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Volumn 20, Issue 5, 2007, Pages 583-589

Congenital myopathies

Author keywords

Congenital myopathies; Gene discovery; Pathobiology; Therapy

Indexed keywords

ALPHA ACTIN; BETA TROPOMYOSIN; COFILIN; MYOSIN HEAVY CHAIN BETA; SELENOPROTEIN; SELENOPROTEIN N; TROPOMYOSIN; UNCLASSIFIED DRUG;

EID: 34648854435     PISSN: 13507540     EISSN: None     Source Type: Journal    
DOI: 10.1097/WCO.0b013e3282ef6e69     Document Type: Review
Times cited : (28)

References (79)
  • 1
    • 0001478427 scopus 로고
    • A new congenital nonprogressive myopathy
    • Shy GM, Magee KR. A new congenital nonprogressive myopathy. Brain 1956; 79:610-621.
    • (1956) Brain , vol.79 , pp. 610-621
    • Shy, G.M.1    Magee, K.R.2
  • 2
    • 0030013872 scopus 로고    scopus 로고
    • Congenital myopathies
    • Goebel HH. Congenital myopathies. Semin Pediatr Neurol 1996; 3:152-161.
    • (1996) Semin Pediatr Neurol , vol.3 , pp. 152-161
    • Goebel, H.H.1
  • 3
    • 0032858915 scopus 로고    scopus 로고
    • Mutations in the skeletal muscle alpha-actin gene in patients with actin myopathy and nemaline myopathy
    • Nowak KJ, Wattanasirichaigoon D, Goebel HH, et al. Mutations in the skeletal muscle alpha-actin gene in patients with actin myopathy and nemaline myopathy. Nat Genet 1999; 23:208-212.
    • (1999) Nat Genet , vol.23 , pp. 208-212
    • Nowak, K.J.1    Wattanasirichaigoon, D.2    Goebel, H.H.3
  • 4
    • 34249049197 scopus 로고    scopus 로고
    • Lehtokari VL, Ceuterick-de Groote C, de Jonghe P, et al. Cap disease caused by heterozygous deletion of the beta-tropomyosin gene TPM2. Neuromuscul Disord 2007; 17:433-442. This paper describes the first gene identified for cap disease as mutated β-tropomyosin (TPM2). The mutation is a single amino acid deletion, a type of mutation not previously seen in TPM2, where other types of mutations have previously been associated with nemaline myopathy or distal arthrogryposis.
    • Lehtokari VL, Ceuterick-de Groote C, de Jonghe P, et al. Cap disease caused by heterozygous deletion of the beta-tropomyosin gene TPM2. Neuromuscul Disord 2007; 17:433-442. This paper describes the first gene identified for cap disease as mutated β-tropomyosin (TPM2). The mutation is a single amino acid deletion, a type of mutation not previously seen in TPM2, where other types of mutations have previously been associated with nemaline myopathy or distal arthrogryposis.
  • 5
    • 0027250785 scopus 로고
    • Mutations in the ryanodine receptor gene in central core disease and malignant hyperthermia
    • Quane KA, Healy JMS, Keating KE, et al. Mutations in the ryanodine receptor gene in central core disease and malignant hyperthermia. Nat Genet 1993; 5:51-55.
    • (1993) Nat Genet , vol.5 , pp. 51-55
    • Quane, K.A.1    Healy, J.M.S.2    Keating, K.E.3
  • 6
    • 0027291158 scopus 로고
    • A mutation in the human ryanodine receptor gene associated with central core disease
    • Zhang Y, Chen HS, Khanna VK, et al. A mutation in the human ryanodine receptor gene associated with central core disease. Nat Genet 1993; 5:46-50.
    • (1993) Nat Genet , vol.5 , pp. 46-50
    • Zhang, Y.1    Chen, H.S.2    Khanna, V.K.3
  • 7
    • 27644543614 scopus 로고    scopus 로고
    • Mutations in dynamin 2 cause dominant centronuclear myopathy
    • Bitoun M, Maugenre S, Jeannet PY, et al. Mutations in dynamin 2 cause dominant centronuclear myopathy. Nat Genet 2005; 37:1207-1209.
    • (2005) Nat Genet , vol.37 , pp. 1207-1209
    • Bitoun, M.1    Maugenre, S.2    Jeannet, P.Y.3
  • 8
    • 34047270223 scopus 로고    scopus 로고
    • Jungbluth H, Zhou H, Sewry CA, et al. Centronuclear myopathy due to a de novo dominant mutation in the skeletal muscle ryanodine receptor (RYR1) gene. Neuromuscul Disord 2007; 17:338-345. This paper suggests that mutations in the ryanodine receptor gene RYR1 may also result in a centronuclear myopathy histopathological phenotype and therefore that RYR1 mutation has to be considered if such a phenotype is seen on histopathological examination in addition to dynamin mutations and MTM1 mutation.
    • Jungbluth H, Zhou H, Sewry CA, et al. Centronuclear myopathy due to a de novo dominant mutation in the skeletal muscle ryanodine receptor (RYR1) gene. Neuromuscul Disord 2007; 17:338-345. This paper suggests that mutations in the ryanodine receptor gene RYR1 may also result in a centronuclear myopathy histopathological phenotype and therefore that RYR1 mutation has to be considered if such a phenotype is seen on histopathological examination in addition to dynamin mutations and MTM1 mutation.
  • 9
    • 9144245756 scopus 로고    scopus 로고
    • Actin mutations are one cause of congenital fibre type disproportion
    • Laing NG, Clarke NF, Dye DE, et al. Actin mutations are one cause of congenital fibre type disproportion. Ann Neurol 2004; 56:689-694.
    • (2004) Ann Neurol , vol.56 , pp. 689-694
    • Laing, N.G.1    Clarke, N.F.2    Dye, D.E.3
  • 10
    • 33644819072 scopus 로고    scopus 로고
    • Clarke NF, Kidson W, Quijano-Roy S, et al. SEPN1: associated with congenital fiber-type disproportion and insulin resistance. Ann Neurol 2006; 59:546-552. This paper demonstrates for the first time that SEPN1 mutations may account for patients with a working diagnosis of congenital fibre type disproportion.
