Seminars in Pediatric Neurology
Volume 13, Issue 2 , Pages 96-103 , June 2006

Protein Aggregate Myopathies

  • Hans H. Goebel, MD

      Affiliations

    • Corresponding Author InformationAddress reprint requests to Hans H. Goebel, MD, Department of Neuropathology, Johannes Gutenberg University Mainz, Medical Center, Langenbeckstrasse 1, Bldg. 706, 55131 Mainz, Germany.
    • ,
  • Harald D. Müller, MD

References 

  1. 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 Neurol. 2004;63:484–498
  2. Goebel HH, Borchert A. Protein surplus myopathies and other rare congenital myopathies. Semin Pediatr Neurol. 2002;9:160–170
  3. Ceuterick-de Groote CM, Lübke U, Durling HJ, et al. A congenital myopathy associated with subsarcolemmal ‘cap-like’ myofibrillar alterations (Myopathology and molecular genetic analysis). Neuromuscul Disord. 2005;15:566;(abstr)
  4. De Bleecker JL, Ertl BB, Engel AG. Patterns of abnormal protein expression in target formations and unstructured cores. Neuromuscul Disord. 1996;6:339–349
  5. 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 Sci. 2003;206:71–78
  6. Selcen D, Ohno K, Engel AG. Myofibrillar myopathy: Clinical, morphological and genetic studies in 63 patients. Brain. 2004;127:439–451
  7. Goebel HH, Warlo IAP. Progress in desmin-related myopathies. J Child Neurol. 2000;15:565–572
  8. Goldfarb LG, Vicart P, Goebel HH, et al. Desmin myopathy. Brain. 2004;127:723–734
  9. 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
  10. 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
  11. Selcen D, Engel AG. Mutations in myotilin cause myofibrillar myopathy. Neurology. 2004;62:1363–1371
  12. Selcen D, Engel AG. Mutations in ZASP define a novel form of muscular dystrophy in humans. Ann Neurol. 2005;57:269–276
  13. Vorgerd M, van der Ven PFM, Bruchertseifer V, et al. A mutation in the dimerization domain of filamin C causes a novel type of autosomal dominant myofibrillar myopathy. Am J Hum Genet. 2005;77:297–304
  14. D’Amico A, Benedetti S, Petrini S, et al. Major myofibrillar changes in early onset myopathy due to de novo heterozygous missense mutation in lamin A/C gene. Neuromuscul Disord. 2005;15:847–850
  15. Xiang F, Nicolao P, Chapon F, et al. A second locus for autosomal dominant myopathy with proximal muscle weakness and early respiratory muscle involvement: A likely chromosomal locus on 2q21. Neuromuscul Disord. 1999;9:308–312
  16. Melberg A, Oldfors A, Blomström-Lundqvist C, et al. Autosomal dominant myofibrillar myopathy with arrhythmogenic right ventricular cardiomyopathy linked to chromosome 10q. Ann Neurol. 1999;46:684–692
  17. Wilhelmsen KC, Blake DM, Lynch T, et al. Chromosome 12-linked autosomal dominant scapuloperoneal muscular dystrophy. Ann Neurol. 1996;39:507–520
  18. Lamont PJ, Davis MR, Mastaglia FL, et al. Adult-onset dominant myopathy with nemaline rods, unstructured cores and desmin on muscle biopsy, linked to chromosome 15q22. J Neurol Sci. 2002;199:S104;(abstr)
  19. Goebel HH, Lenard H-G, Langenbeck U, et al. A form of congenital muscular dystrophy. Brain Dev. 1980;2:387–400
  20. Fidzianska A, Goebel HH, Osborn M, et al. Mallory body-like inclusions in a hereditary congenital neuromuscular disease. Muscle Nerve. 1983;6:195–200
  21. Fidzianska A, Ryniewicz B, Barcikowska M, et al. A new familial congenital myopathy in children with desmin and dystrophin reacting plaques. J Neurol Sci. 1995;131:88–95
  22. Ferreiro A, Quijano-Roy S, Pichereau C, et al. Mutations of the selenoprotein N gene, implicated in rigid spine muscular dystrophy, cause the classical phenotype of multi-minicore disease. Am J Hum Genet. 2002;71:739–749
  23. Gonzales V, Quijano-Roy S, Parain K, et al. SEPN-related myopathy: an emerging entity phenotypical and molecular analysis of 80 cases. Neuromuscul Disord. 2005;15:715;(abstr)
  24. Taratuto AL, Saccoliti M, Espada G, et al. Early-onset myopathy with cytoplasmic and/or Mallory body-like inclusions. Neuromuscul Disord. 2005;15:693–694(abstr)
  25. Parain K, Milic Rasic V, Cabello A, et al. Genetic heterogeneity of desmin-related myopathy with Mallory body-like inclusions. Neuromuscul Disord. 2005;15:694;(abstr)
  26. Goebel HH, Muller J, Gillen HW, et al. Autosomal dominant “spheroid body myopathy.”. Muscle Nerve. 1978;1:14–26
  27. Goebel HH, D’Agostino AN, Wilson J, et al. Spheroid body myopathy—Revisited. Muscle Nerve. 1997;20:1127–1136
  28. Foroud T, Pankratz N, Batchman AP, et al. A mutation in myotilin causes spheroid body myopathy. Neurology. 2005;65:1936–1940
