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Volumn 48, Issue , 1997, Pages 457-466

Dystrophin-associated proteins and the muscular dystrophies

Author keywords

Muscle membrane; Muscle proteins; Myopathy

Indexed keywords

DYSTROGLYCAN; DYSTROPHIN; MUSCLE PROTEIN; SARCOGLYCAN; UTROPHIN;

EID: 8044235811     PISSN: 00664219     EISSN: None     Source Type: Book Series    
DOI: 10.1146/annurev.med.48.1.457     Document Type: Review
Times cited : (53)

References (43)
  • 1
    • 0023904860 scopus 로고
    • The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein
    • Koenig M, Monaco A, Kunkel L. 1988. The complete sequence of dystrophin predicts a rod-shaped cytoskeletal protein. Cell 53: 219-26
    • (1988) Cell , vol.53 , pp. 219-226
    • Koenig, M.1    Monaco, A.2    Kunkel, L.3
  • 2
    • 0024600620 scopus 로고
    • Association of dystrophin and an integral membrane glycoprotein
    • Campbell K, Kahl S. 1989. Association of dystrophin and an integral membrane glycoprotein. Nature 338:259-62
    • (1989) Nature , vol.338 , pp. 259-262
    • Campbell, K.1    Kahl, S.2
  • 3
    • 0025242185 scopus 로고
    • Glycoprotein complex anchoring dystrophin to sarcolemma
    • Yoshida M, Ozawa E. 1990. Glycoprotein complex anchoring dystrophin to sarcolemma. J. Biochem. 108:748-52
    • (1990) J. Biochem. , vol.108 , pp. 748-752
    • Yoshida, M.1    Ozawa, E.2
  • 4
    • 0028845066 scopus 로고
    • Dystrophin-glycoprotein complex: Molecular organization and critical roles in skeletal muscle
    • Sunada Y, Campbell K. 1995. Dystrophin-glycoprotein complex: molecular organization and critical roles in skeletal muscle. Curr. Opin. Neurol. 8:379-84
    • (1995) Curr. Opin. Neurol. , vol.8 , pp. 379-384
    • Sunada, Y.1    Campbell, K.2
  • 5
    • 0028877455 scopus 로고
    • Muscular dystrophies: Diseases of the dystrophin-glycoprotein complex
    • Worton R. 1995. Muscular dystrophies: diseases of the dystrophin-glycoprotein complex. Science 270:755-56
    • (1995) Science , vol.270 , pp. 755-756
    • Worton, R.1
  • 6
    • 0029089582 scopus 로고
    • Dystrophin-associated proteins in muscular dystrophy
    • Ozawa E, Yoshida M, Suzuki A, et al. 1995. Dystrophin-associated proteins in muscular dystrophy. Hum. Molec. Genet. 4:1711-16
    • (1995) Hum. Molec. Genet. , vol.4 , pp. 1711-1716
    • Ozawa, E.1    Yoshida, M.2    Suzuki, A.3
  • 7
    • 0027275643 scopus 로고
    • A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin
    • Ervasti J, Campbell K. 1993. A role for the dystrophin-glycoprotein complex as a transmembrane linker between laminin and actin. J. Cell. Biol. 122:809-23
    • (1993) J. Cell. Biol. , vol.122 , pp. 809-823
    • Ervasti, J.1    Campbell, K.2
  • 8
    • 0028302369 scopus 로고
    • Dissociation of the complex of dystrophin and its associated proteins into several unique groups in by n-octyl beta-D-glucoside
    • Yoshida M, Suzuki A, Yamamoto H, et al. 1994. Dissociation of the complex of dystrophin and its associated proteins into several unique groups in by n-octyl beta-D-glucoside. Eur. J. Biochem. 222:1055-61
    • (1994) Eur. J. Biochem. , vol.222 , pp. 1055-1061
    • Yoshida, M.1    Suzuki, A.2    Yamamoto, H.3
  • 9
    • 0027361264 scopus 로고
