메뉴 건너뛰기




Volumn 74, Issue 1, 2000, Pages 70-80

Neural regulation of α-dystroglycan biosynthesis and glycosylation in skeletal muscle

Author keywords

Dystroglycan; Denervation; Dystrophin associated proteins; Glycosylation; Laminin; Muscle development

Indexed keywords

CELL SURFACE PROTEIN; DYSTROGLYCAN; DYSTROPHIN; LAMININ; MONOCLONAL ANTIBODY; UTROPHIN;

EID: 0033961470     PISSN: 00223042     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1471-4159.2000.0740070.x     Document Type: Article
Times cited : (52)

References (77)
  • 1
    • 0026688298 scopus 로고
    • Different distributions of dystrophin and related proteins at nerve-muscle junctions
    • Bewick G. S., Nicholson L. V. B., Young C., O'Donnell E., and Slater C. R. (1992) Different distributions of dystrophin and related proteins at nerve-muscle junctions. Neuroreport 3, 857-860.
    • (1992) Neuroreport , vol.3 , pp. 857-860
    • Bewick, G.S.1    Nicholson, L.V.B.2    Young, C.3    O'Donnell, E.4    Slater, C.R.5
  • 2
    • 0029985153 scopus 로고    scopus 로고
    • Increased expression of dystrophin, β-dystroglycan and adhalin in denervated rat muscles
    • Biral D., Senter L., and Salviati G. (1996) Increased expression of dystrophin, β-dystroglycan and adhalin in denervated rat muscles. J. Muscle Res. Cell Motil. 17, 523-532.
    • (1996) J. Muscle Res. Cell Motil. , vol.17 , pp. 523-532
    • Biral, D.1    Senter, L.2    Salviati, G.3
  • 4
    • 0028321841 scopus 로고
    • Identification and purification of an agrin receptor from Torpedo post-synaptic membranes: A heterodimeric complex related to the dystroglycans
    • Bowe M. A., Deyst K. A., Leszyk J. D., and Fallon J. R. (1994) Identification and purification of an agrin receptor from Torpedo post-synaptic membranes: a heterodimeric complex related to the dystroglycans. Neuron 12, 1173-1180.
    • (1994) Neuron , vol.12 , pp. 1173-1180
    • Bowe, M.A.1    Deyst, K.A.2    Leszyk, J.D.3    Fallon, J.R.4
  • 5
    • 0343148361 scopus 로고
    • State of play in the neural hypothesis of muscular dystrophy
    • Bradley W. G. (1974) State of play in the neural hypothesis of muscular dystrophy. Nature 250, 285-286.
    • (1974) Nature , vol.250 , pp. 285-286
    • Bradley, W.G.1
  • 6
    • 0343583984 scopus 로고
    • Synthesis of acetylcholine receptor by denervated rat diaphragm muscle
    • Brockes J. P. and Hall Z. W. (1975) Synthesis of acetylcholine receptor by denervated rat diaphragm muscle. Proc. Natl. Acad. Sci. USA 4, 1368-1372.
    • (1975) Proc. Natl. Acad. Sci. USA , vol.4 , pp. 1368-1372
    • Brockes, J.P.1    Hall, Z.W.2
  • 7
    • 0017734798 scopus 로고
    • Development of the neuromuscular junction in the chick embryo: The number, distribution, and stability of acetylcholine receptors
    • Burden S. (1977) Development of the neuromuscular junction in the chick embryo: the number, distribution, and stability of acetylcholine receptors. Dev. Biol. 57, 317-329.
    • (1977) Dev. Biol. , vol.57 , pp. 317-329
    • Burden, S.1
  • 8
    • 0028306787 scopus 로고
    • A role for dystrophin associated glycoproteins and utrophin in agrin-induced AChR clustering
    • Campanelli J. T., Roberds S. L., Campbell K. P., and Scheller R. H. (1994) A role for dystrophin associated glycoproteins and utrophin in agrin-induced AChR clustering. Cell 77, 663-674.
