Few medical disciplines have benefited so enormously from the molecular revolution as myology. Whereas the congenital myopathies have flourished from enzyme histochemistry and electron microscopy, defining individual congenital myopathies by structural abnormalities, genetic research has only recently focused on congenital myopathies. However, a number of congenital myopathies have been molecularly elucidated: central and multiminicore diseases, nemaline myopathy, myotubular myopathy, and congenital myopathy marked by aggregation of proteins, giving rise to the concept of protein aggregate myopathies, to which now desminopathies, α-B crystallinopathies, selenoproteinopathy, myotilinopathy, actinopathies, and myosinopathies belong. Based on recent identification of mutations in respective genes, the principle “from morphology, that is, immunohistochemistry, to molecular analysis” through recognition of certain accrued proteins within muscle fibers and subsequent analysis of their respective genes has resulted in a wealth of genetic data and in reconsidering classification and nosologic interpretation of certain congenital myopathies. This heuristic principle needs to be further applied to other genetically still obscure congenital myopathies. (J Child Neurol 2005;20:94—101).
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References
1.
Shy GM, Magee KR: A new congenital non-progressive myopathy. Brain1956;79:610—621.
2.
Goebel HH: Congenital myopathies at their molecular dawning. Muscle Nerve2003;7:527—548.
3.
Sewry C. Marinesco-Sjögren syndrome, in Karpati G (ed): Structural and Molecular Basis of Skeletal Muscle Diseases. Lawrence, KS, Allen Press , 2002, 277—278.
4.
Manzur AY, Sewry CA, Zirpin J., et al:A severe clinical and pathological variant of central core disease with possible autosomal recessive inheritance. Neuromuscul Disord1998;8:467—473.
5.
Ferreiro A., Estournet B., Chateau D., et al: Multi-minicore disease— Searching for boundaries: Phenotype analysis of 38 cases. Ann Neurol2000;48:745—757.
6.
Kaindl AM, Krause S., Rüschendorf F., et al:Missense mutations of ACTA1 cause dominant congenital myopathy with cores, abstract. Neuromuscul Disord2004;14:562.
7.
Vita G., Migliorato A., Baradello A., et al: Expression of cytoskeletal proteins in central core disease . J Child Neurol1994;124:71—76.
8.
Parain K., Herasse M., Monnier N., et al:Proteins implicated in Ca2+ homeostasis: Expression patterns in genetically characterized core myopathies, abstract. Neuromuscul Disord2004;14:588.
9.
De Bleecker JL, Ertl BB, Engel AG: Patterns of abnormal protein expression in target formations and unstructured cores. Neuromuscul Disord1996;6:339—349.
10.
Bönnemann C. , Thompson TG, van der Ven Pfm, et al: Filamin C accumulation is a strong but nonspecific immunohistochemical marker of core formation in muscle. J Neurol Sci2003;206:71—78.
11.
Ferreiro A. , Monnier N., Romero NB, et al: A recessive form of central core disease, transiently presenting as multi-minicore disease, is associated with a homozygous mutation in the ryanodine receptor type 1 gene. Ann Neurol2002;51:750—759.
12.
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 Neurol2004;55:676—686.
13.
Goebel HH, Piirsoo A., Warlo I., et al: Infantile intranuclear rod myopathy. J Child Neurol1997;12:22—30.
14.
Wallgren-Pettersson C., Pelin K., Nowak KJ, et al: Genotype-phenotype correlations in nemaline myopathy caused by mutations in the genes for nebulin and skeletal muscle α-actin. Neuromuscul Disord2004 ; 14:461-470.
15.
Ohlsson M., Tajsharghi H., Darin N., et al: Follow-up of nemaline myopathy in two patients with novel mutations in the skeletal muscle α-actin gene (ACTA1). Neuromuscul Disord2004; 14:471-475.
16.
Agrawal PB, Strickland CD, Midgett C., et al: Heterogeneity of nemaline myopathy cases with skeletal muscle α-actin gene mutations. Ann Neurol2004;56:86—96.
17.
Sewry CA, Rodillo E., Heckmatt JZ, Dubowitz V.: Immunocytochemical studies of congenital centronuclear and nemaline myopathies, abstract. J Neurol Sci1990;98(Suppl):100.
