메뉴 건너뛰기




Volumn 40, Issue 5, 1996, Pages 782-791

Congenital muscular dystrophy with primary laminin α2 (Merosin) deficiency presenting as inflammatory myopathy

Author keywords

[No Author keywords available]

Indexed keywords

LAMININ;

EID: 10544230641     PISSN: 03645134     EISSN: None     Source Type: Journal    
DOI: 10.1002/ana.410400515     Document Type: Article
Times cited : (102)

References (44)
  • 2
    • 0000122091 scopus 로고
    • The congenital muscular dystrophies
    • Engel AG, Franzini-Armstrong C, eds. New York: McGraw-Hill Book
    • Banker BQ. The congenital muscular dystrophies. In: Engel AG, Franzini-Armstrong C, eds. Myology, vol 1. New York: McGraw-Hill Book, 1994:1275-1289
    • (1994) Myology , vol.1 , pp. 1275-1289
    • Banker, B.Q.1
  • 3
    • 0002618558 scopus 로고
    • A peculiar form of congenital progressive muscular dystrophy
    • Fukuyama Y, Kawazura M, Haruna H. A peculiar form of congenital progressive muscular dystrophy. Pediatr Univ Tokyo 1960;4:5-8
    • (1960) Pediatr Univ Tokyo , vol.4 , pp. 5-8
    • Fukuyama, Y.1    Kawazura, M.2    Haruna, H.3
  • 4
    • 0019471880 scopus 로고
    • Congenital progressive muscular dystrophy of the Fukuyama type - Clinical, genetic and pathological considerations
    • Fukuyama Y, Osawa M, Suzuki H. Congenital progressive muscular dystrophy of the Fukuyama type - clinical, genetic and pathological considerations. Brain Dev 1981;13:1-9
    • (1981) Brain Dev , vol.13 , pp. 1-9
    • Fukuyama, Y.1    Osawa, M.2    Suzuki, H.3
  • 5
    • 0027364850 scopus 로고
    • Localization of a gene for Fukuyama type congenital muscular dystrophy to chromosome 9q31-q33
    • Toda T, Segawa M, Nomura Y, et al. Localization of a gene for Fukuyama type congenital muscular dystrophy to chromosome 9q31-q33. Nature Genet 1993;5:283-286
    • (1993) Nature Genet , vol.5 , pp. 283-286
    • Toda, T.1    Segawa, M.2    Nomura, Y.3
  • 7
    • 0024375162 scopus 로고
    • Muscle-eye-brain disease (MEB)
    • Santavuori P, Somer H, Sainio K, et al. Muscle-eye-brain disease (MEB). Brain Dev 1989;11:147-153
    • (1989) Brain Dev , vol.11 , pp. 147-153
    • Santavuori, P.1    Somer, H.2    Sainio, K.3
  • 8
    • 0024539092 scopus 로고
    • Diagnostic criteria for Walker-Warburg syndrome
    • Dobyns WB, Pagon RA, Armstrong D, et al. Diagnostic criteria for Walker-Warburg syndrome. Am J Med Genet 1989;32: 195-210
    • (1989) Am J Med Genet , vol.32 , pp. 195-210
    • Dobyns, W.B.1    Pagon, R.A.2    Armstrong, D.3
  • 9
    • 0018868593 scopus 로고
    • Light and electron microscopic studies of congenital muscular dystrophy
    • Misugi N. Light and electron microscopic studies of congenital muscular dystrophy. Brain Dev 1980;2:191-199
    • (1980) Brain Dev , vol.2 , pp. 191-199
    • Misugi, N.1
  • 10
    • 0020669289 scopus 로고
    • Inflammatory infiltration in Fukuyama type congenital muscular dystrophy
    • Olney KK, Miller RG. Inflammatory infiltration in Fukuyama type congenital muscular dystrophy. Muscle Nerve 1983;6:75-77
    • (1983) Muscle Nerve , vol.6 , pp. 75-77
    • Olney, K.K.1    Miller, R.G.2
  • 12
    • 0022525211 scopus 로고
    • Ten years follow-up study of steroid therapy for congenital encephalomyopathy
    • Kinoshita M, Mishina M, Koya N. Ten years follow-up study of steroid therapy for congenital encephalomyopathy. Brain Dev 1986;8:280-284
    • (1986) Brain Dev , vol.8 , pp. 280-284
    • Kinoshita, M.1    Mishina, M.2    Koya, N.3
  • 13
    • 0025292541 scopus 로고
    • Congenital inflammatory myopathy
    • Shevell M, Rosenblatt B, Silver K, et al. Congenital inflammatory myopathy. Neurology 1990;40:1111-1114
    • (1990) Neurology , vol.40 , pp. 1111-1114
    • Shevell, M.1    Rosenblatt, B.2    Silver, K.3
  • 14
    • 0020071941 scopus 로고
    • Congenital muscular dystrophy (CMD) - A collagen formative disease?
    • Fidzianska A, Goebel HH, Lenard HG, Heckman C. Congenital muscular dystrophy (CMD) - a collagen formative disease? J Neurol Sci 1982;55:79-90