    • (1994) Cell , vol.77 , pp. 663-674
    • Campanelli, J.T.1    Roberds, S.L.2    Campbell, K.P.3    Scheller, R.H.4
  • 9
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeletal-extracellular matrix linkage
    • Campbell K. P. (1995) Three muscular dystrophies: loss of cytoskeletal-extracellular matrix linkage. Cell 80, 675-679.
    • (1995) Cell , vol.80 , pp. 675-679
    • Campbell, K.P.1
  • 10
    • 0024600620 scopus 로고
    • Association of dystrophin and an integral membrane glycoprotein
    • Campbell K. P. and Kahl S. D. (1989) Association of dystrophin and an integral membrane glycoprotein. Nature 338, 259-262.
    • (1989) Nature , vol.338 , pp. 259-262
    • Campbell, K.P.1    Kahl, S.D.2
  • 11
    • 0031026624 scopus 로고    scopus 로고
    • Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin
    • Chiba A., Matsumura K., Yamada H., Inazu T., Shimizu T., Kusunoki S., Kanazawa I., Kobata A., and Endo T. (1997) Structures of sialylated O-linked oligosaccharides of bovine peripheral nerve α-dystroglycan. The role of a novel O-mannosyl-type oligosaccharide in the binding of α-dystroglycan with laminin. J. Biol. Chem. 272, 2156-2162.
    • (1997) J. Biol. Chem. , vol.272 , pp. 2156-2162
    • Chiba, A.1    Matsumura, K.2    Yamada, H.3    Inazu, T.4    Shimizu, T.5    Kusunoki, S.6    Kanazawa, I.7    Kobata, A.8    Endo, T.9
  • 12
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction
    • Chomczynski P. and Sacchi N. (1987) Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal. Biochem. 162, 156-159.
    • (1987) Anal. Biochem. , vol.162 , pp. 156-159
    • Chomczynski, P.1    Sacchi, N.2
  • 13
    • 0028990431 scopus 로고
    • Distribution of α-dystroglycan during embryonic nerve-muscle synaptogenesis
    • Cohen M. W., Jacobson C., Godfrey E. W., Campbell K. P., and Carbonetto S. (1995) Distribution of α-dystroglycan during embryonic nerve-muscle synaptogenesis. J. Cell Biol. 129, 1093-1101.
    • (1995) J. Cell Biol. , vol.129 , pp. 1093-1101
    • Cohen, M.W.1    Jacobson, C.2    Godfrey, E.W.3    Campbell, K.P.4    Carbonetto, S.5
  • 14
    • 0030968026 scopus 로고    scopus 로고
    • Laminin-induced clustering of dystroglycan on embryonic muscle cells: Comparison with agrin-induced clustering
    • Cohen M. W., Jacobson C., Yurchenco P. D., Morris G. M., and Carbonetto S. (1997) Laminin-induced clustering of dystroglycan on embryonic muscle cells: comparison with agrin-induced clustering. J. Cell Biol. 136, 1047-1058.
    • (1997) J. Cell Biol. , vol.136 , pp. 1047-1058
    • Cohen, M.W.1    Jacobson, C.2    Yurchenco, P.D.3    Morris, G.M.4    Carbonetto, S.5
  • 15
    • 0033519279 scopus 로고    scopus 로고
    • Laminin polymerization induces a receptor-cytoskeleton network
    • Colognato H., Winkelmann D. A., and Yurchenco P. D. (1999) Laminin polymerization induces a receptor-cytoskeleton network. J. Cell Biol. 145, 619-631.
    • (1999) J. Cell Biol. , vol.145 , pp. 619-631
    • Colognato, H.1    Winkelmann, D.A.2    Yurchenco, P.D.3
  • 16
    • 0031451562 scopus 로고    scopus 로고
    • Sarcospan, the 25-kDa transmembrane component of the dystrophir-glycoprotein complex
    • Crosbie R. H., Heighway J., Venzke D. P., Lee J. C., and Campbell K. P. (1997) Sarcospan, the 25-kDa transmembrane component of the dystrophir-glycoprotein complex. J. Biol. Chem. 272, 31221-31224.