18.
Goebel HH, Warlo I.: Nemaline myopathy with intranuclear rods— Intranuclear rod myopathy . Neuromuscul Disord1997;7:13—19.
19.
Nowak K., Wattanasirichaigoon D., Goebel HH, et al: Mutations in the skeletal muscle α-actin gene in patients with actin myopathy and nemaline myopathy. Nat Genet1999;23:208—212.
20.
Monnier N., Romero NB, Lerale J., et al: An autosomal dominant congenital myopathy with cores and rods is associated with a neomutation in the RYR1 gene encoding the skeletal muscle ryanodine receptor. Hum Mol Genet2000;9:2599—2608.
21.
Scacheri PC , Hoffman EP, Fratkin JD, et al: A novel ryanodine receptor gene mutation causing both cores and rods in congenital myopathy. Neurology2000;55:1689—1696.
Karpati G., Carpenter S.: Skeletal muscle in neuromuscular diseases, in Rowland LP, DiMauro S (eds): Myopathies-Handbook of Clinical Neurology, vol 18. Amsterdam, Elsevier Science Publishers BV, 1992, 1—48.
24.
Cancilla PA , Kalyanaraman K., Verity MA, et al: Familial myopathy with probable lysis of myofibrils in type I fibres. Neurology1971;21:579—585.
25.
Nucci A., Queiroz LS: A sporadic case of hyaline body myopathy, abstract. Neuromuscul Disord2004;14:566.
26.
Ceuterick C. , Martin J-J., Martens C.: Hyaline bodies in skeletal muscle of a patient with a mild chronic nonprogressive congenital myopathy. Clin Neuropathol1993; 12: 79—83.
27.
Masuzugawa S., Kuzuhara S., Narita Y., et al: Autosomal dominant hyaline body myopathy presenting as scapuloperoneal syndrome: Clinical features and muscle pathology . Neurology1997;48:253—257.
28.
Tajsharghi H., Thornell L-E., Lindberg C., et al: Myosin storage myopathy associated with a heterozygous missense mutation in MYH7. Ann Neurol2003;54:494—500.
29.
Bohlega S., Abu-Amero SN, Wakil SM, et al: Mutation of the slow myosin heavy chain rod domain underlies hyaline body myopathy. Neurology2004;62:1518—1521.
30.
Goebel HH, Fardeau M.: Familial desmin-related myopathies and cardiomyopathies—From myopathology to molecular and clinical genetics. 36th European Neuromuscular Centre (ENMC)-Sponsored International Workshop, 20-22 October 1995, Naarden, The Netherlands. Neuromuscul Disord1996;6:383—388.
Engel AG: Myofibrillar myopathy, editorial. Ann Neurol1999; 46:681—683.
33.
Goldfarb LG , Park K-Y., Cervenáková S., et al: Missense mutations in desmin associated with familial cardiac and skeletal myopathy, letter. Nat Genet1998;19:402—403.
Fardeau M., Godet-Guillain J., Tomé Fsm, et al: Une nouvelle affection musculaire familiale, définie par l'accumulation intra-sarco-plasmique d'un matériel granulo-filamentaire dense en microscopie électronique. Rev Neurol (Paris)1978;134:411—425.
38.
Osborn M., Goebel HH: The cytoplasmic bodies in a congenital myopathy can be stained with antibodies to desmin, the muscle-specific intermediate filament protein. Acta Neuropathol (Berl)1983;62:149—152.
39.
Goebel HH, Voit T., Warlo I., et al: Immunohistologic and electron microscopic abnormalities of desmin and dystrophin in familial cardiomyopathy and myopathy. Rev Neurol (Paris)1994;150:452—459.
40.
Goebel HH, Anderson JR, Hübner C., et al:Congenital myopathy with excess of thin myofilaments. Neuromuscul Disord1997;7:160—168.
41.
Fardeau M., Vicart P., Caron A., et al: Myopathie familiale avec surcharge en desmine, sous forme de matériel granulo-filamentaire dense en microscopie électronique, avec mutation dans le gène de l'alpha-B-cristalline. Rev Neurol (Paris)2000; 156:497-504.
42.