    • Clarke NF, Kidson W, Quijano-Roy S, et al. SEPN1: associated with congenital fiber-type disproportion and insulin resistance. Ann Neurol 2006; 59:546-552. This paper demonstrates for the first time that SEPN1 mutations may account for patients with a working diagnosis of congenital fibre type disproportion.
  • 11
    • 11144353966 scopus 로고    scopus 로고
    • Desmin-related myopathy with Mallory body-like inclusions is caused by mutations of the selenoprotein N gene
    • Ferreiro A, Ceuterick-de Groote C, Marks JJ, et al. Desmin-related myopathy with Mallory body-like inclusions is caused by mutations of the selenoprotein N gene. Ann Neurol 2004; 55:676-686.
    • (2004) Ann Neurol , vol.55 , pp. 676-686
    • Ferreiro, A.1    Ceuterick-de Groote, C.2    Marks, J.J.3
  • 12
    • 0036260805 scopus 로고    scopus 로고
    • A recessive form of central core disease, transiently presenting as multiminicore disease, is associated with a homozygous mutation in the ryanodine receptor type 1 gene
    • Ferreiro A, Monnier N, Romero NB, et al. A recessive form of central core disease, transiently presenting as multiminicore disease, is associated with a homozygous mutation in the ryanodine receptor type 1 gene. Ann Neurol 2002; 51:750-759.
    • (2002) Ann Neurol , vol.51 , pp. 750-759
    • Ferreiro, A.1    Monnier, N.2    Romero, N.B.3
  • 13
    • 19044375929 scopus 로고    scopus 로고
    • Mutations of the selenoprotein N gene, which is implicated in rigid spine muscular dystrophy, cause the classical phenotype of multiminicore disease: Reassessing the nosology of early-onset myopathies
    • Ferreiro A, Quijano-Roy S, Pichereau C, et al. Mutations of the selenoprotein N gene, which is implicated in rigid spine muscular dystrophy, cause the classical phenotype of multiminicore disease: reassessing the nosology of early-onset myopathies. Am J Hum Genet 2002; 71:739-749.
    • (2002) Am J Hum Genet , vol.71 , pp. 739-749
    • Ferreiro, A.1    Quijano-Roy, S.2    Pichereau, C.3
  • 14
    • 0141535360 scopus 로고    scopus 로고
    • Myosin storage myopathy associated with a heterozygous missense mutation in MYH7
    • Tajsharghi H, Thornell LE, Lindberg C, et al. Myosin storage myopathy associated with a heterozygous missense mutation in MYH7. Ann Neurol 2003; 54:494-500.
    • (2003) Ann Neurol , vol.54 , pp. 494-500
    • Tajsharghi, H.1    Thornell, L.E.2    Lindberg, C.3
  • 15
    • 9844265393 scopus 로고    scopus 로고
    • Mutations in the MTM1 gene implicated in X-linked myotubular myopathy. ENMC International Consortium on Myotubular Myopathy. European Neuro-Muscular Center
    • Laporte J, Guiraud-Chaumeil C, Vincent MC, et al. Mutations in the MTM1 gene implicated in X-linked myotubular myopathy. ENMC International Consortium on Myotubular Myopathy. European Neuro-Muscular Center. Hum Mol Genet 1997; 6:1505-1511.
    • (1997) Hum Mol Genet , vol.6 , pp. 1505-1511
    • Laporte, J.1    Guiraud-Chaumeil, C.2    Vincent, M.C.3
  • 16
    • 33845977054 scopus 로고    scopus 로고
    • Agrawal PB, Greenleaf RS, Tomczak KK, et al. Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2. Am J Hum Genet 2007; 80:162-167. This paper identifies the sixth known genetic cause of nemaline myopathy as mutated muscle-specific cofilin CFL2. The authors found a homozygous mutation of CFL2 segregating with nemaline myopathy in one family of Middle Eastern origin.
    • Agrawal PB, Greenleaf RS, Tomczak KK, et al. Nemaline myopathy with minicores caused by mutation of the CFL2 gene encoding the skeletal muscle actin-binding protein, cofilin-2. Am J Hum Genet 2007; 80:162-167. This paper identifies the sixth known genetic cause of nemaline myopathy as mutated muscle-specific cofilin CFL2. The authors found a homozygous mutation of CFL2 segregating with nemaline myopathy in one family of Middle Eastern origin.
  • 17
    • 13044312720 scopus 로고    scopus 로고
    • Mutations in the nebulin gene associated with autosomal recessive nemaline myopathy
    • Pelin K, Hilpela P, Donner K, et al. Mutations in the nebulin gene associated with autosomal recessive nemaline myopathy. Proc Natl Acad Sci U S A 1999; 96:2305-2310.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 2305-2310
    • Pelin, K.1    Hilpela, P.2    Donner, K.3
  • 18
    • 0036133714 scopus 로고    scopus 로고
    • Mutations in the β-tropomyosin (TPM2) gene: A rare cause of nemaline myopathy
    • Donner K, Ollikainen M, Ridanpää M, et al. Mutations in the β-tropomyosin (TPM2) gene: a rare cause of nemaline myopathy. Neuromuscul Disord 2002; 12:151-158.
    • (2002) Neuromuscul Disord , vol.12 , pp. 151-158
    • Donner, K.1    Ollikainen, M.2    Ridanpää, M.3
  • 19
    • 0028852835 scopus 로고
    • A mutation in the a-tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy
    • Laing NG, Wilton SD, Akkari PA, et al. A mutation in the a-tropomyosin gene TPM3 associated with autosomal dominant nemaline myopathy. Nat Genet 1995; 9:75-79.