    • (1997) J. Biol. Chem. , vol.272 , pp. 31221-31224
    • Crosbie, R.H.1    Heighway, J.2    Venzke, D.P.3    Lee, J.C.4    Campbell, K.P.5
  • 17
    • 0028824320 scopus 로고
    • Laminin overrides the inhibitory effects of peripheral nervous system and central nervous system myelin-derived inhibitors of neunte growth
    • David S., Braun P. E., Jackson D. L., Kottis V., and McKerracher L. (1995) Laminin overrides the inhibitory effects of peripheral nervous system and central nervous system myelin-derived inhibitors of neunte growth. J. Neurosci. Res. 42, 594-602.
    • (1995) J. Neurosci. Res. , vol.42 , pp. 594-602
    • David, S.1    Braun, P.E.2    Jackson, D.L.3    Kottis, V.4    McKerracher, L.5
  • 18
    • 0017198766 scopus 로고
    • Synthesis of the acetylcholine receptor by cultured chick myotubes and denervated extensor digitorum longus muscles
    • Devreotes P. N. and Fambrough D. M. (1976) Synthesis of the acetylcholine receptor by cultured chick myotubes and denervated extensor digitorum longus muscles. Proc. Natl. Acad. Sci. USA 73, 161-164.
    • (1976) Proc. Natl. Acad. Sci. USA , vol.73 , pp. 161-164
    • Devreotes, P.N.1    Fambrough, D.M.2
  • 19
    • 0028972484 scopus 로고
    • The α-dystroglycan-β-dystroglycan complex. Membrane organization and relationship to an agrin receptor
    • Deyst K. A., Bowe M. A., Leszyk J. D., and Fallon J. R. (1995) The α-dystroglycan-β-dystroglycan complex. Membrane organization and relationship to an agrin receptor. J. Biol. Chem. 270, 25956-25959.
    • (1995) J. Biol. Chem. , vol.270 , pp. 25956-25959
    • Deyst, K.A.1    Bowe, M.A.2    Leszyk, J.D.3    Fallon, J.R.4
  • 20
    • 0023737217 scopus 로고
    • Isolation and partial characterisation of high affinity laminin receptors in neural cells
    • Douville P. J., Harvey W. J., and Carbonetto S. (1988) Isolation and partial characterisation of high affinity laminin receptors in neural cells. J. Biol. Chem. 263, 14964-14969.
    • (1988) J. Biol. Chem. , vol.263 , pp. 14964-14969
    • Douville, P.J.1    Harvey, W.J.2    Carbonetto, S.3
  • 22
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti J. M. and Campbell K. P. (1991) Membrane organization of the dystrophin-glycoprotein complex. Cell 66, 1121-1131.
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Campbell, K.P.2
  • 23
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti J. M. and Campbell K. P. (1993) A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell Biol. 122, 809-823.
    • (1993) J. Cell Biol. , vol.122 , pp. 809-823
    • Ervasti, J.M.1    Campbell, K.P.2
  • 24
    • 0025272250 scopus 로고
    • Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle
    • Ervasti J. M., Ohlendieck K., Kahl S. D., Gaver M. G. and Campbell K. P. (1990) Deficiency of a glycoprotein component of the dystrophin complex in dystrophic muscle. Nature 345, 313-319.
    • (1990) Nature , vol.345 , pp. 313-319
    • Ervasti, J.M.1    Ohlendieck, K.2    Kahl, S.D.3    Gaver, M.G.4    Campbell, K.P.5
  • 25
    • 0030826509 scopus 로고    scopus 로고
    • Tissue-specific heterogeneity in α-dystroglycan sialoglycosylation. Skeletal muscle α-dystroglycan is a latent receptor for Vicia villosa agglutinin b4 masked by sialic acid modification
    • Ervasti J. M., Burwell A. L., and Geissler A. L. (1997) Tissue-specific heterogeneity in α-dystroglycan sialoglycosylation. Skeletal muscle α-dystroglycan is a latent receptor for Vicia villosa agglutinin b4 masked by sialic acid modification. J. Biol. Chem. 272, 22315-22321.