    • (1982) J Neurol Sci , vol.55 , pp. 79-90
    • Fidzianska, A.1    Goebel, H.H.2    Lenard, H.G.3    Heckman, C.4
  • 15
    • 0024600620 scopus 로고
    • Association of dystrophin and integral membrane glycoprotein
    • Campbell KP, Kahl SD. Association of dystrophin and integral membrane glycoprotein. Nature 1989;338:259-262
    • (1989) Nature , vol.338 , pp. 259-262
    • Campbell, K.P.1    Kahl, S.D.2
  • 16
    • 0025815479 scopus 로고
    • Membrane organization of the dystrophin-glycoprotein complex
    • Ervasti JM, Campbell KP. Membrane organization of the dystrophin-glycoprotein complex. Cell 1991;66:1121-1131
    • (1991) Cell , vol.66 , pp. 1121-1131
    • Ervasti, J.M.1    Kp, C.2
  • 17
    • 0026543686 scopus 로고
    • Primary structure of dystrophin-associated glycoproteins linking dystrophin to extracellular matrix
    • Ibraghimov-Beskrovnaya O, Ervasti JM, Leveille CJ, et al. Primary structure of dystrophin-associated glycoproteins linking dystrophin to extracellular matrix. Nature 1992;355: 696-702
    • (1992) Nature , vol.355 , pp. 696-702
    • Ibraghimov-Beskrovnaya, O.1    Ervasti, J.M.2    Leveille, C.J.3
  • 18
    • 0026695175 scopus 로고
    • Glycoprotein-binding site of dystrophin is confined to the cysteine-rich domain and the first half of the carboxyl-terminal domain
    • Suzuki A, Yoshida M, Yamamoto H, Ozawa E. Glycoprotein-binding site of dystrophin is confined to the cysteine-rich domain and the first half of the carboxyl-terminal domain. FEBS Lett 1992;308:154-160
    • (1992) FEBS Lett , vol.308 , pp. 154-160
    • Suzuki, A.1    Yoshida, M.2    Yamamoto, H.3    Ozawa, E.4
  • 20
    • 0028914964 scopus 로고
    • Three muscular dystrophies: Loss of cytoskeleton-extracellular matrix linkage
    • Campbell KP. Three muscular dystrophies: loss of cytoskeleton-extracellular matrix linkage. Cell 1995;80:675-679
    • (1995) Cell , vol.80 , pp. 675-679
    • Kp, C.1
  • 21
    • 0025373178 scopus 로고
    • Merosin, a tissue-specific basement membrane protein, is a laminin like protein
    • Ehrig K, Leivo I, Argraves WS, et al. Merosin, a tissue-specific basement membrane protein, is a laminin like protein. Proc Natl Acad Sci USA 1990;87:3264-3268
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3264-3268
    • Ehrig, K.1    Leivo, I.2    Argraves, W.S.3
  • 22
    • 0018691714 scopus 로고
    • Laminin a glycoprotein from basement membranes
    • Timpl R, Rohde H, Gehron Robey P, et al. Laminin a glycoprotein from basement membranes. J Biol Chem 1979;254: 9933-9937
    • (1979) J Biol Chem , vol.254 , pp. 9933-9937
    • Timpl, R.1    Rohde, H.2    Gehron Robey, P.3
  • 23
    • 0019814244 scopus 로고
    • Studies on the biosynthesis of laminin by murine parietal endoderm cells
    • Cooper AR, Kurkinen A, Taylor A, Hogan BLM. Studies on the biosynthesis of laminin by murine parietal endoderm cells. Eur J Biochem 1981;119:189-197
    • (1981) Eur J Biochem , vol.119 , pp. 189-197
    • Cooper, A.R.1    Kurkinen, A.2    Taylor, A.3    Blm, H.4
  • 24
    • 0028066764 scopus 로고
    • Human laminin M chain (merosin): Complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues
    • Voulteenaho R, Nissinen M, Sainio K, et al. Human laminin M chain (merosin): complete primary structure, chromosomal assignment, and expression of the M and A chain in human fetal tissues. J Cell Biol 1994;124:381-394
    • (1994) J Cell Biol , vol.124 , pp. 381-394
    • Voulteenaho, R.1    Nissinen, M.2    Sainio, K.3
  • 25
    • 0028232215 scopus 로고
    • Congenital muscular dystrophy with merosin deficiency
    • Tomé FMS, Evangelista T, Leclerc A, et al. Congenital muscular dystrophy with merosin deficiency. C R Acad Sci Paris 1994;317:351-357
    • (1994) C R Acad Sci Paris , vol.317 , pp. 351-357
    • Tomé, F.M.S.1    Evangelista, T.2    Leclerc, A.3
  • 26
    • 0028094441 scopus 로고