Pica EC, Pramono Zad, Lai PS, Yee WC: A novel desmin mutation S13F in a case of spheroid body myopathy with desmin storage, abstract. Neuromuscul Disord2004 ;14:565.
43.
Goebel HH, Borchert A.: Protein surplus myopathies and other rare congenital myopathies. SeminPediatr Neurol2002;9:160—170.
44.
Vicart P., Caron A., Guicheney P., et al: A missense mutation in the alpha-B crystallin chaperone gene causes a desmin-related myopathy. Nat Genet1998;20:92—95.
45.
Selcen D., Engel AG: Myofibrillar myopathy caused by novel dominant negative αB-crystallin mutations. Ann Neurol2003;54:804—810.
46.
Selcen D., Engel AG: Mutations in myotilin cause myofibrillar myopathy. Neurology2004;62:1363—1371.
47.
De Bleecker JL, Engel AG, Ertl BB: Myofibrillar myopathy with abnormal foci of desmin positivity. II. Immunocytochemical analysis reveals accumulation of multiple other proteins. J Neuropathol Exp Neurol1996;55:563—577.
48.
Ferrer I., Martín B., Castaño JG, et al: Proteasomal expression, induction of immunoproteasome subunits, and local MHC class I presentation in myofibrillar myopathy and inclusion body myositis. J Neuropathol Exp Neurol2004 ;63:484—498.
49.
Goebel HH, Halbig LE, Goldfarb L., et al:Reducing body myopathy with cytoplasmic bodies and rigid spine syndrome: A mixed congenital myopathy. Neuropediatrics2001;32:196—205.
50.
Kiyomoto BH , Murakami N., Kobayashi Y., et al: Fatal reducing body myopathy: Ultrastructural and immunohistochemical observations. J Neurol Sci1995;128:58—65.
51.
Liewluck T. , Ohsawa M., Sasaki M., et al:ER stress-mediated apoptosis in autosomal dominant reducing body myopathy, abstract. Neuromuscul Disord2004;14:588—589.
52.
Rapuzzi S., Prelle A., Moggio M., et al: High serum creatine kinase levels associated with cylindrical spirals at muscle biopsy. Acta Neuropathol (Berl)1995;90:660—664.
53.
Biancalana V., Caron O., Gallati S., et al: Characterization of mutations in 77 patients with X-linked myotubular myopathy, including a family with a very mild phenotype. Hum Genet2003;112:135—142.
54.
Tsai TC, Horinouchi H., Noguchi S., et al:Characterization of MTM1 mutations in 32 Japanese patients with myotubular myopathy, including a patient carrying 240 kb deletion in Xq28 without male hypogenitalism, abstract. Neuromuscul Disord2004;14:589.
55.
Buj-Bello A. , Laporte J., Mandel JL: A novel antibody for rapid diagnosis of X-linked myotubular myopathy by immunodetection of myotubularin, abstract G.P.8.06Neuromuscul Disord2004;14:589.
56.
Jeannet PY, Bassez G., Eymard B., et al: Clinical and histologic findings in autosomal centronuclear myopathy. Neurology2004;62:1484—1490.
57.
Tiret L., Blot S., Kessler JL, et al: The CNM locus, a canine homologue of human autosomal forms of centronuclear myopathy, maps to chromosome 2. Hum Genet2003;113:297—306.
58.
Clarke NF, Laing NB, Walker KR, et al: The genetic basis and clinical features of congenital fibre type disproportion, abstract. Neuromuscul Disord2004;14:588.
59.
Schröder JM: Congenital fiber type disproportion, in Lane RJM (ed): Handbook of Muscle Disease. New York, Marcel Dekker, 1996, 195—200.
60.
Vorwerk G., Christoffersen CT, Muller J., et al: Alternative splicing of exon 17 and a missense mutation in exon 20 of the insulin receptor gene in two brothers with a novel syndrome of insulin resistance (congenital fiber-type disproportion myopathy). Horm Res1999;52:211—220.
61.
Sharma MC, Sarkar C., Gulati S., Singh S.: Congenital myopathy—A clinicopathological study of 11 cases: An Indian experience, abstract. Neuromuscul Disord2004 ;14:591.