    • (1997) J. Biol. Chem. , vol.272 , pp. 22315-22321
    • Ervasti, J.M.1    Burwell, A.L.2    Geissler, A.L.3
  • 26
    • 0024522577 scopus 로고
    • Agrin-related molecules are concentrated at acetylcholine receptor clusters in normal and aneural developing muscle
    • Fallon J. R. and Gelfman C. E. (1989) Agrin-related molecules are concentrated at acetylcholine receptor clusters in normal and aneural developing muscle. J. Cell Biol. 108, 1527-1535.
    • (1989) J. Cell Biol. , vol.108 , pp. 1527-1535
    • Fallon, J.R.1    Gelfman, C.E.2
  • 27
    • 0027321171 scopus 로고
    • Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin
    • Gee S. H., Blacher R. W., Douville P. J., Provost P. R., Yurchenco P. D., and Carbonetto S. (1993) Laminin-binding protein 120 from brain is closely related to the dystrophin-associated glycoprotein, dystroglycan, and binds with high affinity to the major heparin binding domain of laminin. J. Biol. Chem. 268, 14972-14980.
    • (1993) J. Biol. Chem. , vol.268 , pp. 14972-14980
    • Gee, S.H.1    Blacher, R.W.2    Douville, P.J.3    Provost, P.R.4    Yurchenco, P.D.5    Carbonetto, S.6
  • 28
  • 29
    • 0032494165 scopus 로고    scopus 로고
    • γ-Sarcoglycan deficiency leads to muscle membrane defects and apoptosis independent of dystrophin
    • Hack A. A., Ly C. T., Jiang F., Clendenin C. J., Sigrist K. S., Wollmann R. L., and McNally E. M. (1998) γ-Sarcoglycan deficiency leads to muscle membrane defects and apoptosis independent of dystrophin. J. Cell Biol. 142, 1279-1287.
    • (1998) J. Cell Biol. , vol.142 , pp. 1279-1287
    • Hack, A.A.1    Ly, C.T.2    Jiang, F.3    Clendenin, C.J.4    Sigrist, K.S.5    Wollmann, R.L.6    McNally, E.M.7
  • 30
    • 0027480289 scopus 로고
    • Synaptic structure and development: The neuromuscular junction
    • Hall Z. W. and Sanes J. R. (1993) Synaptic structure and development: the neuromuscular junction. Neuron 10, 99-121.
    • (1993) Neuron , vol.10 , pp. 99-121
    • Hall, Z.W.1    Sanes, J.R.2
  • 32
    • 0032445403 scopus 로고    scopus 로고
    • A role for dystroglycan in basement membrane assembly
    • Henry M. D. and Campbell K. P. (1998) A role for dystroglycan in basement membrane assembly. Cell 95, 859-870.
    • (1998) Cell , vol.95 , pp. 859-870
    • Henry, M.D.1    Campbell, K.P.2
  • 33
    • 0023614188 scopus 로고
    • Dystrophin: The protein product of the Duchenne muscular dystrophy locus
    • Hoffman E. P., Brown R. J., and Kunkel L. M. (1987) Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 51, 919-928.
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown, R.J.2    Kunkel, L.M.3
  • 36
    • 0027533969 scopus 로고
    • Dystrophin-glycoprotein complex and laminin colocalize to the sarcolemma and transverse tubules of cardiac muscle
    • Klietsch R., Ervasti J. M., Arnold W., Campbell K. P., and Jorgensen A. O. (1992) Dystrophin-glycoprotein complex and laminin colocalize to the sarcolemma and transverse tubules of cardiac muscle. Circ. Res. 72, 349-360.
    • (1992) Circ. Res. , vol.72 , pp. 349-360
    • Klietsch, R.1    Ervasti, J.M.2    Arnold, W.3    Campbell, K.P.4    Jorgensen, A.O.5
  • 37
    • 0029033193 scopus 로고
    • Temporal and spatial appearance of α-dystroglycan in differentiated mouse myoblasts in culture
    • Kostrominova T. Y. and Tanzer M. L. (1995) Temporal and spatial appearance of α-dystroglycan in differentiated mouse myoblasts in culture. J. Cell. Biochem. 58, 527-534.