    • Localization of merosinnegative congenital muscular dystrophy to chromosome 6q2 by homozygosity mapping
    • Hillaire D, Leclerc A, Fauré S, et al. Localization of merosinnegative congenital muscular dystrophy to chromosome 6q2 by homozygosity mapping. Hum Mol Genet 1994;3:1657-1661
    • (1994) Hum Mol Genet , vol.3 , pp. 1657-1661
    • Hillaire, D.1    Leclerc, A.2    Fauré, S.3
  • 27
    • 0028980027 scopus 로고
    • Mutations in the laminin α2-chain gene (LAMA2) cause merosin-deficient congenital muscular dystrophy
    • Helbling-Leclerc A, Zhang X, Topaloglu H, et al. Mutations in the laminin α2-chain gene (LAMA2) cause merosin-deficient congenital muscular dystrophy. Nature Genet 1995;11:216-218
    • (1995) Nature Genet , vol.11 , pp. 216-218
    • Helbling-Leclerc, A.1    Zhang, X.2    Topaloglu, H.3
  • 28
    • 0023614188 scopus 로고
    • Dystrophin: The protein product of the Duchenne muscular dystrophy locus
    • Hoffman EP, Brown RH, Kunkel LM. Dystrophin: the protein product of the Duchenne muscular dystrophy locus. Cell 1987; 51:919-928
    • (1987) Cell , vol.51 , pp. 919-928
    • Hoffman, E.P.1    Brown, R.H.2    Kunkel, L.M.3
  • 29
    • 0024428185 scopus 로고
    • Improved diagnosis of Becker muscular dystrophy by dystrophin testing
    • Hoffman EP, Kunkel LM, Angelini C, et al. Improved diagnosis of Becker muscular dystrophy by dystrophin testing. Neurology 1989;39:1011-1017
    • (1989) Neurology , vol.39 , pp. 1011-1017
    • Hoffman, E.P.1    Kunkel, L.M.2    Angelini, C.3
  • 30
    • 0024284028 scopus 로고
    • A simple salting out procedure for extracting DNA from human nucleated cells
    • Miller SA, Dykes DD, Polesky HF. A simple salting out procedure for extracting DNA from human nucleated cells. Nucleic Acids Res 1988;16:1215
    • (1988) Nucleic Acids Res , vol.16 , pp. 1215
    • Miller, S.A.1    Dykes, D.D.2    Polesky, H.F.3
  • 31
    • 0028904169 scopus 로고
    • Genetic and biochemical normalization in female carriers of Duchenne muscular dystrophy: Evidence for failure of dystrophin production in dystrophin competent myonuclei
    • Pegoraro E, Schimke RN, Garcia C, et al. Genetic and biochemical normalization in female carriers of Duchenne muscular dystrophy: evidence for failure of dystrophin production in dystrophin competent myonuclei. Neurology 1995;45:677-690
    • (1995) Neurology , vol.45 , pp. 677-690
    • Pegoraro, E.1    Schimke, R.N.2    Garcia, C.3
  • 32
    • 0016207067 scopus 로고
    • Ribonucleic acid isolated by cesium chloride centrifugation
    • Glisin VR, Crkvenjadov R, Byus C. Ribonucleic acid isolated by cesium chloride centrifugation. Biochemistry 1974;13: 2633-2637
    • (1974) Biochemistry , vol.13 , pp. 2633-2637
    • Glisin, V.R.1    Crkvenjadov, R.2    Byus, C.3
  • 33
    • 0028229055 scopus 로고
    • Pathophysiology of sodium channelopathies: Studies of sodium channel expression by quantitative multiplex fluorescence polymerase chain reaction
    • Zhou J, Hoffman EP. Pathophysiology of sodium channelopathies: studies of sodium channel expression by quantitative multiplex fluorescence polymerase chain reaction. J Biol Chem 1994;269:18563-18571
    • (1994) J Biol Chem , vol.269 , pp. 18563-18571
    • Zhou, J.1    Hoffman, E.P.2
  • 34
    • 85035185704 scopus 로고    scopus 로고
    • Adhalinopathies: Complete biochemical deficiency patients are 5% of childhoodonset dystrophin-normal muscular dystrophy and most partial deficiency patients do not have gene mutations
    • in press
    • Duggan DJ, Fanin M, Pegoraro E, et al. Adhalinopathies: complete biochemical deficiency patients are 5% of childhoodonset dystrophin-normal muscular dystrophy and most partial deficiency patients do not have gene mutations. J Neurol Sci (in press)
    • J Neurol Sci
    • Duggan, D.J.1    Fanin, M.2    Pegoraro, E.3
  • 35
    • 18344413641 scopus 로고
    • Herlitz's junctional epidermolysis bullosa is linked to mutations in the gene (LAMC2) for the gamma-2 subunit on nicein/kalinin (laminin-5)
