메뉴 건너뛰기




Volumn 116, Issue 4, 2006, Pages 1016-1024

Induction of myasthenia by immunization against muscle-specific kinase

Author keywords

[No Author keywords available]

Indexed keywords

AUTOANTIBODY; MUSCLE SPECIFIC KINASE ENZYME; NICOTINIC RECEPTOR; PHOSPHOTRANSFERASE; UNCLASSIFIED DRUG;

EID: 33645521800     PISSN: 00219738     EISSN: 15588238     Source Type: Journal    
DOI: 10.1172/JCI21545     Document Type: Article
Times cited : (137)

References (51)
  • 1
    • 0016912621 scopus 로고
    • Experimental autoimmune myasthenia gravis and myasthenia gravis: Biochemical and immunochemical aspects
    • Lindstrom, J.M., Lennon, V.A., Seybold, M.E., and Whittingham, S. 1976. Experimental autoimmune myasthenia gravis and myasthenia gravis: biochemical and immunochemical aspects. Ann. N. Y. Acad. Sci. 274:254-274.
    • (1976) Ann. N. Y. Acad. Sci. , vol.274 , pp. 254-274
    • Lindstrom, J.M.1    Lennon, V.A.2    Seybold, M.E.3    Whittingham, S.4
  • 2
    • 0035105784 scopus 로고    scopus 로고
    • Auto-antibodies to the receptor tyrosine kinase MuSK in patients with myasthenia gravis without acetylcholine receptor antibodies
    • Hoch, W., et al. 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
  • 3
    • 0242336467 scopus 로고    scopus 로고
    • Clinical correlates with anti-MuSK antibodies in generalized seronegative myasthenia gravis
    • Evoli, A., et al. 2003. Clinical correlates with anti-MuSK antibodies in generalized seronegative myasthenia gravis. Brain. 126:2304-2311.
    • (2003) Brain , vol.126 , pp. 2304-2311
    • Evoli, A.1
  • 4
    • 1642348179 scopus 로고    scopus 로고
    • Detection and characterization of MuSK antibodies in seronegative myasthenia gravis
    • McConville, J., et al. 2004. Detection and characterization of MuSK antibodies in seronegative myasthenia gravis. Ann. Neurol. 55:580-584.
    • (2004) Ann. Neurol. , vol.55 , pp. 580-584
    • McConville, J.1
  • 5
    • 2942566392 scopus 로고    scopus 로고
    • MuSK antibodies in AChR Ab-seropositive MG vs AChR Ab-seronegative MG
    • Ohta, K., et al. 2004. MuSK antibodies in AChR Ab-seropositive MG vs AChR Ab-seronegative MG. Neurology. 62:2132-2133.
    • (2004) Neurology , vol.62 , pp. 2132-2133
    • Ohta, K.1
  • 6
    • 33645498675 scopus 로고    scopus 로고
    • MuSK Ab described in seropositive MG sera found to be Ab to alkaline phosphatase
    • Ohta, K., et al. 2005. MuSK Ab described in seropositive MG sera found to be Ab to alkaline phosphatase. Neurology. 65:1988.
    • (2005) Neurology , vol.65 , pp. 1988
    • Ohta, K.1
  • 8
    • 2942531039 scopus 로고    scopus 로고
    • Low frequency of MuSK antibody in generalized seronegative myasthenia gravis among Chinese
    • Yeh, J.H., Chen, W.H., Chiu, H.C., and Vincent, A. 2004. Low frequency of MuSK antibody in generalized seronegative myasthenia gravis among Chinese. Neurology. 62:2131-2132.
    • (2004) Neurology , vol.62 , pp. 2131-2132
    • Yeh, J.H.1    Chen, W.H.2    Chiu, H.C.3    Vincent, A.4
  • 9
    • 3042852639 scopus 로고    scopus 로고
    • Clinical comparison of muscle-specific tyrosine kinase (MuSK) antibody-positive and -negative myasthenic patients
    • Zhou, L., et al. 2004. Clinical comparison of muscle-specific tyrosine kinase (MuSK) antibody-positive and -negative myasthenic patients. Muscle Nerve. 30:55-60.
    • (2004) Muscle Nerve , vol.30 , pp. 55-60
    • Zhou, L.1
  • 10
    • 2942532978 scopus 로고    scopus 로고
    • Is "seronegative" MG explained by autoantibodies to MuSK?
    • Lindstrom, J. 2004. Is "seronegative" MG explained by autoantibodies to MuSK? Neurology. 62:1920-1921.