    • (1995) J. Cell. Biochem. , vol.58 , pp. 527-534
    • Kostrominova, T.Y.1    Tanzer, M.L.2
  • 38
    • 0031722943 scopus 로고    scopus 로고
    • The sarcoglycan complex in limb girdle muscular dystrophy
    • Lim L. E. and Campbell K. P. (1998) The sarcoglycan complex in limb girdle muscular dystrophy. Curr. Opin. Neurol. 11, 443-452.
    • (1998) Curr. Opin. Neurol. , vol.11 , pp. 443-452
    • Lim, L.E.1    Campbell, K.P.2
  • 40
    • 0018740809 scopus 로고
    • Biosynthesis and degradation of acetylcholine receptors in rat skeletal muscles. Effects of electrical stimulation
    • Linden D. C. and Fambrough D. M. (1979) Biosynthesis and degradation of acetylcholine receptors in rat skeletal muscles. Effects of electrical stimulation. Neuroscience 4, 527-528.
    • (1979) Neuroscience , vol.4 , pp. 527-528
    • Linden, D.C.1    Fambrough, D.M.2
  • 41
    • 0018820957 scopus 로고
    • Acetylcholine sensitivity of developing ectopic nerve-muscle junctions in adult rat soleus muscles
    • Lømo T. and Slater C. R. (1980) Acetylcholine sensitivity of developing ectopic nerve-muscle junctions in adult rat soleus muscles. J. Physiol. (Lond.) 303, 173-189.
    • (1980) J. Physiol. (Lond.) , vol.303 , pp. 173-189
    • Lømo, T.1    Slater, C.R.2
  • 42
    • 0030914822 scopus 로고    scopus 로고
    • Electron microscopic study of long-term denervated rat skeletal muscle
    • Lu D. X., Huang S. K., and Carlson B. M. (1997) Electron microscopic study of long-term denervated rat skeletal muscle. Anat. Rec. 248, 355-361.
    • (1997) Anat. Rec. , vol.248 , pp. 355-361
    • Lu, D.X.1    Huang, S.K.2    Carlson, B.M.3
  • 43
    • 0028817970 scopus 로고
    • Vizualization of dystrophic muscle fibers in mdx mouse by vital staining with Evans blue: Evidence of apoptosis in dystrophin-deficient muscle
    • Matsuda R., Nishikawa A., and Tanaka H. (1995) Vizualization of dystrophic muscle fibers in mdx mouse by vital staining with Evans blue: evidence of apoptosis in dystrophin-deficient muscle. J. Biochem. (Tokyo) 118, 959-964.
    • (1995) J. Biochem. (Tokyo) , vol.118 , pp. 959-964
    • Matsuda, R.1    Nishikawa, A.2    Tanaka, H.3
  • 44
    • 0026621608 scopus 로고
    • Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle
    • Matsumura K., Ervasti J. M., Ohlendieck K., Kahl S. D., and Campbell K. P. (1992) Association of dystrophin-related protein with dystrophin-associated proteins in mdx mouse muscle. Nature 360, 588-591.
    • (1992) Nature , vol.360 , pp. 588-591
    • Matsumura, K.1    Ervasti, J.M.2    Ohlendieck, K.3    Kahl, S.D.4    Campbell, K.P.5
  • 46
    • 0032559065 scopus 로고    scopus 로고
    • Human ε-sarcoglycan is highly related to α-sarcoglycan (adhalin), the limb girdle muscular dystrophy 2D gene
    • McNally E. M., Ly C. T., and Kunkel L. M. (1998) Human ε-sarcoglycan is highly related to α-sarcoglycan (adhalin), the limb girdle muscular dystrophy 2D gene. FEBS Lett. 422, 27-32.
    • (1998) FEBS Lett. , vol.422 , pp. 27-32
    • McNally, E.M.1    Ly, C.T.2    Kunkel, L.M.3
  • 47
    • 0021248964 scopus 로고
    • Denervation supersensitivity in skeletal muscle: Analysis with a cloned cDNA probe
    • Merlie J. P., Isenberg K. E., Russell S. D., and Sanes J. R. (1984) Denervation supersensitivity in skeletal muscle: analysis with a cloned cDNA probe. J. Cell Biol. 99, 332-335.
