanes, J.R. and Lee, K.F. (2001) Distinct roles of nerve and muscle in postsynaptic differentiation of the neuromuscular synapse. Nature, 410, 1057-1064.
    • (2001) Nature , vol.410 , pp. 1057-1064
    • Lin, W.1    Burgess, R.W.2    Dominguez, B.3    Pfaff, S.L.4    Sanes, J.R.5    Lee, K.F.6
  • 18
    • 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. and Sanes, J.R. (1999) Alternatively spliced isoforms of nerve- and muscle-derived agrin: their roles at the neuromuscular junction. Neuron, 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
  • 19
    • 33846155569 scopus 로고    scopus 로고
    • LDL-receptor-related protein 4 is crucial for formation of the neuromuscular junction
    • Weatherbee, S.D., Anderson, K.V. and Niswander, L.A. (2006) LDL-receptor-related protein 4 is crucial for formation of the neuromuscular junction. Development, 133, 4993-5000.
    • (2006) Development , vol.133 , pp. 4993-5000
    • Weatherbee, S.D.1    Anderson, K.V.2    Niswander, L.A.3
  • 24
    • 0035105784 scopus 로고    scopus 로고
    • Auto-antibodies to the receptor tyrosine kinase MuSK in patients with myasthenia gravis without acetylcholine receptor antibodies
    • Hoch, W., McConville, J., Helms, S., Newsom-Davis, J., Melms, A. and Vincent, A. (2001) Auto-antibodies to the receptor tyrosine kinase MuSK in patients with myasthenia gravis without acetylcholine receptor antibodies. Nat. Med., 7, 365-368.
    • (2001) Nat. Med. , vol.7 , pp. 365-368
    • Hoch, W.1    McConville, J.2    Helms, S.3    Newsom-Davis, J.4    Melms, A.5    Vincent, A.6
  • 27
    • 33748545328 scopus 로고    scopus 로고
    • An active dominant mutation of glycyl-tRNA synthetase causes neuropathy in a Charcot-Marie-Tooth 2D mouse model
    • Seburn, K.L., Nangle, L.A., Cox, G.A., Schimmel, P. and Burgess, R.W. (2006) An active dominant mutation of glycyl-tRNA synthetase causes neuropathy in a Charcot-Marie-Tooth 2D mouse model. Neuron, 51, 715-726.
    • (2006) Neuron , vol.51 , pp. 715-726
    • Seburn, K.L.1    Nangle, L.A.2    Cox, G.A.3    Schimmel, P.4    Burgess, R.W.5
  • 28
    • 46249110939 scopus 로고    scopus 로고
    • A single point mutation in the LN domain of LAMA2 causes muscular dystrophy and peripheral amyelination
    • Patton, B.L., Wang, B., Tarumi, Y.S., Seburn, K.L. and Burgess, R.W. (2008) A single point mutation in the LN domain of LAMA2 causes muscular dystrophy and peripheral amyelination. J. Cell Sci., 121, 1593-1604.
    • (2008) J. Cell Sci. , vol.121 , pp. 1593-1604
    • Patton, B.L.1    Wang, B.2    Tarumi, Y.S.3    Seburn, K.L.4    Burgess, R.W.5
  • 29
    • 70349773389 scopus 로고    scopus 로고
    • An ENU-induced mutation in mouse glycyl-tRNA synthetase (GARS) causes peripheral sensory and motor phenotypes creating a model of Charcot-Marie-Tooth type 2D peripheral neuropathy
    • Achilli, F., Bros-Facer, V., Williams, H.P., Banks, G.T., AlQatari, M., Chia, R., Tucci, V., Groves, M., Nickols, C.D., Seburn, K.L. et al. (2009) An ENU-induced mutation in mouse glycyl-tRNA synthetase (GARS) causes peripheral sensory and motor phenotypes creating a model of Charcot-Marie-Tooth type 2D peripheral neuropathy. Dis. Model Mech., 2, 359-373.
    • (2009) Dis. Model Mech. , vol.2 , pp. 359-373
    • Achilli, F.1    Bros-Facer, V.2    Williams, H.P.3    Banks, G.T.4    AlQatari, M.5    Chia, R.6    Tucci, V.7    Groves, M.8    Nickols, C.D.9    Seburn, K.L.10
  • 30
    • 33846924789 scopus 로고    scopus 로고
    • Defects in eye development in transgenic mice overexpressing the heparan sulfate proteoglycan agrin
    • Fuerst, P.G., Rauch, S.M. and Burgess, R.W. (2007) Defects in eye development in transgenic mice overexpressing the heparan sulfate proteoglycan agrin. Dev. Biol., 303, 165-180.