    • Primary structure and muscle-specific expression of the 50-kd dystrophin-associated glycoprotein (adhalin)
    • Roberds S, Anderson R, Ibraghimov-Beskrovnaya O, et al. 1993. Primary structure and muscle-specific expression of the 50-kd dystrophin-associated glycoprotein (adhalin). J. Biol. Chem. 268:23739-42
    • (1993) J. Biol. Chem. , vol.268 , pp. 23739-23742
    • Roberds, S.1    Anderson, R.2    Ibraghimov-Beskrovnaya, O.3
  • 10
    • 0027959491 scopus 로고
    • Human adhalin is alternatively spliced and the gene is located on chromosome 17q21
    • McNally E, Yoshida M, Mizuno Y, et al. 1994. Human adhalin is alternatively spliced and the gene is located on chromosome 17q21. Proc. Natl. Acad. Sci. USA 91:9690-94
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 9690-9694
    • McNally, E.1    Yoshida, M.2    Mizuno, Y.3
  • 11
    • 0028146869 scopus 로고
    • Missense mutations in the adhalin gene linked to autosomal recessive muscular dystrophy
    • Roberds S, Leturcq F, Allamand V, et al. 1994. Missense mutations in the adhalin gene linked to autosomal recessive muscular dystrophy. Cell 78:625-33
    • (1994) Cell , vol.78 , pp. 625-633
    • Roberds, S.1    Leturcq, F.2    Allamand, V.3
  • 12
    • 0028971219 scopus 로고
    • Beta-sarcoglycan (A3b) mutations cause autosomal recessive muscular dystrophy with loss of the sarcoglycan complex
    • Bonnemann C, Modi R, Noguchi S, et al. 1995. Beta-sarcoglycan (A3b) mutations cause autosomal recessive muscular dystrophy with loss of the sarcoglycan complex. Nature Genet. 11:266-73
    • (1995) Nature Genet. , vol.11 , pp. 266-273
    • Bonnemann, C.1    Modi, R.2    Noguchi, S.3
  • 13
    • 0028971221 scopus 로고
    • Beta-sarcoglycan: Characterization and role in limb-girdle muscular dystrophy linked to 4q12
    • Lim L, Duclos F, Broux O, et al. 1995. Beta-sarcoglycan: characterization and role in limb-girdle muscular dystrophy linked to 4q12. Nature Genet. 11:257-65
    • (1995) Nature Genet. , vol.11 , pp. 257-265
    • Lim, L.1    Duclos, F.2    Broux, O.3
  • 14
    • 0028883973 scopus 로고
    • Mutations in the dystrophin-associated protein gamma-sarcoglycan in chromosome 13 muscular dystrophy
    • Noguchi S, McNally E, Othmane K, et al. 1995. Mutations in the dystrophin-associated protein gamma-sarcoglycan in chromosome 13 muscular dystrophy. Science 270:819-22
    • (1995) Science , vol.270 , pp. 819-822
    • Noguchi, S.1    McNally, E.2    Othmane, K.3
  • 15
    • 0028206868 scopus 로고
    • Molecular organization at the glycoprotein-complex-binding site of dystrophin
    • Suzuki A, Yoshida M, Hayashi K, et al. 1994. Molecular organization at the glycoprotein-complex-binding site of dystrophin. Eur. J. Biochem. 220:283-92
    • (1994) Eur. J. Biochem. , vol.220 , pp. 283-292
    • Suzuki, A.1    Yoshida, M.2    Hayashi, K.3
  • 16
    • 0028046502 scopus 로고
    • Nitric oxide in skeletal muscle
    • Kobzik L, Reid M, Bredt D, et al. 1994. Nitric oxide in skeletal muscle. Nature 372: 546-48
    • (1994) Nature , vol.372 , pp. 546-548
    • Kobzik, L.1    Reid, M.2    Bredt, D.3
  • 17
    • 0027473029 scopus 로고
    • Cloned human brain nitric oxide is highly expressed in skeletal muscle
    • Nakane M, Schmidt H, Pollock J, et al. 1993. Cloned human brain nitric oxide is highly expressed in skeletal muscle. FEBS Lett. 316:175-80