    • Aberdam D, Galliano MF, Vailly J, et al. Herlitz's junctional epidermolysis bullosa is linked to mutations in the gene (LAMC2) for the gamma-2 subunit on nicein/kalinin (laminin-5). Nature Genet 1994;6:299-304
    • (1994) Nature Genet , vol.6 , pp. 299-304
    • Aberdam, D.1    Galliano, M.F.2    Vailly, J.3
  • 36
    • 0025010542 scopus 로고
    • Molecular heterogeneity of basal laminae: Isoform of laminin and collagen IV at the neuromuscular junction and elsewhere
    • Sanes JR, Engvall E, Butkowski R, Hunter DD. Molecular heterogeneity of basal laminae: isoform of laminin and collagen IV at the neuromuscular junction and elsewhere. J Cell Biol 1990;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
  • 37
    • 0027222921 scopus 로고
    • Laminin variants: Why, where and when?
    • Engvall E. Laminin variants: why, where and when? Kidney Int 1993;43:2-6
    • (1993) Kidney Int , vol.43 , pp. 2-6
    • Engvall, E.1
  • 38
    • 0023970247 scopus 로고
    • Merosin, a protein specific for basement membrane of Schwann cells, striated muscle and trophoblast, is expressed late in nerve and muscle development
    • Leivo I, Engvall E. Merosin, a protein specific for basement membrane of Schwann cells, striated muscle and trophoblast, is expressed late in nerve and muscle development. Proc Natl Acad Sci USA 1990;85:1544-1548
    • (1990) Proc Natl Acad Sci USA , vol.85 , pp. 1544-1548
    • Leivo, I.1    Engvall, E.2
  • 39
    • 0029124239 scopus 로고
    • Expression of laminin subunits in human fetal skeletal muscle
    • Sewry CA, Chevallay M, Tomé FMS. Expression of laminin subunits in human fetal skeletal muscle. Histochem J 1995;27: 497-504
    • (1995) Histochem J , vol.27 , pp. 497-504
    • Sewry, C.A.1    Chevallay, M.2    Tomé, F.M.S.3
  • 40
    • 0025494189 scopus 로고
    • Distribution and isolation of four laminin variants; tissue restricted distribution of heterotrimers assembled from five different subunits
    • Engvall E, Earwicker D, Haaparanta T, et al. Distribution and isolation of four laminin variants; tissue restricted distribution of heterotrimers assembled from five different subunits. Cell Regul 1990;1:731-740
    • (1990) Cell Regul , vol.1 , pp. 731-740
    • Engvall, E.1    Earwicker, D.2    Haaparanta, T.3
  • 41
    • 0025358179 scopus 로고
    • MR imaging of the brain in five members of a family with Paelizeus-Merzbacher disease
    • Silverstein AM, Hirsh DK, Trobe JD, Gebarski SS. MR imaging of the brain in five members of a family with Paelizeus-Merzbacher disease. Am J Neuroradiol 1990;11:495-499
    • (1990) Am J Neuroradiol , vol.11 , pp. 495-499
    • Silverstein, A.M.1    Hirsh, D.K.2    Trobe, J.D.3    Gebarski, S.S.4
  • 42
    • 0028788685 scopus 로고
    • Demyelinating peripheral neuropathy in merosin-deficient congenital muscular dystrophy
    • Shorer Z, Philpot J, Muntoni F, et al. Demyelinating peripheral neuropathy in merosin-deficient congenital muscular dystrophy. J Child Neurol 1995;10:472-475
    • (1995) J Child Neurol , vol.10 , pp. 472-475
    • Shorer, Z.1    Philpot, J.2    Muntoni, F.3
  • 43
    • 0022628251 scopus 로고
    • Anti basement membrane antibodies in the serum of healthy subjects
    • Bernard A, Lauwerys R, Mahieu P, Foidart JM. Anti basement membrane antibodies in the serum of healthy subjects. N Engl J Med 1986;314:1456-1457
    • (1986) N Engl J Med , vol.314 , pp. 1456-1457
    • Bernard, A.1    Lauwerys, R.2    Mahieu, P.3    Foidart, J.M.4
  • 44
    • 0026024507 scopus 로고
    • Antibodies against galactosyl (α → 3) galactose in connective tissue diseases
    • Gabrielli A, Leoni P, Danieli G, et al. Antibodies against galactosyl (α → 3) galactose in connective tissue diseases. Arthritis Rheum 1991;34:375-376
    • (1991) Arthritis Rheum , vol.34 , pp. 375-376
    • Gabrielli, A.1    Leoni, P.2    Danieli, G.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.