    • (2007) Dev. Biol. , vol.303 , pp. 165-180
    • Fuerst, P.G.1    Rauch, S.M.2    Burgess, R.W.3
  • 31
    • 0029013157 scopus 로고
    • The SEA module: a new extracellular domain associated with O-glycosylation
    • Bork, P. and Patthy, L. (1995) The SEA module: a new extracellular domain associated with O-glycosylation. Prot. Sci., 4, 1421-1425.
    • (1995) Prot. Sci. , vol.4 , pp. 1421-1425
    • Bork, P.1    Patthy, L.2
  • 34
    • 0242500302 scopus 로고    scopus 로고
    • Molecular organization of the extraocular muscle neuromuscular junction: partial conservation of and divergence from the skeletal muscle prototype
    • Khanna, S., Richmonds, C.R., Kaminski, H.J. and Porter, J.D. (2003) Molecular organization of the extraocular muscle neuromuscular junction: partial conservation of and divergence from the skeletal muscle prototype. Invest. Ophth. Vis. Sci., 44, 1918-1926.
    • (2003) Invest. Ophth. Vis. Sci. , vol.44 , pp. 1918-1926
    • Khanna, S.1    Richmonds, C.R.2    Kaminski, H.J.3    Porter, J.D.4
  • 35
    • 0027313159 scopus 로고
    • Evidence for compartmental identity in the development of the rat lateral gastrocnemius muscle
    • Gatesy, S.M. and English, A.W. (1993) Evidence for compartmental identity in the development of the rat lateral gastrocnemius muscle. Dev. Dyn., 196, 174-182.
    • (1993) Dev. Dyn. , vol.196 , pp. 174-182
    • Gatesy, S.M.1    English, A.W.2
  • 36
    • 67349164383 scopus 로고    scopus 로고
    • A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice
    • Saxena, S., Cabuy, E. and Caroni, P. (2009) A role for motoneuron subtype-selective ER stress in disease manifestations of FALS mice. Nat. Neurosci., 12, 627-636.
    • (2009) Nat. Neurosci. , vol.12 , pp. 627-636
    • Saxena, S.1    Cabuy, E.2    Caroni, P.3
  • 37
    • 33344462702 scopus 로고    scopus 로고
    • Selective vulnerability and pruning of phasic motoneuron axons in motoneuron disease alleviated by CNTF
    • Pun, S., Santos, A.F., Saxena, S., Xu, L. and Caroni, P. (2006) Selective vulnerability and pruning of phasic motoneuron axons in motoneuron disease alleviated by CNTF. Nat. Neurosci., 9, 408-419.
    • (2006) Nat. Neurosci. , vol.9 , pp. 408-419
    • Pun, S.1    Santos, A.F.2    Saxena, S.3    Xu, L.4    Caroni, P.5
  • 44
    • 0029050847 scopus 로고
    • Failure of postsynaptic specialization to develop at neuromuscular junctions of rapsyn-deficient mice
    • Gautam, M., Noakes, P.G., Mudd, J., Nichol, M., Chu, G., Sanes, J.A. and Merlie, J. (1995) Failure of postsynaptic specialization to develop at neuromuscular junctions of rapsyn-deficient mice. Nature, 377, 232-236.
    • (1995) Nature , vol.377 , pp. 232-236
    • Gautam, M.1    Noakes, P.G.2    Mudd, J.3    Nichol, M.4    Chu, G.5    Sanes, J.A.6    Merlie, J.7
  • 46
    • 0028897167 scopus 로고
    • Acetylcholine receptor-aggregating activity of agrin isoforms and mapping of the active site
    • Gesemann, M., Denzer, A.J. and Ruegg, M.A. (1995) Acetylcholine receptor-aggregating activity of agrin isoforms and mapping of the active site. J. Cell Biol., 128, 625-636.
    • (1995) J. Cell Biol. , vol.128 , pp. 625-636
    • Gesemann, M.1    Denzer, A.J.2    Ruegg, M.A.3
  • 48
    • 38949156757 scopus 로고    scopus 로고
    • SEA domain proteolysis determines the functional composition of dystroglycan
    • Akhavan, A., Crivelli, S.N., Singh, M., Lingappa, V.R. and Muschler, J.L. (2008) SEA domain proteolysis determines the functional composition of dystroglycan. FASEB J., 22, 612-621.