    • (1993) FEBS Lett. , vol.316 , pp. 175-180
    • Nakane, M.1    Schmidt, H.2    Pollock, J.3
  • 18
    • 0026695175 scopus 로고
    • Glycoprotein-binding site of dystrophin is confined to the cysteine-rich domain and the first half of the carboxy-terminal domain
    • Suzuki A, Yoshida M, Yamamoto H, et al. 1992. Glycoprotein-binding site of dystrophin is confined to the cysteine-rich domain and the first half of the carboxy-terminal domain. FEBS Lett. 308:154-60
    • (1992) FEBS Lett. , vol.308 , pp. 154-160
    • Suzuki, A.1    Yoshida, M.2    Yamamoto, H.3
  • 19
    • 0028219584 scopus 로고
    • A1, a distinct 59-kDa dystrophin-associated protein encoded on chromosome 8q23-24
    • Ahn A, Yoshida M, Andersen M, et al. 1994. A1, a distinct 59-kDa dystrophin-associated protein encoded on chromosome 8q23-24. Proc. Natl. Acad. Sci. USA 91: 4446-50
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4446-4450
    • Ahn, A.1    Yoshida, M.2    Andersen, M.3
  • 20
    • 0027998866 scopus 로고
    • Heterogeneity of the 59-kDa dystrophin-associated protein revealed by cDNA cloning and expression
    • Yang B, Ibraghimov-Beskrovnaya O, Moomaw C, et al. 1994. Heterogeneity of the 59-kDa dystrophin-associated protein revealed by cDNA cloning and expression. J. Biol. Chem. 269:6040-44
    • (1994) J. Biol. Chem. , vol.269 , pp. 6040-6044
    • Yang, B.1    Ibraghimov-Beskrovnaya, O.2    Moomaw, C.3
  • 21
    • 0027375539 scopus 로고
    • Two forms of mouse syntrophin, a 58kD dystrophin-associated protein, differ in primary structure and tissue distribution
    • Adams M, Butler M, Dwyer T, et al. 1993. Two forms of mouse syntrophin, a 58kD dystrophin-associated protein, differ in primary structure and tissue distribution. Neuron 11:531-40
    • (1993) Neuron , vol.11 , pp. 531-540
    • Adams, M.1    Butler, M.2    Dwyer, T.3
  • 22
    • 0027182201 scopus 로고
    • Interaction of dystrophin with cytoskeletal proteins: Binding to talin and actin
    • Senter L, Luise M, Presotto C, et al. 1993. Interaction of dystrophin with cytoskeletal proteins: binding to talin and actin. Biochem. Biophys. Res. Commun. 192:899-904
    • (1993) Biochem. Biophys. Res. Commun. , vol.192 , pp. 899-904
    • Senter, L.1    Luise, M.2    Presotto, C.3
  • 23
    • 0026711133 scopus 로고
    • Dystrophin colocalizes with beta-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle
    • Porter G, Dmytrenko G, Winkelmann J, et al. 1992. Dystrophin colocalizes with beta-spectrin in distinct subsarcolemmal domains in mammalian skeletal muscle. J. Cell. Biol. 117:997-1005
    • (1992) J. Cell. Biol. , vol.117 , pp. 997-1005
    • Porter, G.1    Dmytrenko, G.2    Winkelmann, J.3
  • 24
    • 0026785988 scopus 로고
    • Dystrophin at the plasma membrane of human muscle fibers shows a coslameric localization
    • Minetti C, Beltrame F, Marcenaro G, et al. 1992. Dystrophin at the plasma membrane of human muscle fibers shows a coslameric localization. Neuromusc. Disord. 2:99-109
    • (1992) Neuromusc. Disord. , vol.2 , pp. 99-109
    • Minetti, C.1    Beltrame, F.2    Marcenaro, G.3
  • 25
    • 0026621049 scopus 로고
    • Primary structure of dystrophin-related protein