    • (1995) Nat Genet , vol.9 , pp. 75-79
    • Laing, N.G.1    Wilton, S.D.2    Akkari, P.A.3
  • 20
    • 0033799745 scopus 로고    scopus 로고
    • A novel nemaline myopathy in the Amish caused by a mutation in troponin T1
    • Johnston JJ, Kelley RI, Crawford TO, et al. A novel nemaline myopathy in the Amish caused by a mutation in troponin T1. Am J Hum Genet 2000; 67:814-821.
    • (2000) Am J Hum Genet , vol.67 , pp. 814-821
    • Johnston, J.J.1    Kelley, R.I.2    Crawford, T.O.3
  • 21
    • 16344367908 scopus 로고    scopus 로고
    • Commonality of TRIM32 mutation in causing sarcotubular myopathy and LGMD2H
    • Schoser BG, Frosk P, Engel AG, et al. Commonality of TRIM32 mutation in causing sarcotubular myopathy and LGMD2H. Ann Neurol 2005; 57:591-595.
    • (2005) Ann Neurol , vol.57 , pp. 591-595
    • Schoser, B.G.1    Frosk, P.2    Engel, A.G.3
  • 22
    • 33645650403 scopus 로고    scopus 로고
    • A mutation in myotilin causes spheroid body myopathy
    • Foroud T, Pankratz N, Batchman AP, et al. A mutation in myotilin causes spheroid body myopathy. Neurology 2005; 65:1936-1940.
    • (2005) Neurology , vol.65 , pp. 1936-1940
    • Foroud, T.1    Pankratz, N.2    Batchman, A.P.3
  • 23
    • 17044440789 scopus 로고    scopus 로고
    • Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease)
    • Nishino I, Fu J, Tanji K, et al. Primary LAMP-2 deficiency causes X-linked vacuolar cardiomyopathy and myopathy (Danon disease). Nature 2000; 406:906-910.
    • (2000) Nature , vol.406 , pp. 906-910
    • Nishino, I.1    Fu, J.2    Tanji, K.3
  • 24
    • 33847623295 scopus 로고    scopus 로고
    • Nowak KJ, Sewry CA, Navarro C, et al. Nemaline myopathy caused by absence of alpha-skeletal muscle actin. Ann Neurol 2007; 61:175-184. This paper describes for the first time patients from various consanguineous ethnic groups homozygous for different null mutations in the skeletal muscle actin gene ACTA1. The patients have no skeletal actin but have increased cardiac actin in their skeletal muscles, cardiac actin being the fetal isoform of actin in skeletal muscle. The increased cardiac actin partially compensates for the absence of skeletal actin. Some of the patients have zebra bodies in their muscle, suggesting that mutations of actin may be the cause of the previously described zebra body myopathy.
    • Nowak KJ, Sewry CA, Navarro C, et al. Nemaline myopathy caused by absence of alpha-skeletal muscle actin. Ann Neurol 2007; 61:175-184. This paper describes for the first time patients from various consanguineous ethnic groups homozygous for different null mutations in the skeletal muscle actin gene ACTA1. The patients have no skeletal actin but have increased cardiac actin in their skeletal muscles, cardiac actin being the fetal isoform of actin in skeletal muscle. The increased cardiac actin partially compensates for the absence of skeletal actin. Some of the patients have zebra bodies in their muscle, suggesting that mutations of actin may be the cause of the previously described zebra body myopathy.
  • 25
    • 33847146380 scopus 로고    scopus 로고
    • A congenital myopathy with diaphragmatic weakness not linked to the SMARD1 locus
    • This paper suggests the existence of a novel congenital myopathy
    • Hartley L, Kinali M, Knight R, et al. A congenital myopathy with diaphragmatic weakness not linked to the SMARD1 locus. Neuromuscul Disord 2007; 17:174-179. This paper suggests the existence of a novel congenital myopathy.
    • (2007) Neuromuscul Disord , vol.17 , pp. 174-179
    • Hartley, L.1    Kinali, M.2    Knight, R.3
  • 26
    • 33749155966 scopus 로고    scopus 로고
    • A benign congenital myopathy in an inbred Samaritan family
    • This paper suggests the existence of a novel congenital myopathy
    • Lev D, Sadeh M, Watemberg N, et al. A benign congenital myopathy in an inbred Samaritan family. Eur J Paediatr Neurol 2006; 10:182-185. This paper suggests the existence of a novel congenital myopathy.
    • (2006) Eur J Paediatr Neurol , vol.10 , pp. 182-185
    • Lev, D.1    Sadeh, M.2    Watemberg, N.3
  • 27
    • 33846123642 scopus 로고    scopus 로고
    • A benign congenital myopathy in an inbred Samaritan family
    • Liewluck T. A benign congenital myopathy in an inbred Samaritan family. Eur J Paediatr Neurol 2007; 11:55.
    • (2007) Eur J Paediatr Neurol , vol.11 , pp. 55
    • Liewluck, T.1
  • 28
    • 0037369803 scopus 로고    scopus 로고
    • Mutations in genes encoding fast-twitch contractile proteins cause distal arthrogryposis syndromes
    • Sung SS, Brassington AM, Grannatt K, et al. Mutations in genes encoding fast-twitch contractile proteins cause distal arthrogryposis syndromes. Am J Hum Genet 2003; 72:681-690.
    • (2003) Am J Hum Genet , vol.72 , pp. 681-690
    • Sung, S.S.1    Brassington, A.M.2    Grannatt, K.3
  • 30
    • 0016661085 scopus 로고
    • Zebra body myopathy. Clinical, histochemical and ultrastructural studies
    • Lake BD, Wilson J. Zebra body myopathy. Clinical, histochemical and ultrastructural studies. J Neurol Sci 1975; 24:437-446.
    • (1975) J Neurol Sci , vol.24 , pp. 437-446
    • Lake, B.D.1    Wilson, J.2
  • 31
    • 33751094327 scopus 로고    scopus 로고
    • Zhou H, Brockington M, Jungbluth H, et al. Epigenetic allele silencing unveils recessive RYR1 mutations in core myopathies. Am J Hum Genet 2006; 79:859-868. This paper demonstrates remarkably that some patients with recessive RYR1-based core myopathies have the disease because in their muscles their normal RYR1-allele has been epigenetically silenced. This was the first determination of the mechanism of an epigenetic phenomenon in the congenital myopathies.