    • (2004) Neurology , vol.62 , pp. 1920-1921
    • Lindstrom, J.1
  • 11
    • 0030940161 scopus 로고    scopus 로고
    • Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold
    • Apel, E.D., Glass, D.J., Moscoso, L.M., Yancopoulos, G.D., and Sanes, J.R. 1997. Rapsyn is required for MuSK signaling and recruits synaptic components to a MuSK-containing scaffold. Neuron. 18:623-635.
    • (1997) Neuron , vol.18 , pp. 623-635
    • Apel, E.D.1    Glass, D.J.2    Moscoso, L.M.3    Yancopoulos, G.D.4    Sanes, J.R.5
  • 12
    • 0037126630 scopus 로고    scopus 로고
    • Acetylcholine receptors are required for agrin-induced clustering of postsynaptic proteins
    • Marangi, P.A., et al. 2001. Acetylcholine receptors are required for agrin-induced clustering of postsynaptic proteins. EMBO J. 20:7060-7073.
    • (2001) EMBO J. , vol.20 , pp. 7060-7073
    • Marangi, P.A.1
  • 13
    • 0035953645 scopus 로고    scopus 로고
    • Distinct roles of nerve and muscle in postsynaptic differentiation of the neuromuscular synapse
    • Lin, W., et al. 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
  • 14
    • 0034983538 scopus 로고    scopus 로고
    • Patterning of muscle acetylcholine receptor gene expression in the absence of motor innervation
    • Yang, X., et al. 2001. Patterning of muscle acetylcholine receptor gene expression in the absence of motor innervation. Neuron. 30:399-410.
    • (2001) Neuron , vol.30 , pp. 399-410
    • Yang, X.1
  • 15
    • 15844417385 scopus 로고    scopus 로고
    • The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo
    • DeChiara, T.M., et al. 1996. The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo. Cell. 85:501-512.
    • (1996) Cell , vol.85 , pp. 501-512
    • DeChiara, T.M.1
  • 16
    • 0029050847 scopus 로고
    • Failure of postsynaptic specialization to develop at neuromuscular junctions of rapsyn-deficient mice
    • Gautam, M., et al. 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
  • 17
    • 15844380040 scopus 로고    scopus 로고
    • Agrin acts via a MuSK receptor complex
    • Glass, D.J., et al. 1996. Agrin acts via a MuSK receptor complex. Cell. 85:513-523.
    • (1996) Cell , vol.85 , pp. 513-523
    • Glass, D.J.1
  • 18
    • 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
  • 19
    • 0029928633 scopus 로고    scopus 로고
    • Agrin-induced acetylcholine receptor clustering in mammalian muscle requires tyrosine phosphorylation
    • Ferns, M., Deiner, M., and Hall, Z. 1996. Agrin-induced acetylcholine receptor clustering in mammalian muscle requires tyrosine phosphorylation. J. Cell Biol. 132:937-944.
    • (1996) J. Cell Biol. , vol.132 , pp. 937-944
    • Ferns, M.1    Deiner, M.2    Hall, Z.3
  • 20
    • 0026583243 scopus 로고
    • The agrin gene codes for a family of basal lamina proteins that differ in function and distribution
    • Ruegg, M.A., et al. 1992. The agrin gene codes for a family of basal lamina proteins that differ in function and distribution. Neuron. 8:691-699.
    • (1992) Neuron , vol.8 , pp. 691-699
    • Ruegg, M.A.1
  • 21
    • 0033009432 scopus 로고    scopus 로고
    • Xenopus muscle-specific kinase: Molecular cloning and prominent expression in neural tissues during early embryonic development
    • Fu, A.K., et al. 1999. Xenopus muscle-specific kinase: molecular cloning and prominent expression in neural tissues during early embryonic development. Eur. J. Neurosci. 11:373-382.
    • (1999) Eur. J. Neurosci. , vol.11 , pp. 373-382
    • Fu, A.K.1
  • 22
    • 0029150962 scopus 로고
    • Cloning and developmental expression of Nsk2, a novel receptor tyrosine kinase implicated in skeletal myogenesis
    • Ganju, P., Walls, E., Brennan, J., and Reith, A.D. 1995. Cloning and developmental expression of Nsk2, a novel receptor tyrosine kinase implicated in skeletal myogenesis. Oncogene. 11:281-290.
    • (1995) Oncogene , vol.11 , pp. 281-290
    • Ganju, P.1    Walls, E.2    Brennan, J.3    Reith, A.D.4
  • 23
    • 0034530366 scopus 로고    scopus 로고
    • Cloning and characterization of muscle-specific kinase in chicken
    • Ip, F.C., et al. 2000. Cloning and characterization of muscle-specific kinase in chicken. Mol. Cell. Neurosci. 16:661-673.