    • (1984) J. Cell Biol. , vol.99 , pp. 332-335
    • Merlie, J.P.1    Isenberg, K.E.2    Russell, S.D.3    Sanes, J.R.4
  • 48
    • 0030601202 scopus 로고    scopus 로고
    • Induction of dystrophin-associated proteins together with nicotinic acetylcholine receptors by denervation in the absence of dystrophin in skeletal muscles of mdx mice
    • Mitsui T., Kawai H., Kawajiri M., Kunishige M., Aki K., and Saito S. (1996) Induction of dystrophin-associated proteins together with nicotinic acetylcholine receptors by denervation in the absence of dystrophin in skeletal muscles of mdx mice. Biochem. Biophys. Res. Commun. 224, 802-807.
    • (1996) Biochem. Biophys. Res. Commun. , vol.224 , pp. 802-807
    • Mitsui, T.1    Kawai, H.2    Kawajiri, M.3    Kunishige, M.4    Aki, K.5    Saito, S.6
  • 50
    • 0028877307 scopus 로고
    • Dystroglycan expression in the wild type and mdx mouse neural retina: Synaptic colocalization with dystrophin, dystrophin-related protein but not laminin
    • Montanaro F., Carbonetto S., Campbell K. P., and Lindenbaum M. (1995) Dystroglycan expression in the wild type and mdx mouse neural retina: synaptic colocalization with dystrophin, dystrophin-related protein but not laminin. J. Neurosci. Res. 42, 528-538.
    • (1995) J. Neurosci. Res. , vol.42 , pp. 528-538
    • Montanaro, F.1    Carbonetto, S.2    Campbell, K.P.3    Lindenbaum, M.4
  • 51
    • 0032519864 scopus 로고    scopus 로고
    • Laminin and α-dystroglycan mediate acetylcholine receptor aggregation via a MuSK-independent pathway
    • Montanaro F., Gee S. H., Jacobson C., Lindenbaum M. H., Froehner S. C., and Carbonetto S. (1998) Laminin and α-dystroglycan mediate acetylcholine receptor aggregation via a MuSK-independent pathway. J. Neurosci. 18, 1250-1260.
    • (1998) J. Neurosci. , vol.18 , pp. 1250-1260
    • Montanaro, F.1    Gee, S.H.2    Jacobson, C.3    Lindenbaum, M.H.4    Froehner, S.C.5    Carbonetto, S.6
  • 52
    • 0033553906 scopus 로고    scopus 로고
    • α-Dystroglycan is a laminin receptor involved in extracellular matrix assembly on myotubes and muscle cell viability
    • Montanaro F., Lindenbaum M. H., and Carbonetto S. (1999) α-Dystroglycan is a laminin receptor involved in extracellular matrix assembly on myotubes and muscle cell viability. J. Cell Biol. 145, 1325-1340.
    • (1999) J. Cell Biol. , vol.145 , pp. 1325-1340
    • Montanaro, F.1    Lindenbaum, M.H.2    Carbonetto, S.3
  • 55
    • 0026328022 scopus 로고
    • Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice
    • Ohlendieck K. and Campbell K. P. (1991) Dystrophin-associated proteins are greatly reduced in skeletal muscle from mdx mice. J. Cell Biol. 115, 1685-1694.
    • (1991) J. Cell Biol. , vol.115 , pp. 1685-1694
    • Ohlendieck, K.1    Campbell, K.P.2
  • 56
    • 0026094250 scopus 로고
    • Dystrophin-related protein is localized to neuromuscular junctions of adult skeletal muscle
    • Ohlendieck K., Ervasti J. M., Matsumura K., Kahl S. D., Leveille C. J., and Campbell K. P. (1991) Dystrophin-related protein is localized to neuromuscular junctions of adult skeletal muscle. Neuron 7, 499-508.