    • Zhou H, Brockington M, Jungbluth H, et al. Epigenetic allele silencing unveils recessive RYR1 mutations in core myopathies. Am J Hum Genet 2006; 79:859-868. This paper demonstrates remarkably that some patients with recessive RYR1-based core myopathies have the disease because in their muscles their normal RYR1-allele has been epigenetically silenced. This was the first determination of the mechanism of an epigenetic phenomenon in the congenital myopathies.
  • 32
    • 33748752700 scopus 로고    scopus 로고
    • Zhou H, Yamaguchi N, Xu L, et al. Characterization of recessive RYR1 mutations in core myopathies. Hum Mol Genet 2006; 15:2791-2803. This paper suggests that recessive core disease caused by mutations in RYR1 is more common than previously thought.
    • Zhou H, Yamaguchi N, Xu L, et al. Characterization of recessive RYR1 mutations in core myopathies. Hum Mol Genet 2006; 15:2791-2803. This paper suggests that recessive core disease caused by mutations in RYR1 is more common than previously thought.
  • 33
    • 34247573351 scopus 로고    scopus 로고
    • Kossugue PM, Paim JF, Navarro MM, et al. Central core disease due to recessive mutations in RYR1 gene: Is it more common than described? Muscle Nerve 2007; 35:670-674. This paper suggests that recessive core disease caused by mutations in RYR1 is more common than previously thought.
    • Kossugue PM, Paim JF, Navarro MM, et al. Central core disease due to recessive mutations in RYR1 gene: Is it more common than described? Muscle Nerve 2007; 35:670-674. This paper suggests that recessive core disease caused by mutations in RYR1 is more common than previously thought.
  • 34
    • 33745085922 scopus 로고    scopus 로고
    • Wu S, Ibarra MC, Malicdan MC, et al. Central core disease is due to RYR1 mutations in more than 90% of patients. Brain 2006; 129:1470-1480. This is an excellent review of the current knowledge of RYR1 mutations causing central core disease in the Japanese population. It demonstrates many mutations outside the known hotspots.
    • Wu S, Ibarra MC, Malicdan MC, et al. Central core disease is due to RYR1 mutations in more than 90% of patients. Brain 2006; 129:1470-1480. This is an excellent review of the current knowledge of RYR1 mutations causing central core disease in the Japanese population. It demonstrates many mutations outside the known hotspots.
  • 35
    • 33748997392 scopus 로고    scopus 로고
    • Robinson R, Carpenter D, Shaw MA, et al. Mutations in RYR1 in malignant hyperthermia and central core disease. Hum Mutat 2006; 27:977-989. This is an excellent review of RYR1 mutations. It demonstrates many mutations outside the known hotspots.
    • Robinson R, Carpenter D, Shaw MA, et al. Mutations in RYR1 in malignant hyperthermia and central core disease. Hum Mutat 2006; 27:977-989. This is an excellent review of RYR1 mutations. It demonstrates many mutations outside the known hotspots.
  • 36
    • 33645532321 scopus 로고    scopus 로고
    • A single homozygous point mutation in a 3′ untranslated region motif of selenoprotein N mRNA causes SEPN1-related myopathy
    • Allamand V, Richard P, Lescure A, et al. A single homozygous point mutation in a 3′ untranslated region motif of selenoprotein N mRNA causes SEPN1-related myopathy. EMBO Rep 2006; 7:450-454.
    • (2006) EMBO Rep , vol.7 , pp. 450-454
    • Allamand, V.1    Richard, P.2    Lescure, A.3
  • 37
    • 33746061222 scopus 로고    scopus 로고
    • Molecular mechanism of rigid spine with muscular dystrophy type 1 caused by novel mutations of selenoprotein N gene
    • Okamoto Y, Takashima H, Higuchi I, et al. Molecular mechanism of rigid spine with muscular dystrophy type 1 caused by novel mutations of selenoprotein N gene. Neurogenetics 2006; 7:175-183.
    • (2006) Neurogenetics , vol.7 , pp. 175-183
    • Okamoto, Y.1    Takashima, H.2    Higuchi, I.3
  • 38
    • 33847021853 scopus 로고    scopus 로고
    • Functional effects of mutations identified in patients with multiminicore disease
    • Zorzato F, Jungbluth H, Zhou H, et al. Functional effects of mutations identified in patients with multiminicore disease. IUBMB Life 2007; 59:14-20.
    • (2007) IUBMB Life , vol.59 , pp. 14-20
    • Zorzato, F.1    Jungbluth, H.2    Zhou, H.3
  • 39
    • 0028332473 scopus 로고
    • Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene
    • Takeshima H, Iino M, Takekura H, et al. Excitation-contraction uncoupling and muscular degeneration in mice lacking functional skeletal muscle ryanodine-receptor gene. Nature 1994; 369:556-559.
    • (1994) Nature , vol.369 , pp. 556-559
    • Takeshima, H.1    Iino, M.2    Takekura, H.3
  • 40
    • 33845932952 scopus 로고    scopus 로고
    • Two central core disease (CCD) deletions in the C-terminal region of RYR1 alter muscle excitation-contraction (EC) coupling by distinct mechanisms
    • Lyfenko AD, Ducreux S, Wang Y, et al. Two central core disease (CCD) deletions in the C-terminal region of RYR1 alter muscle excitation-contraction (EC) coupling by distinct mechanisms. Hum Mutat 2007; 28:61-68.
    • (2007) Hum Mutat , vol.28 , pp. 61-68
    • Lyfenko, A.D.1    Ducreux, S.2    Wang, Y.3
  • 41
    • 33645796192 scopus 로고    scopus 로고
    • Functional properties of ryanodine receptors carrying three amino acid substitutions identified in patients affected by multiminicore disease and central core disease, expressed in immortalized lymphocytes
    • Ducreux S, Zorzato F, Ferreiro A, et al. Functional properties of ryanodine receptors carrying three amino acid substitutions identified in patients affected by multiminicore disease and central core disease, expressed in immortalized lymphocytes. Biochem J 2006; 395:259-266.