    • (2000) Mol. Cell. Neurosci. , vol.16 , pp. 661-673
    • Ip, F.C.1
  • 24
    • 0027400467 scopus 로고
    • Muscle-specific trk-related receptor with a kringle domain defines a distinct class of receptor tyrosine kinases
    • Jennings, C.G., Dyer, S.M., and Burden, S.J. 1993. Muscle-specific trk-related receptor with a kringle domain defines a distinct class of receptor tyrosine kinases. Proc. Natl. Acad. Sci. U. S. A. 90:2895-2899.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2895-2899
    • Jennings, C.G.1    Dyer, S.M.2    Burden, S.J.3
  • 25
    • 0029160025 scopus 로고
    • Receptor tyrosine kinase specific for the skeletal muscle lineage: Expression in embryonic muscle, at the neuromuscular junction, and after injury
    • Valenzuela, D.M., et al. 1995. Receptor tyrosine kinase specific for the skeletal muscle lineage: expression in embryonic muscle, at the neuromuscular junction, and after injury. Neuron. 15:573-584.
    • (1995) Neuron , vol.15 , pp. 573-584
    • Valenzuela, D.M.1
  • 26
    • 0032880802 scopus 로고    scopus 로고
    • Distinct domains of MuSK mediate its abilities to induce and to associate with postsynaptic specializations
    • Zhou, H., Glass, D.J., Yancopoulos, G.D., and Sanes, J.R. 1999. Distinct domains of MuSK mediate its abilities to induce and to associate with postsynaptic specializations. J. Cell Biol. 146:1133-1146.
    • (1999) J. Cell Biol. , vol.146 , pp. 1133-1146
    • Zhou, H.1    Glass, D.J.2    Yancopoulos, G.D.3    Sanes, J.R.4
  • 27
    • 0030806280 scopus 로고    scopus 로고
    • Kinase domain of the muscle-specific receptor tyrosine kinase (MuSK) is sufficient for phosphorylation but not clustering of acetylcholine receptors: Required role for the MuSK ectodomain?
    • Glass, D.J., et al. 1997. Kinase domain of the muscle-specific receptor tyrosine kinase (MuSK) is sufficient for phosphorylation but not clustering of acetylcholine receptors: required role for the MuSK ectodomain? Proc. Natl. Acad. Sci. U. S. A. 94:8848-8853.
    • (1997) Proc. Natl. Acad. Sci. U. S. A. , vol.94 , pp. 8848-8853
    • Glass, D.J.1
  • 28
    • 0033135386 scopus 로고    scopus 로고
    • Constitutively active MuSK is clustered in the absence of agrin and induces ectopic postsynaptic-like membranes in skeletal muscle fibers
    • Jones, G., Moore, C., Hashemolhosseini, S., and Brenner, H.R. 1999. Constitutively active MuSK is clustered in the absence of agrin and induces ectopic postsynaptic-like membranes in skeletal muscle fibers. J. Neurosci. 19:3376-3383.
    • (1999) J. Neurosci. , vol.19 , pp. 3376-3383
    • Jones, G.1    Moore, C.2    Hashemolhosseini, S.3    Brenner, H.R.4
  • 29
    • 0033569388 scopus 로고    scopus 로고
    • Rapid and reversible effects of activity on acetylcholine receptor density at the neuromuscular junction in vivo
    • Akaaboune, M., Culican, S.M., Turney, S.G., and Lichtman, J.W. 1999. Rapid and reversible effects of activity on acetylcholine receptor density at the neuromuscular junction in vivo. Science. 286:503-507.
    • (1999) Science , vol.286 , pp. 503-507
    • Akaaboune, M.1    Culican, S.M.2    Turney, S.G.3    Lichtman, J.W.4
  • 30
    • 0037071873 scopus 로고    scopus 로고
    • Neurotransmitter receptor dynamics studied in vivo by reversible photo-unbinding of fluorescent ligands
    • Akaaboune, M., Grady, R.M., Turney, S., Sanes, J.R., and Lichtman, J.W. 2002. Neurotransmitter receptor dynamics studied in vivo by reversible photo-unbinding of fluorescent ligands. Neuron. 34:865-876.
    • (2002) Neuron , vol.34 , pp. 865-876
    • Akaaboune, M.1    Grady, R.M.2    Turney, S.3    Sanes, J.R.4    Lichtman, J.W.5
  • 31
    • 1642487117 scopus 로고    scopus 로고
    • Inhibition of synapse assembly in mammalian muscle in vivo by RNA interference
    • Kong, X.C., Barzaghi, P., and Ruegg, M.A. 2004. Inhibition of synapse assembly in mammalian muscle in vivo by RNA interference. EMBO Rep. 5:183-188.