    • Tinsley J, Blake D, Roche A, et al. 1992. Primary structure of dystrophin-related protein. Nature 360:591-93
    • (1992) Nature , vol.360 , pp. 591-593
    • Tinsley, J.1    Blake, D.2    Roche, A.3
  • 26
    • 0025167294 scopus 로고
    • Identification of a chromosome 6-encoded dystrophin-related protein
    • Khurana T, Hoffman E, Kunkel L. 1990. Identification of a chromosome 6-encoded dystrophin-related protein. J. Biol. Chem. 265:16717-20
    • (1990) J. Biol. Chem. , vol.265 , pp. 16717-16720
    • Khurana, T.1    Hoffman, E.2    Kunkel, L.3
  • 27
    • 0028321841 scopus 로고
    • Identification and purification of an agrin receptor from Torpedo post-synaptic membrane: A heteromeric complex related to the dystroglycans
    • Bowe M, Deyst K, Leszyk J, et al. 1994. Identification and purification of an agrin receptor from Torpedo post-synaptic membrane: a heteromeric complex related to the dystroglycans. Neuron 12:1173-80
    • (1994) Neuron , vol.12 , pp. 1173-1180
    • Bowe, M.1    Deyst, K.2    Leszyk, J.3
  • 28
    • 0023906647 scopus 로고
    • Dystrophin characterization in muscle biopsies from Duchenne and Becker muscular dystrophy patients
    • Hoffman E, Fischbeck K, Brown R, et al. 1988. Dystrophin characterization in muscle biopsies from Duchenne and Becker muscular dystrophy patients. N. Engl. J. Med. 318:1363-68
    • (1988) N. Engl. J. Med. , vol.318 , pp. 1363-1368
    • Hoffman, E.1    Fischbeck, K.2    Brown, R.3
  • 29
    • 0020606260 scopus 로고
    • Severe childhood muscular dystrophy affecting both sexes and frequent in Tunisia
    • Ben Hamida M, Fardeau M, Attia N. 1980. Severe childhood muscular dystrophy affecting both sexes and frequent in Tunisia. Muscle Nerve 6:469-80
    • (1980) Muscle Nerve , vol.6 , pp. 469-480
    • Ben Hamida, M.1    Fardeau, M.2    Attia, N.3
  • 30
    • 0027032694 scopus 로고
    • Linkage of Tunisian autosomal recessive Duchenne-like muscular dystrophy to the pericentromeric region of chromosome 13q
    • Othmane K, Ben Hamida M, Pericak-Vance M, et al. 1992. Linkage of Tunisian autosomal recessive Duchenne-like muscular dystrophy to the pericentromeric region of chromosome 13q. Nature Genet. 2:315-17
    • (1992) Nature Genet. , vol.2 , pp. 315-317
    • Othmane, K.1    Ben Hamida, M.2    Pericak-Vance, M.3
  • 31
    • 0030008373 scopus 로고    scopus 로고
    • Linkage analysis in autosomal recessive limb-girdle muscular dystrophy (AR LGMD) maps a sixth form to 5q33-34 (LGMD2F) and indicates that there is at least one more subtype of LGMD
    • Passos-Bueno M, Moreira E, Vainzof M, et al. 1996. Linkage analysis in autosomal recessive limb-girdle muscular dystrophy (AR LGMD) maps a sixth form to 5q33-34 (LGMD2F) and indicates that there is at least one more subtype of LGMD. Hum. Molec. Genet. 5:815-20
    • (1996) Hum. Molec. Genet. , vol.5 , pp. 815-820
    • Passos-Bueno, M.1    Moreira, E.2    Vainzof, M.3
  • 32
    • 0029816797 scopus 로고    scopus 로고
    • The 5q autosomal recessive limb-girdle muscular dystrophy (LGMD2F) is caused by a mutation in the d-sarcoglycan gene
    • In press
    • Nigro V, Moreira E, Piluso G, et al. 1996. The 5q autosomal recessive limb-girdle muscular dystrophy (LGMD2F) is caused by a mutation in the d-sarcoglycan gene. Nature Genet. In press
    • (1996) Nature Genet.