    • (2006) Biochem J , vol.395 , pp. 259-266
    • Ducreux, S.1    Zorzato, F.2    Ferreiro, A.3
  • 42
    • 33644882215 scopus 로고    scopus 로고
    • Heat- and anesthesia-induced malignant hyperthermia in an RyR1 knock-in mouse
    • Chelu MG, Goonasekera SA, Durham WJ, et al. Heat- and anesthesia-induced malignant hyperthermia in an RyR1 knock-in mouse. Faseb J 2006; 20:329-330.
    • (2006) Faseb J , vol.20 , pp. 329-330
    • Chelu, M.G.1    Goonasekera, S.A.2    Durham, W.J.3
  • 43
    • 33748331343 scopus 로고    scopus 로고
    • Dulhunty AF, Beard NA, Pouliquin P, Kimura T. Novel regulators of RyR Ca2+ release channels: insight into molecular changes in genetically-linked myopathies. J Muscle Res Cell Motil 2006; 27:351-365. This is an excellent review of the current knowledge of the pathobiology of RYR1 gene mutations. The authors also introduce the possibility of a role for RYR1 in myotonic dystrophy myopathy.
    • Dulhunty AF, Beard NA, Pouliquin P, Kimura T. Novel regulators of RyR Ca2+ release channels: insight into molecular changes in genetically-linked myopathies. J Muscle Res Cell Motil 2006; 27:351-365. This is an excellent review of the current knowledge of the pathobiology of RYR1 gene mutations. The authors also introduce the possibility of a role for RYR1 in myotonic dystrophy myopathy.
  • 44
    • 33845934128 scopus 로고    scopus 로고
    • Fischer D, Herasse M, Ferreiro A, et al. Muscle imaging in dominant core myopathies linked or unlinked to the ryanodine receptor 1 gene. Neurology 2006; 67:2217-2220. This very useful paper describes the differences in the pattern of muscles affected in RYR1 or non-RYR1 core myopathies as seen with MRI
    • Fischer D, Herasse M, Ferreiro A, et al. Muscle imaging in dominant core myopathies linked or unlinked to the ryanodine receptor 1 gene. Neurology 2006; 67:2217-2220. This very useful paper describes the differences in the pattern of muscles affected in RYR1 or non-RYR1 core myopathies as seen with MRI
  • 45
    • 33846097627 scopus 로고    scopus 로고
    • Herasse M, Parain K, Marty I, et al. Abnormal distribution of calcium-handling proteins: a novel distinctive marker in core myopathies. J Neuropathol Exp Neurol 2007; 66:57-65. This paper suggests that RYR1 and non-RYR1 related myopathies may be distinguished by immunohistochemistry for RyR1, which is absent from RYR1-related cores.
    • Herasse M, Parain K, Marty I, et al. Abnormal distribution of calcium-handling proteins: a novel distinctive marker in core myopathies. J Neuropathol Exp Neurol 2007; 66:57-65. This paper suggests that RYR1 and non-RYR1 related myopathies may be distinguished by immunohistochemistry for RyR1, which is absent from RYR1-related cores.
  • 46
    • 33646250165 scopus 로고    scopus 로고
    • Lujan Feliu-Pascual A, Shelton GD, Targett MP, et al. Inherited myopathy of great Danes. J Small Anim Pract 2006; 47:249-254.
    • Lujan Feliu-Pascual A, Shelton GD, Targett MP, et al. Inherited myopathy of great Danes. J Small Anim Pract 2006; 47:249-254.
  • 47
    • 33846597651 scopus 로고    scopus 로고
    • Autosomal dominant nemaline myopathy: A new phenotype unlinked to previously known genetic loci
    • This paper identifies further genetic heterogeneity for dominant nemaline myopathy, suggesting that there is yet another locus to find
    • Jeannet PY, Mittaz L, Dunand M, et al. Autosomal dominant nemaline myopathy: a new phenotype unlinked to previously known genetic loci. Neuromuscul Disord 2007; 17:6-12. This paper identifies further genetic heterogeneity for dominant nemaline myopathy, suggesting that there is yet another locus to find.
    • (2007) Neuromuscul Disord , vol.17 , pp. 6-12
    • Jeannet, P.Y.1    Mittaz, L.2    Dunand, M.3
  • 48
    • 0028233412 scopus 로고    scopus 로고
    • Dunwoodie SL, Joya JE, Arkell RM. Hardeman EC Multiple regions of the human cardiac actin gene are necessary for maturation-based expression in striated muscle. J Biol Chem 1994; 269:12212-12219.
    • Dunwoodie SL, Joya JE, Arkell RM. Hardeman EC Multiple regions of the human cardiac actin gene are necessary for maturation-based expression in striated muscle. J Biol Chem 1994; 269:12212-12219.
  • 49
    • 28244446353 scopus 로고    scopus 로고
    • Defining alpha-skeletal and alphacardiac actin expression in human heart and skeletal muscle explains the absence of cardiac involvement in ACTA1 nemaline myopathy
    • Ilkovski B, Clement S, Sewry C, et al. Defining alpha-skeletal and alphacardiac actin expression in human heart and skeletal muscle explains the absence of cardiac involvement in ACTA1 nemaline myopathy. Neuromuscul Disord 2005; 15:829-835.
    • (2005) Neuromuscul Disord , vol.15 , pp. 829-835
    • Ilkovski, B.1    Clement, S.2    Sewry, C.3
  • 50
    • 30344471516 scopus 로고    scopus 로고
    • Adult-onset nemaline myopathy and monoclonal gammopathy
    • Keller CE, Hays AP, Rowland LP, et al. Adult-onset nemaline myopathy and monoclonal gammopathy. Arch Neurol 2006; 63:132-134.