    • (2008) FASEB J , vol.22 , pp. 612-621
    • Akhavan, A.1    Crivelli, S.N.2    Singh, M.3    Lingappa, V.R.4    Muschler, J.L.5
  • 49
    • 20444445503 scopus 로고    scopus 로고
    • The role of the SEA (sea urchin sperm protein, enterokinase and agrin) module in cleavage of membrane-tethered mucins
    • Palmai-Pallag, T., Khodabukus, N., Kinarsky, L., Leir, S.H., Sherman, S., Hollingsworth, M.A. and Harris, A. (2005) The role of the SEA (sea urchin sperm protein, enterokinase and agrin) module in cleavage of membrane-tethered mucins. FEBS J., 272, 2901-2911.
    • (2005) FEBS J , vol.272 , pp. 2901-2911
    • Palmai-Pallag, T.1    Khodabukus, N.2    Kinarsky, L.3    Leir, S.H.4    Sherman, S.5    Hollingsworth, M.A.6    Harris, A.7
  • 51
    • 30044448792 scopus 로고    scopus 로고
    • Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin
    • Macao, B., Johansson, D.G., Hansson, G.C. and Hard, T. (2006) Autoproteolysis coupled to protein folding in the SEA domain of the membrane-bound MUC1 mucin. Nat. Struct. Mol. Biol., 13, 71-76.
    • (2006) Nat. Struct. Mol. Biol. , vol.13 , pp. 71-76
    • Macao, B.1    Johansson, D.G.2    Hansson, G.C.3    Hard, T.4
  • 52
    • 0031041170 scopus 로고    scopus 로고
    • Identification of sites in domain I of perlecan that regulate heparan sulfate synthesis
    • Dolan, M., Horchar, T., Rigatti, B. and Hassell, J.R. (1997) Identification of sites in domain I of perlecan that regulate heparan sulfate synthesis. J. Biol. Chem., 272, 4316-4322.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4316-4322
    • Dolan, M.1    Horchar, T.2    Rigatti, B.3    Hassell, J.R.4
  • 53
    • 0034091912 scopus 로고    scopus 로고
    • Matrix metalloproteinase-3 removes agrin from synaptic basal lamina
    • VanSaun, M. and Werle, M.J. (2000) Matrix metalloproteinase-3 removes agrin from synaptic basal lamina. J. Neurobiol., 43, 140-149.
    • (2000) J. Neurobiol. , vol.43 , pp. 140-149
    • VanSaun, M.1    Werle, M.J.2
  • 54
    • 3442883363 scopus 로고    scopus 로고
    • Structural alterations at the neuromuscular junctions of matrix metalloproteinase 3 null mutant mice
    • VanSaun, M., Herrera, A.A. and Werle, M.J. (2003) Structural alterations at the neuromuscular junctions of matrix metalloproteinase 3 null mutant mice. J. Neurocytol., 32, 1129-1142.
    • (2003) J. Neurocytol. , vol.32 , pp. 1129-1142
    • VanSaun, M.1    Herrera, A.A.2    Werle, M.J.3
  • 55
    • 3042576001 scopus 로고    scopus 로고
    • Activity dependent removal of agrin from synaptic basal lamina by matrix metalloproteinase 3
    • Werle, M.J. and VanSaun, M. (2003) Activity dependent removal of agrin from synaptic basal lamina by matrix metalloproteinase 3. J. Neurocytol., 32, 905-913.
    • (2003) J. Neurocytol. , vol.32 , pp. 905-913
    • Werle, M.J.1    VanSaun, M.2
  • 56
    • 0036252145 scopus 로고    scopus 로고
    • Modulation of agrin binding and activity by the CT and related carbohydrate antigens
    • Xia, B. and Martin, P.T. (2002) Modulation of agrin binding and activity by the CT and related carbohydrate antigens. Mol. Cell Neurosci., 19, 539-551.
    • (2002) Mol. Cell Neurosci. , vol.19 , pp. 539-551
    • Xia, B.1    Martin, P.T.2
  • 57
    • 77449125821 scopus 로고    scopus 로고
    • Neuromuscular disease models and analysis
    • Burgess, R.W., Cox, G.A. and Seburn, K.L. (2010) Neuromuscular disease models and analysis. Methods Mol. Biol., 602, 347-393.
    • (2010) Methods Mol. Biol. , vol.602 , pp. 347-393
    • Burgess, R.W.1    Cox, G.A.2    Seburn, K.L.3
  • 58
    • 0037835964 scopus 로고    scopus 로고
    • Expression of mouse agrin in normal, denervated and dystrophic muscle
    • Eusebio, A., Oliveri, F., Barzaghi, P. and Ruegg, M.A. (2003) Expression of mouse agrin in normal, denervated and dystrophic muscle. Neuromuscul. Disord., 13, 408-415.