    • Nigro, V.1    Moreira, E.2    Piluso, G.3
  • 33
    • 0028094441 scopus 로고
    • Localization of merosin-negative congenital muscular dystrophy to chromosome 6q22 by homozygosity mapping
    • Hillaire D, Leclerc A, Faure S, et al. 1994. Localization of merosin-negative congenital muscular dystrophy to chromosome 6q22 by homozygosity mapping. Hum. Molec. Genet. 3:1657-61
    • (1994) Hum. Molec. Genet. , vol.3 , pp. 1657-1661
    • Hillaire, D.1    Leclerc, A.2    Faure, S.3
  • 34
    • 0028980027 scopus 로고
    • Mutations in the laminin a2-chain gene (LAMA2) cause merosin deficient congenital muscular dystrophy
    • Helbling-Leclerc A, Zhang X, Topaloglu H, et al. 1995. Mutations in the laminin a2-chain gene (LAMA2) cause merosin deficient congenital muscular dystrophy. Nature Genet. 11:216-18
    • (1995) Nature Genet. , vol.11 , pp. 216-218
    • Helbling-Leclerc, A.1    Zhang, X.2    Topaloglu, H.3
  • 35
  • 36
    • 0029874852 scopus 로고    scopus 로고
    • Emerin deficiency at the nuclear membrane in patients with Emery-Dreyfuss muscular dystrophy
    • Nagano A, Koga R, Ogawa M, et al. 1996. Emerin deficiency at the nuclear membrane in patients with Emery-Dreyfuss muscular dystrophy. Nature Genet. 12:254-59
    • (1996) Nature Genet. , vol.12 , pp. 254-259
    • Nagano, A.1    Koga, R.2    Ogawa, M.3
  • 37
    • 0010397284 scopus 로고    scopus 로고
    • The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein
    • Manilal S, Man N, Sewry C, et al. 1996. The Emery-Dreifuss muscular dystrophy protein, emerin, is a nuclear membrane protein. Hum. Molec. Genet. 5:801-8
    • (1996) Hum. Molec. Genet. , vol.5 , pp. 801-808
    • Manilal, S.1    Man, N.2    Sewry, C.3
  • 38
    • 0028905205 scopus 로고
    • Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2a
    • Richard I, Broux O, Allamand V, et al. 1995. Mutations in the proteolytic enzyme calpain 3 cause limb-girdle muscular dystrophy type 2a. Cell 81:27-40
    • (1995) Cell , vol.81 , pp. 27-40
    • Richard, I.1    Broux, O.2    Allamand, V.3
  • 39
    • 0028852835 scopus 로고
    • A mutation in the alpha-tropomyosin gene TPM2 associated with autosomal dominant distal myopathy
    • Laing N, Wilton S, Akkari P, et al. 1995. A mutation in the alpha-tropomyosin gene TPM2 associated with autosomal dominant distal myopathy. Nature Genet. 9:75-79
    • (1995) Nature Genet. , vol.9 , pp. 75-79
    • Laing, N.1    Wilton, S.2    Akkari, P.3
  • 40
    • 0027221634 scopus 로고
    • Missense mutations in the beta-myosin heavy-chain cause central core disease in hypertrophic cardiomyopathy
    • Fananapazir L, Dalakas M, Cyran F, et al. 1993. Missense mutations in the beta-myosin heavy-chain cause central core disease in hypertrophic cardiomyopathy. Proc. Natl. Acad. Sci. USA 90:3993-97
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 3993-3997
    • Fananapazir, L.1    Dalakas, M.2    Cyran, F.3
  • 41
    • 0026566108 scopus 로고
    • Molecular basis of myotonic dystrophy expansion of a trinucleotide (CTG) repeat at the 3′ end of a transcript encoding a protein kinase family member
    • Brook J, McCurrach M, Harley M, et al. 1992. Molecular basis of myotonic dystrophy expansion of a trinucleotide (CTG) repeat at the 3′ end of a transcript encoding a protein kinase family member. Cell 68: 799-808
    • (1992) Cell , vol.68 , pp. 799-808
    • Brook, J.1    McCurrach, M.2    Harley, M.3
  • 42
    • 0025160101 scopus 로고
    • Location of a facioscapulohumeral muscular dystrophy gene on chromosome 4
    • Wijmenga C, Frants R, Brouwer O, et al. 1990. Location of a facioscapulohumeral muscular dystrophy gene on chromosome 4. Lancet 336:651-53
    • (1990) Lancet , vol.336 , pp. 651-653
    • Wijmenga, C.1    Frants, R.2    Brouwer, O.3
  • 43
    • 0028364727 scopus 로고
    • Gene therapy prospects for Duchenne muscular dystrophy
    • Clemens P, Caskey C. 1994. Gene therapy prospects for Duchenne muscular dystrophy. Eur. Neurol. 34:181-85
    • (1994) Eur. Neurol. , vol.34 , pp. 181-185
    • Clemens, P.1    Caskey, C.2


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