    • (1991) Neuron , vol.7 , pp. 499-508
    • Ohlendieck, K.1    Ervasti, J.M.2    Matsumura, K.3    Kahl, S.D.4    Leveille, C.J.5    Campbell, K.P.6
  • 57
    • 0030026572 scopus 로고    scopus 로고
    • Differential heparin inhibition of skeletal muscle α-dystroglycan binding to laminins
    • Pall E. A., Bolton K. M., and Ervasti J. M. (1996) Differential heparin inhibition of skeletal muscle α-dystroglycan binding to laminins. J. Biol. Chem. 271, 3817-3821.
    • (1996) J. Biol. Chem. , vol.271 , pp. 3817-3821
    • Pall, E.A.1    Bolton, K.M.2    Ervasti, J.M.3
  • 58
    • 0031456144 scopus 로고    scopus 로고
    • Distribution and function of laminins in the neuromuscular system of developing, adult, and mutant mice
    • Patton B. L., Miner J. H., Chiu A. Y., and Sanes J. R. (1997) Distribution and function of laminins in the neuromuscular system of developing, adult, and mutant mice. J. Cell Biol. 139, 1507-1521.
    • (1997) J. Cell Biol. , vol.139 , pp. 1507-1521
    • Patton, B.L.1    Miner, J.H.2    Chiu, A.Y.3    Sanes, J.R.4
  • 59
    • 0031770342 scopus 로고    scopus 로고
    • The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction
    • Peng H. B., Ali A. A., Daggett D. F., Rauvala H., Hassell J. R., and Smalheiser N. R. (1998) The relationship between perlecan and dystroglycan and its implication in the formation of the neuromuscular junction. Cell Adhes. Commun. 5, 475-489.
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 475-489
    • Peng, H.B.1    Ali, A.A.2    Daggett, D.F.3    Rauvala, H.4    Hassell, J.R.5    Smalheiser, N.R.6
  • 62
    • 0031471956 scopus 로고    scopus 로고
    • Both hypertrophic and dilated cardiomyopathies are caused by mutation of the same gene, δ-sarcoglycan, in hamster: An animal model of disrupted dystrophin-associated glycoprotein complex
    • Sakamoto A., Ono K., Abe M., Jasmin G., Eki T., Murakami Y., Masaki T., Toyo-Oka T., and Hanaoka F. (1997) Both hypertrophic and dilated cardiomyopathies are caused by mutation of the same gene, δ-sarcoglycan, in hamster: an animal model of disrupted dystrophin-associated glycoprotein complex. Proc. Natl. Acad. Sci. USA 94, 13873-13878.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 13873-13878
    • Sakamoto, A.1    Ono, K.2    Abe, M.3    Jasmin, G.4    Eki, T.5    Murakami, Y.6    Masaki, T.7    Toyo-Oka, T.8    Hanaoka, F.9
  • 63
    • 0025010542 scopus 로고
    • Molecular heterogeneity of basal laminae: Isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere
    • Sanes J. R., Engvall E., Butkowski R., and Hunter D. D. (1990) Molecular heterogeneity of basal laminae: isoforms of laminin and collagen IV at the neuromuscular junction and elsewhere. J. Cell Biol. 111, 1685-1699.
    • (1990) J. Cell Biol. , vol.111 , pp. 1685-1699
    • Sanes, J.R.1    Engvall, E.2    Butkowski, R.3    Hunter, D.D.4
  • 64
    • 0029072703 scopus 로고
    • Purification of cranin, a laminin binding membrane protein: Identity with djstroglycan and reassessment of its carbohydrate moieties
    • Smalheiser N. R. and Kim E. (1995) Purification of cranin, a laminin binding membrane protein: identity with djstroglycan and reassessment of its carbohydrate moieties. J. Biol. Chem. 270, 15425-15433.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15425-15433
    • Smalheiser, N.R.1    Kim, E.2
  • 65
    • 0023410821 scopus 로고
    • Cranin: A laminin-binding protein of cell membranes
    • Smalheiser N. R. and Schwartz N. B. (1987) Cranin: a laminin-binding protein of cell membranes. Proc. Natl. Acad. Sci. USA 84, 6457-6461.