    • (2006) Arch Neurol , vol.63 , pp. 132-134
    • Keller, C.E.1    Hays, A.P.2    Rowland, L.P.3
  • 51
    • 33847677261 scopus 로고    scopus 로고
    • Camptocormia in a patient with Parkinson disease and a myopathy with nemaline rods
    • Ozer F, Ozturk O, Meral H, et al. Camptocormia in a patient with Parkinson disease and a myopathy with nemaline rods. Am J Phys Med Rehabil 2007; 86:3-6.
    • (2007) Am J Phys Med Rehabil , vol.86 , pp. 3-6
    • Ozer, F.1    Ozturk, O.2    Meral, H.3
  • 52
    • 33846947179 scopus 로고    scopus 로고
    • Variable presentation of nemaline myopathy: Novel mutation of alpha actin gene
    • Bouldin AA, Parisi MA, Laing N, et al. Variable presentation of nemaline myopathy: novel mutation of alpha actin gene. Muscle Nerve 2007; 35:254-258.
    • (2007) Muscle Nerve , vol.35 , pp. 254-258
    • Bouldin, A.A.1    Parisi, M.A.2    Laing, N.3
  • 53
    • 33748360319 scopus 로고    scopus 로고
    • Identification of 45 novel mutations in the nebulin gene associated with autosomal recessive nemaline myopathy
    • Lehtokari VL, Pelin K, Sandbacka M, et al. Identification of 45 novel mutations in the nebulin gene associated with autosomal recessive nemaline myopathy. Hum Mutat 2006; 27:946-956.
    • (2006) Hum Mutat , vol.27 , pp. 946-956
    • Lehtokari, V.L.1    Pelin, K.2    Sandbacka, M.3
  • 54
    • 30644474315 scopus 로고    scopus 로고
    • NG 138th ENMC Workshop: Nemaline Myopathy, 20-22 May 2005, Naarden, The Netherlands
    • Wallgren-Pettersson C. Laing NG 138th ENMC Workshop: Nemaline Myopathy, 20-22 May 2005, Naarden, The Netherlands. Neuromuscul Disord 2006; 16:54-60.
    • (2006) Neuromuscul Disord , vol.16 , pp. 54-60
    • Laing, W.C.1
  • 55
    • 31944440024 scopus 로고    scopus 로고
    • Autosomal dominant nemaline myopathy with intranuclear rods due to mutation of the skeletal muscle ACTA1 gene: Clinical and pathological variability within a kindred
    • Hutchinson DO, Charlton A, Laing NG, et al. Autosomal dominant nemaline myopathy with intranuclear rods due to mutation of the skeletal muscle ACTA1 gene: Clinical and pathological variability within a kindred. Neuromuscul Disord 2006; 16:113-121.
    • (2006) Neuromuscul Disord , vol.16 , pp. 113-121
    • Hutchinson, D.O.1    Charlton, A.2    Laing, N.G.3
  • 56
  • 57
    • 33748699638 scopus 로고    scopus 로고
    • Wallefeld W, Krause S, Nowak KJ, et al. Severe nemaline myopathy caused by mutations of the stop codon of the skeletal muscle alpha actin gene (ACTA1). Neuromuscul Disord 2006; 16:541-547. This paper for the first time identifies severely affected nemaline myopathy patients with mutations of the normal ACTA1 stop codon. The muscle in these patients is extremely dystrophic.
    • Wallefeld W, Krause S, Nowak KJ, et al. Severe nemaline myopathy caused by mutations of the stop codon of the skeletal muscle alpha actin gene (ACTA1). Neuromuscul Disord 2006; 16:541-547. This paper for the first time identifies severely affected nemaline myopathy patients with mutations of the normal ACTA1 stop codon. The muscle in these patients is extremely dystrophic.
  • 58
    • 33746035315 scopus 로고    scopus 로고
    • Patient with actin aggregate myopathy and not formerly identified ACTA1 mutation is heterozygous for the Gly15Arg mutation of ACTA1, which has previously been associated with actinopathy
    • Goebel HH, Brockman K, Bonnemann CG, et al. Patient with actin aggregate myopathy and not formerly identified ACTA1 mutation is heterozygous for the Gly15Arg mutation of ACTA1, which has previously been associated with actinopathy. J Child Neurol 2006; 21:545.
    • (2006) J Child Neurol , vol.21 , pp. 545
    • Goebel, H.H.1    Brockman, K.2    Bonnemann, C.G.3
  • 59
    • 1842433696 scopus 로고    scopus 로고
    • Actin-related myopathy without any missense mutation in the ACTA1 gene
    • Goebel HH, Brockmann K, Bonnemann CG, et al. Actin-related myopathy without any missense mutation in the ACTA1 gene. J Child Neurol 2004; 19:149-153.
    • (2004) J Child Neurol , vol.19 , pp. 149-153
    • Goebel, H.H.1    Brockmann, K.2    Bonnemann, C.G.3
  • 60
    • 34250854550 scopus 로고    scopus 로고
    • Wallgren-Pettersson C, Lehtokari VL, Kalimo H, et al. Distal myopathy caused by homozygous missense mutations in the nebulin gene. Brain 2007; 130:1465-1476. This remarkable paper demonstrates that patients homozygous for missense mutations in the nebulin gene (NEB) develop an early-onset distal myopathy similar to the one caused by certain mutations in slow-skeletal/β-cardiac myosin (MYH7). The same NEB missense mutations had previously been shown to cause nemaline myopathy when inherited with frameshift, nonsense or splice-site mutations in the other NEB allele.
    • Wallgren-Pettersson C, Lehtokari VL, Kalimo H, et al. Distal myopathy caused by homozygous missense mutations in the nebulin gene. Brain 2007; 130:1465-1476. This remarkable paper demonstrates that patients homozygous for missense mutations in the nebulin gene (NEB) develop an early-onset distal myopathy similar to the one caused by certain mutations in slow-skeletal/β-cardiac myosin (MYH7). The same NEB missense mutations had previously been shown to cause nemaline myopathy when inherited with frameshift, nonsense or splice-site mutations in the other NEB allele.