    • (2003) Neuromuscul. Disord. , vol.13 , pp. 408-415
    • Eusebio, A.1    Oliveri, F.2    Barzaghi, P.3    Ruegg, M.A.4
  • 60
    • 0027320778 scopus 로고
    • 'Cold SSCP': a simple, rapid and non-radioactive method for optimized single-strand conformation polymorphism analyses
    • Hongyo, T., Buzard, G.S., Calvert, R.J. and Weghorst, C.M. (1993) 'Cold SSCP': a simple, rapid and non-radioactive method for optimized single-strand conformation polymorphism analyses. Nucleic Acids Res., 21, 3637-3642.
    • (1993) Nucleic Acids Res , vol.21 , pp. 3637-3642
    • Hongyo, T.1    Buzard, G.S.2    Calvert, R.J.3    Weghorst, C.M.4
  • 61
    • 0030699217 scopus 로고    scopus 로고
    • High resolution single strand conformation polymorphism analysis using formamide and ethidium bromide staining
    • Xie, T., Ho, S.L. and Ma, O.C. (1997) High resolution single strand conformation polymorphism analysis using formamide and ethidium bromide staining. Mol. Pathol., 50, 276-278.
    • (1997) Mol. Pathol. , vol.50 , pp. 276-278
    • Xie, T.1    Ho, S.L.2    Ma, O.C.3
  • 63
    • 77954385137 scopus 로고    scopus 로고
    • Induction of filopodia-like protrusions by transmembrane agrin: role of agrin glycosaminoglycan chains and Rho-family GTPases
    • Lin, L., McCroskery, S., Ross, J.M., Chak, Y., Neuhuber, B. and Daniels, M.P. (2010) Induction of filopodia-like protrusions by transmembrane agrin: role of agrin glycosaminoglycan chains and Rho-family GTPases. Exp. Cell Res., 316, 2260-2277.
    • (2010) Exp. Cell Res. , vol.316 , pp. 2260-2277
    • Lin, L.1    McCroskery, S.2    Ross, J.M.3    Chak, Y.4    Neuhuber, B.5    Daniels, M.P.6
  • 64
    • 0034581176 scopus 로고    scopus 로고
    • Alkaline phosphatase fusions of ligands or receptors as in situ probes for staining of cells, tissues, and embryos
    • Flanagan, J.G., Cheng, H.J., Feldheim, D.A., Hattori, M., Lu, Q. and Vanderhaeghen, P. (2000) Alkaline phosphatase fusions of ligands or receptors as in situ probes for staining of cells, tissues, and embryos. Methods Enzymol., 327, 19-35.
    • (2000) Methods Enzymol , vol.327 , pp. 19-35
    • Flanagan, J.G.1    Cheng, H.J.2    Feldheim, D.A.3    Hattori, M.4    Lu, Q.5    Vanderhaeghen, P.6
  • 67
    • 65449188232 scopus 로고    scopus 로고
    • Jalview Version 2-a multiple sequence alignment editor and analysis workbench
    • Waterhouse, A.M., Procter, J.B., Martin, D.M., Clamp, M. and Barton, G.J. (2009) Jalview Version 2-a multiple sequence alignment editor and analysis workbench. Bioinformatics, 25, 1189-1191.
    • (2009) Bioinformatics , vol.25 , pp. 1189-1191
    • Waterhouse, A.M.1    Procter, J.B.2    Martin, D.M.3    Clamp, M.4    Barton, G.J.5
  • 68
    • 25444436686 scopus 로고    scopus 로고
    • The Molecular Biology Toolkit (MBT): a modular platform for developing molecular visualization applications
    • Moreland, J.L., Gramada, A., Buzko, O.V., Zhang, Q. and Bourne, P.E. (2005) The Molecular Biology Toolkit (MBT): a modular platform for developing molecular visualization applications. BMC Bioinformatics, 6, 21.
    • (2005) BMC Bioinformatics , vol.6 , pp. 21
    • Moreland, J.L.1    Gramada, A.2    Buzko, O.V.3    Zhang, Q.4    Bourne, P.E.5
  • 69
    • 48449106792 scopus 로고    scopus 로고
    • The Jpred 3 secondary structure prediction server
    • Cole, C., Barber, J.D. and Barton, G.J. (2008) The Jpred 3 secondary structure prediction server. Nucleic Acids Res., 36, W197-W201.
    • (2008) Nucleic Acids Res , vol.36
    • Cole, C.1    Barber, J.D.2    Barton, G.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.