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 6457-6461
    • Smalheiser, N.R.1    Schwartz, N.B.2
  • 66
    • 0027941192 scopus 로고
    • Dystroglycan binds nerve and muscle agrin
    • Sugiyama J., Bowen D. C., and Hall Z. W. (1994) Dystroglycan binds nerve and muscle agrin. Neuron 13, 103-115.
    • (1994) Neuron , vol.13 , pp. 103-115
    • Sugiyama, J.1    Bowen, D.C.2    Hall, Z.W.3
  • 67
    • 0030742809 scopus 로고    scopus 로고
    • DNA-fragmentation and expression of apoptosis-related proteins in muscular dystrophies
    • Tews D. S. and Goebel H. H. (1997) DNA-fragmentation and expression of apoptosis-related proteins in muscular dystrophies. Neuropathol. Appl. Neurobiol. 23, 331-338.
    • (1997) Neuropathol. Appl. Neurobiol. , vol.23 , pp. 331-338
    • Tews, D.S.1    Goebel, H.H.2
  • 68
    • 0030462678 scopus 로고    scopus 로고
    • Dystroglycan in the cerebellum is a laminin α2-chain binding protein at the glial-vascular interface and is expressed in Purkinje cells
    • Tian M., Jacobson C., Gee S. H., Campbell K. P., and Jucker M. (1996) Dystroglycan in the cerebellum is a laminin α2-chain binding protein at the glial-vascular interface and is expressed in Purkinje cells. Eur. J. Neurosci. 8, 2739-2747.
    • (1996) Eur. J. Neurosci. , vol.8 , pp. 2739-2747
    • Tian, M.1    Jacobson, C.2    Gee, S.H.3    Campbell, K.P.4    Jucker, M.5
  • 70
    • 0029794008 scopus 로고    scopus 로고
    • Merosin and laminin in myogenesis: Requirement for merosin in myotube stability and survival
    • Vachon P. H., Loechel F., Xu H., Wewer U. M., and Engvall E. (1996) Merosin and laminin in myogenesis: requirement for merosin in myotube stability and survival. J. Cell Biol. 134, 1483-1497.
    • (1996) J. Cell Biol. , vol.134 , pp. 1483-1497
    • Vachon, P.H.1    Loechel, F.2    Xu, H.3    Wewer, U.M.4    Engvall, E.5
  • 72
    • 0029013328 scopus 로고
    • The expression of dystrophin-associated glycoproteins during skeletal muscle degeneration and regeneration. An immunofluorescence study
    • Vater R., Harris J. B., Anderson V. B., Roberds S. L., Campbell K. P., and Cullen M. J. (1995) The expression of dystrophin-associated glycoproteins during skeletal muscle degeneration and regeneration. An immunofluorescence study. J. Neuropathol. Exp. Neurol. 54, 557-569.
    • (1995) J. Neuropathol. Exp. Neurol. , vol.54 , pp. 557-569
    • Vater, R.1    Harris, J.B.2    Anderson, V.B.3    Roberds, S.L.4    Campbell, K.P.5    Cullen, M.J.6
  • 73
    • 0018426146 scopus 로고
    • Junctional forms of acetylcholinesterase restored at nerve free endplates
    • Weinberg C. B. and Hall Z. W. (1979) Junctional forms of acetylcholinesterase restored at nerve free endplates. Dev. Biol. 68, 631-668.
    • (1979) Dev. Biol. , vol.68 , pp. 631-668
    • Weinberg, C.B.1    Hall, Z.W.2
  • 75
    • 0028877455 scopus 로고
    • Muscular dystrophies: Diseases of the dystrophin-glycoprotein complex
    • Worton R. (1995) Muscular dystrophies: diseases of the dystrophin-glycoprotein complex. Science 270, 755-756.
    • (1995) Science , vol.270 , pp. 755-756
    • Worton, R.1
  • 77
    • 0025242185 scopus 로고
    • Glycoprotein complex anchoring dystrophin to sarcolemma
    • Yoshida M. and Ozawa E. (1990) Glycoprotein complex anchoring dystrophin to sarcolemma. J. Biochem. (Tokyo) 108, 748-752.
    • (1990) J. Biochem. (Tokyo) , vol.108 , pp. 748-752
    • Yoshida, M.1    Ozawa, E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.