    • (2004) EMBO Rep. , vol.5 , pp. 183-188
    • Kong, X.C.1    Barzaghi, P.2    Ruegg, M.A.3
  • 32
    • 0030879133 scopus 로고    scopus 로고
    • Laminin-induced acetylcholine receptor clustering: An alternative pathway
    • Sugiyama, J.E., Glass, D.J., Yancopoulos, G.D., and Hall, Z.W. 1997. Laminin-induced acetylcholine receptor clustering: an alternative pathway. J. Cell Biol. 139:181-191.
    • (1997) J. Cell Biol. , vol.139 , pp. 181-191
    • Sugiyama, J.E.1    Glass, D.J.2    Yancopoulos, G.D.3    Hall, Z.W.4
  • 33
    • 0020458870 scopus 로고
    • Lectin binding reveals a synapse-specific carbohydrate in skeletal muscle
    • Sanes, J.R., and Cheney, J.M. 1982. Lectin binding reveals a synapse-specific carbohydrate in skeletal muscle. Nature. 300:646-647.
    • (1982) Nature , vol.300 , pp. 646-647
    • Sanes, J.R.1    Cheney, J.M.2
  • 34
    • 0028935085 scopus 로고
    • Role for a synapse-specific carbohydrate in agrin-induced clustering of acetylcholine receptors
    • Martin, P.T., and Sanes, J.R. 1995. Role for a synapse-specific carbohydrate in agrin-induced clustering of acetylcholine receptors. Neuron. 14:743-754.
    • (1995) Neuron , vol.14 , pp. 743-754
    • Martin, P.T.1    Sanes, J.R.2
  • 35
    • 0037182593 scopus 로고    scopus 로고
    • Laminin-1 redistributes postsynaptic proteins and requires rapsyn, tyrosine phosphorylation, and Src and Fyn to stably cluster acetylcholine receptors
    • Marangi, P.A., Wieland, S.T., and Fuhrer, C. 2002. Laminin-1 redistributes postsynaptic proteins and requires rapsyn, tyrosine phosphorylation, and Src and Fyn to stably cluster acetylcholine receptors. J. Cell Biol. 157:883-895.
    • (2002) J. Cell Biol. , vol.157 , pp. 883-895
    • Marangi, P.A.1    Wieland, S.T.2    Fuhrer, C.3
  • 37
    • 0345204134 scopus 로고
    • Major general pathological reactions and their consequences on skeletal muslce cells
    • S. Carpenter and G. Karpati, editors. Churchill Livingstone Inc. New York, New York, USA
    • Carpenter, S., and Karpati, G. 1984. Major general pathological reactions and their consequences on skeletal muslce cells. In Pathology of skeletal muscle. S. Carpenter and G. Karpati, editors. Churchill Livingstone Inc. New York, New York, USA. 63-139.
    • (1984) Pathology of Skeletal Muscle , pp. 63-139
    • Carpenter, S.1    Karpati, G.2
  • 38
    • 0015935638 scopus 로고
    • Autoimmune response to acetylcholine receptor
    • Patrick, J., and Lindstrom, J. 1973. Autoimmune response to acetylcholine receptor. Science. 180:871-872.
    • (1973) Science , vol.180 , pp. 871-872
    • Patrick, J.1    Lindstrom, J.2
  • 39
    • 0032513058 scopus 로고    scopus 로고
    • Dimerization of the muscle-specific kinase induces tyrosine phosphorylation of acetylcholine receptors and their aggregation on the surface of myotubes
    • Hopf, C., and Hoch, W. 1998. Dimerization of the muscle-specific kinase induces tyrosine phosphorylation of acetylcholine receptors and their aggregation on the surface of myotubes. J. Biol. Chem. 273:6467-6473.
    • (1998) J. Biol. Chem. , vol.273 , pp. 6467-6473
    • Hopf, C.1    Hoch, W.2
  • 40
    • 0035957950 scopus 로고    scopus 로고
    • Agrin-induced activation of acetylcholine receptor-bound Src family kinases requires Rapsyn and correlates with acetylcholine receptor clustering
    • Mittaud, P., Marangi, P.A., Erb-Vogtli, S., and Fuhrer, C. 2001. Agrin-induced activation of acetylcholine receptor-bound Src family kinases requires Rapsyn and correlates with acetylcholine receptor clustering. J. Biol. Chem. 276:14505-14513.