  • 61
    • 4544374719 scopus 로고    scopus 로고
    • Mutations in the slow skeletal muscle fiber myosin heavy chain gene (MYH7) cause Laing early-onset distal myopathy (MPD1)
    • Meredith C, Herrmann R, Parry C, et al. Mutations in the slow skeletal muscle fiber myosin heavy chain gene (MYH7) cause Laing early-onset distal myopathy (MPD1). Am J Hum Genet 2004; 75:703-708.
    • (2004) Am J Hum Genet , vol.75 , pp. 703-708
    • Meredith, C.1    Herrmann, R.2    Parry, C.3
  • 62
    • 33947541830 scopus 로고    scopus 로고
    • Distal arthrogryposis and muscle weakness associated with a beta-tropomyosin mutation
    • Tajsharghi H, Kimber E, Holmgren D, et al. Distal arthrogryposis and muscle weakness associated with a beta-tropomyosin mutation. Neurology 2007; 68:772-775.
    • (2007) Neurology , vol.68 , pp. 772-775
    • Tajsharghi, H.1    Kimber, E.2    Holmgren, D.3
  • 63
    • 0032723891 scopus 로고    scopus 로고
    • Homozygosity for a nonsense mutation in the alpha-tropomyosin gene TPM3 in a patient with severe infantile nemaline myopathy
    • Tan P, Briner J, Boltshauser E, et al. Homozygosity for a nonsense mutation in the alpha-tropomyosin gene TPM3 in a patient with severe infantile nemaline myopathy. Neuromusc Disord 1999; 9:573-579.
    • (1999) Neuromusc Disord , vol.9 , pp. 573-579
    • Tan, P.1    Briner, J.2    Boltshauser, E.3
  • 64
    • 33745243854 scopus 로고    scopus 로고
    • Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle
    • This paper demonstrates, remarkably, that knockout mice lacking any nebulin can survive after birth. Thin filaments are present in the nebulin knockout mouse muscle though of abnormal length and thus there are fall-back mechanisms that can control thin filament length in the absence of nebulin
    • Bang ML, Li X, Littlefield R, et al. Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle. J Cell Biol 2006; 173:905-916. This paper demonstrates, remarkably, that knockout mice lacking any nebulin can survive after birth. Thin filaments are present in the nebulin knockout mouse muscle though of abnormal length and thus there are fall-back mechanisms that can control thin filament length in the absence of nebulin.
    • (2006) J Cell Biol , vol.173 , pp. 905-916
    • Bang, M.L.1    Li, X.2    Littlefield, R.3
  • 65
    • 33748058496 scopus 로고    scopus 로고
    • Witt CC, Burkart C, Labeit D, et al. Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo. EMBO J 2006; 25:3843-3855. This paper demonstrates, remarkably, that knockout mice lacking any nebulin can survive after birth. Thin filaments are present in the nebulin knockout mouse muscle though of abnormal length and thus there are fall-back mechanisms that can control thin filament length in the absence of nebulin.
    • Witt CC, Burkart C, Labeit D, et al. Nebulin regulates thin filament length, contractility, and Z-disk structure in vivo. EMBO J 2006; 25:3843-3855. This paper demonstrates, remarkably, that knockout mice lacking any nebulin can survive after birth. Thin filaments are present in the nebulin knockout mouse muscle though of abnormal length and thus there are fall-back mechanisms that can control thin filament length in the absence of nebulin.
  • 66
    • 33747881610 scopus 로고    scopus 로고
    • Sanoudou D, Corbett MA, Han M, et al. Skeletal muscle repair in a mouse model of nemaline myopathy. Hum Mol Genet 2006; 15:2603-2612. This paper suggests that there is ongoing repair, regeneration and immature muscle fibres in the slow α-tropomyosin Met9Arg mouse model of nemaline myopathy.
    • Sanoudou D, Corbett MA, Han M, et al. Skeletal muscle repair in a mouse model of nemaline myopathy. Hum Mol Genet 2006; 15:2603-2612. This paper suggests that there is ongoing repair, regeneration and immature muscle fibres in the slow α-tropomyosin Met9Arg mouse model of nemaline myopathy.
  • 67
    • 0037447073 scopus 로고    scopus 로고
    • Expression profiling reveals altered satellite cell numbers and glycolytic enzyme transcription in nemaline myopathy muscle
    • Sanoudou D, Haslett JN, Kho AT, et al. Expression profiling reveals altered satellite cell numbers and glycolytic enzyme transcription in nemaline myopathy muscle. Proc Natl Acad Sci U S A 2003; 100:4666-4671.
    • (2003) Proc Natl Acad Sci U S A , vol.100 , pp. 4666-4671
    • Sanoudou, D.1    Haslett, J.N.2    Kho, A.T.3
  • 68
    • 1842576559 scopus 로고    scopus 로고
    • Molecular classification of nemaline myopathies: "nontyping" specimens exhibit unique patterns of gene expression
    • Sanoudou D, Frieden LA, Haslett JN, et al. Molecular classification of nemaline myopathies: "nontyping" specimens exhibit unique patterns of gene expression. Neurobiol Dis 2004; 15:590-600.
    • (2004) Neurobiol Dis , vol.15 , pp. 590-600
    • Sanoudou, D.1    Frieden, L.A.2    Haslett, J.N.3
  • 69
    • 33748529918 scopus 로고    scopus 로고
    • Fatal hypertrophic cardiomyopathy and nemaline myopathy associated with ACTA1 K336E mutation
    • D'Amico A, Graziano C, Pacileo G, et al. Fatal hypertrophic cardiomyopathy and nemaline myopathy associated with ACTA1 K336E mutation. Neuromuscul Disord 2006; 16:548-552.