    • (2001) J. Biol. Chem. , vol.276 , pp. 14505-14513
    • Mittaud, P.1    Marangi, P.A.2    Erb-Vogtli, S.3    Fuhrer, C.4
  • 41
    • 0028260234 scopus 로고
    • Staurosporine inhibits agrin-induced acetylcholine receptor phosphorylation and aggregation
    • Wallace, B.G. 1994. Staurosporine inhibits agrin-induced acetylcholine receptor phosphorylation and aggregation. J. Cell Biol. 125:661-668.
    • (1994) J. Cell Biol. , vol.125 , pp. 661-668
    • Wallace, B.G.1
  • 42
    • 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
  • 43
    • 0029893117 scopus 로고    scopus 로고
    • Defective neuromuscular synaptogenesis in agrin-deficient mutant mice
    • Gautam, M., et al. 1996. Defective neuromuscular synaptogenesis in agrin-deficient mutant mice. Cell. 85:525-535.
    • (1996) Cell , vol.85 , pp. 525-535
    • Gautam, M.1
  • 44
    • 0035860772 scopus 로고    scopus 로고
    • Differential Vicia villosa agglutinin reactivity identifies three distinct dystroglycan complexes in skeletal muscle
    • McDearmon, E.L., Combs, A.C., and Ervasti, J.M. 2001. Differential Vicia villosa agglutinin reactivity identifies three distinct dystroglycan complexes in skeletal muscle. J. Biol. Chem. 276:35078-35086.
    • (2001) J. Biol. Chem. , vol.276 , pp. 35078-35086
    • McDearmon, E.L.1    Combs, A.C.2    Ervasti, J.M.3
  • 45
    • 0037184974 scopus 로고    scopus 로고
    • MuSK glycosylation restrains MuSK activation and acetylcholine receptor clustering
    • Watty, A., and Burden, S.J. 2002. MuSK glycosylation restrains MuSK activation and acetylcholine receptor clustering. J. Biol. Chem. 277:50457-50462.
    • (2002) J. Biol. Chem. , vol.277 , pp. 50457-50462
    • Watty, A.1    Burden, S.J.2
  • 46
    • 0029982641 scopus 로고    scopus 로고
    • Rapsyn clusters and activates the synapse-specific receptor tyrosine kinase MuSK
    • Gillespie, S.K., Balasubramanian, S., Fung, E.T., and Huganir, R.L. 1996. Rapsyn clusters and activates the synapse-specific receptor tyrosine kinase MuSK. Neuron. 16:953-962.
    • (1996) Neuron , vol.16 , pp. 953-962
    • Gillespie, S.K.1    Balasubramanian, S.2    Fung, E.T.3    Huganir, R.L.4
  • 47
    • 0034670092 scopus 로고    scopus 로고
    • Identification and characterization of 5′ extension of mammalian agrin cDNA, the exons and the promoter sequences
    • Shigemoto, K., et al. 2000. Identification and characterization of 5′ extension of mammalian agrin cDNA, the exons and the promoter sequences. Biochim. Biophys. Acta. 1494:170-174.
    • (2000) Biochim. Biophys. Acta. , vol.1494 , pp. 170-174
    • Shigemoto, K.1
  • 48
    • 0029086140 scopus 로고
    • Complementary gradients in expression and binding of ELF-1 and Mek4 in development of the topographic retinotectal projection map
    • Cheng, H.J., Nakamoto, M., Bergemann, A.D., and Flanagan, J.G. 1995. Complementary gradients in expression and binding of ELF-1 and Mek4 in development of the topographic retinotectal projection map. Cell. 82:371-381.
    • (1995) Cell , vol.82 , pp. 371-381
    • Cheng, H.J.1    Nakamoto, M.2    Bergemann, A.D.3    Flanagan, J.G.4
  • 50
    • 0026667750 scopus 로고
    • Structure and chromosomal localization of the mammalian agrin gene
    • Rupp, F., et al. 1992. Structure and chromosomal localization of the mammalian agrin gene. J. Neurosci. 12:3535-3544.
    • (1992) J. Neurosci. , vol.12 , pp. 3535-3544
    • Rupp, F.1
  • 51
    • 0019866066 scopus 로고
    • Mapping of surface structures of electrophorus acetylcholine receptor using monoclonal antibodies
    • Tzartos, S.J., Rand, D.E., Einarson, B.L., and Lindstrom, J.M. 1981. Mapping of surface structures of electrophorus acetylcholine receptor using monoclonal antibodies. J. Biol. Chem. 256:8635-8645.
    • (1981) J. Biol. Chem. , vol.256 , pp. 8635-8645
    • Tzartos, S.J.1    Rand, D.E.2    Einarson, B.L.3    Lindstrom, J.M.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.