    • (2006) Neuromuscul Disord , vol.16 , pp. 548-552
    • D'Amico, A.1    Graziano, C.2    Pacileo, G.3
  • 70
    • 33847377664 scopus 로고    scopus 로고
    • Robinson P, Lipscomb S, Preston LC, et al. Mutations in fast skeletal troponin I, troponin T, and beta-tropomyosin that cause distal arthrogryposis all increase contractile function. Faseb J 2007; 21:896-905. This paper demonstrates that mutations in three different proteins that lead to distal arthrogryposis all increase muscle contractility, a remarkable pathobiological consensus.
    • Robinson P, Lipscomb S, Preston LC, et al. Mutations in fast skeletal troponin I, troponin T, and beta-tropomyosin that cause distal arthrogryposis all increase contractile function. Faseb J 2007; 21:896-905. This paper demonstrates that mutations in three different proteins that lead to distal arthrogryposis all increase muscle contractility, a remarkable pathobiological consensus.
  • 72
    • 33749261091 scopus 로고    scopus 로고
    • Autophagic vacuolar myopathy
    • This is an excellent review of the vacuolar myopathies
    • Nishino I. Autophagic vacuolar myopathy. Semin Pediatr Neurol 2006; 13:90-95. This is an excellent review of the vacuolar myopathies.
    • (2006) Semin Pediatr Neurol , vol.13 , pp. 90-95
    • Nishino, I.1
  • 73
    • 33745082176 scopus 로고    scopus 로고
    • Fischer D, Herasse M, Bitoun M, et al. Characterization of the muscle involvement in dynamin 2-related centronuclear myopathy. Brain 2006; 129:1463-1469. This paper demonstrates the characteristic pattern of muscle involvement in dynamin-2 centronuclear myopathy useful in diagnosis.
    • Fischer D, Herasse M, Bitoun M, et al. Characterization of the muscle involvement in dynamin 2-related centronuclear myopathy. Brain 2006; 129:1463-1469. This paper demonstrates the characteristic pattern of muscle involvement in dynamin-2 centronuclear myopathy useful in diagnosis.
  • 74
    • 33846585109 scopus 로고    scopus 로고
    • Schessl J, Medne L, Hu Y, et al. MRI in DNM2-related centronuclear myopathy: evidence for highly selective muscle involvement. Neuromuscul Disord 2007; 17:28-32. This paper demonstrates the characteristic pattern of muscle involvement in dynamin-2 centronuclear myopathy useful in diagnosis.
    • Schessl J, Medne L, Hu Y, et al. MRI in DNM2-related centronuclear myopathy: evidence for highly selective muscle involvement. Neuromuscul Disord 2007; 17:28-32. This paper demonstrates the characteristic pattern of muscle involvement in dynamin-2 centronuclear myopathy useful in diagnosis.
  • 75
    • 33845362643 scopus 로고    scopus 로고
    • Myogenin (Myf4) upregulation in transdifferentiating fibroblasts from a congenital myopathy with arrest of myogenesis and defects of myotube formation
    • Weise C, Dai F, Prols F, et al. Myogenin (Myf4) upregulation in transdifferentiating fibroblasts from a congenital myopathy with arrest of myogenesis and defects of myotube formation. Anat Embryol (Berl) 2006; 211:639-648.
    • (2006) Anat Embryol (Berl) , vol.211 , pp. 639-648
    • Weise, C.1    Dai, F.2    Prols, F.3
  • 76
    • 24744460506 scopus 로고    scopus 로고
    • Congenital myopathy with arrest of myogenesis prior to formation of myotubes
    • Ketelsen UP, Brand-Saberi B, Uhlenberg B, et al. Congenital myopathy with arrest of myogenesis prior to formation of myotubes. Neuropediatrics 2005; 36:246-251.
    • (2005) Neuropediatrics , vol.36 , pp. 246-251
    • Ketelsen, U.P.1    Brand-Saberi, B.2    Uhlenberg, B.3
  • 77
    • 34147122549 scopus 로고    scopus 로고
    • Tajsharghi H, Oldfors A, Macleod DP, Swash M. Homozygous mutation in MYH7 in myosin storage myopathy and cardiomyopathy. Neurology 2007; 68:962. This paper demonstrates homozygous mutation in the gene for slow-skeletal/β- cardiac myosin (MYH7) in patients with recessive myosin storage myopathy with cardiomyopathy. Previously patients with dominant myosin storage myopathy had also been shown to have different mutations in MYH7.
    • Tajsharghi H, Oldfors A, Macleod DP, Swash M. Homozygous mutation in MYH7 in myosin storage myopathy and cardiomyopathy. Neurology 2007; 68:962. This paper demonstrates homozygous mutation in the gene for slow-skeletal/β- cardiac myosin (MYH7) in patients with recessive myosin storage myopathy with cardiomyopathy. Previously patients with dominant myosin storage myopathy had also been shown to have different mutations in MYH7.
  • 78
    • 33745114085 scopus 로고    scopus 로고
    • Dye DE, Azzarelli B, Goebel HH, Laing NG. Novel slow-skeletal myosin (MYH7) mutation in the original myosin storage myopathy kindred. Neuromuscul Disord 2006; 16:357-360. This paper by molecular analysis of archival material demonstrates a previously unidentified MYH7 mutation in the seminal myosin storage myopathy kindred.
    • Dye DE, Azzarelli B, Goebel HH, Laing NG. Novel slow-skeletal myosin (MYH7) mutation in the original myosin storage myopathy kindred. Neuromuscul Disord 2006; 16:357-360. This paper by molecular analysis of archival material demonstrates a previously unidentified MYH7 mutation in the seminal myosin storage myopathy kindred.
  • 79
    • 33845290280 scopus 로고    scopus 로고
    • Myosin storage (hyaline body) myopathy: A case report
    • Shingde MV, Spring PJ, Maxwell A, et al. Myosin storage (hyaline body) myopathy: a case report. Neuromuscul Disord 2006; 16:882-886.
    • (2006) Neuromuscul Disord , vol.16 , pp. 882-886
    • Shingde, M.V.1    Spring, P.J.2    Maxwell, A.3


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