  29. Dagvadorj A, Olivé M, Urtizberea J-A, et al. A series of West European patients with severe cardiac and skeletal myopathy associated with a de novo R406W mutation in desmin. J Neurol. 2004;251:143–149
  30. Muntoni F, Mercuri E, Bonne G, et al. Double lamin-emerin and lamin-desmin trouble. Neuromuscul Disord. 2005;15:677;(abstr)
  31. Dubowitz V. In: Muscle Biopsy: A Practical Approach. London: Baillière Tindall; 1985;p. 664–670
  32. Agrawal PB, Strickland CD, Midgett C, et al. Heterogeneity of nemaline myopathy cases with skeletal muscle α-actin gene mutations. Ann Neurol. 2004;56:86–96
  33. Goebel HH, Brockmann K, Bönnemann C, et al. Actin-related myopathy without any missense mutation in the ACTA1 gene. J Child Neurol. 2004;19:149–153
  34. 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
  35. Barohn RJ, Brumback RA, Mendell JR. Hyaline body myopathy. Neuromuscul Disord. 1994;4:257–262
  36. Cancilla PA, Kalyanaraman K, Verity MA, et al. Familial myopathy with probable lysis of myofibrils in type I fibres. Neurology. 1971;21:579–585
  37. Dye DE, Azzarelli B, Goebel HH, et al. Novel slow-skeletal myosin (MYH7) mutation in the original myosin storage myopathy kindred. Neuromuscul Disord. 2006;16:357–360
  38. Tajsharghi H, Thornell L-E, Lindberg C, et al. Myosin storage myopathy associated with a heterozygous missense mutation in MYH7. Ann Neurol. 2003;54:494–500
  39. Bohlega S, Abu-Amero SN, Wakil SM, et al. Mutation of the slow myosin heavy chain rod domain underlies hyaline body myopathy. Neurology. 2004;62:1518–1521
  40. Ceuterick C, Martin J-J, Martens C. Hyaline bodies in skeletal muscle of a patient with a mild chronic nonprogressive congenital myopathy. Clin Neuropathol. 1993;12:79–83
  41. Laing NG, Ceuterick-de Groote C, Dye DE, et al. Myosin storage myopathy: Slow skeletal myosin (MYH7) mutation in two isolated cases. Neurology. 2005;64:527–529
  42. Masuzugawa S, Kuzuhara S, Narita Y, et al. Autosomal dominant hyaline body myopathy presenting as scapuloperoneal syndrome: Clinical features and muscle pathology. Neurology. 1997;48:253–257
  43. Bohlega S, Lach B, Meyer BF, et al. Autosomal dominant hyaline body myopathy: Clinical variability and pathologic findings. Neurology. 2003;61:1519–1523
  44. Önengüt S, Ugur SA, Karasoy H, et al. Identification of a locus for an autosomal recessive hyaline body myopathy at chromosome 3p22.2-p21.32. Neuromuscul Disord. 2004;14:4–9
  45. Bertini E, Bosman C, Ricci E, et al. Neuromyopathy and restrictive cardiomyopathy with accumulation of intermediate filaments: A clinical, morphological and biochemical study. Acta Neuropathol (Berl). 1991;81:632–640
  46. Amato AA, Kagan-Hallet K, Jackson CE, et al. The wide spectrum of myofibrillar myopathy suggests a multifactorial etiology and pathogenesis. Neurology. 1998;51:1646–1655
  47. Park K-Y, Dalakas MC, Goebel HH, et al. Desmin splice variants causing cardiac and skeletal myopathy. J Med Genet. 2000;37:851–857
  48. Liu HM, Gumbinas M. Axonal filamentous spheroids associated with cardiomyopathy with “targetoid fibres.”. Neurology. 1974;24:547–554
  49. Sabatelli M, Bertini E, Ricci E, et al. Peripheral neuropathy with giant axons and cardiomyopathy associated with desmin type intermediate filaments in skeletal muscle. J Neurol Sci. 1992;109:1–10
  50. Bertini E, Salviati G, Apollo F, et al. Reducing body myopathy and desmin storage in skeletal muscle: Morphological and biochemical findings. Acta Neuropathol (Berl). 1994;87:106–112
  51. Prelle A, Moggio M, Comi GP, et al. Congenital myopathy associated with abnormal accumulation of desmin and dystrophin. Neuromuscul Disord. 1992;2:169–175
  52. Bertini E, Ricci E, Boldrini R, et al. Involvement of repiratory muscles in cytoplasmic body myopathy. Brain Dev. 1990;12:798–806
  53. Sarnat HB. Myofibrillar myopathy in infancy and childhood: five cases in two families of an unclassified congenital myopathy. J Child Neurol. 1997;12:132–133(abstr)
  54. Calderon A, Becker LE, Murphy EG. Subsarcolemmal vermiform deposits in skeletal muscle, associated with familial cardiomyopathy: Report of two cases of a new entity. Pediatr Neurosci. 1987;13:108–112
  55. Vajsar J, Becker LE, Freedom RM, et al. Familial desminopathy: Myopathy with accumulation of desmin-type intermediate filaments. J Neurol Neurosurg Psychiatry. 1993;56:644–648
  56. Telerman-Toppet N, Bauherz G, Noël S. Auriculo-ventricular block and distal myopathy with rimmed vacuoles and desmin storage. Clin Neuropathol. 1991;10:61–64
  57. Sparrow JC, Nowak KJ, Durling HJ, et al. Muscle disease caused by mutations in the skeletal muscle alpha-actin gene (ACTA1). Neuromuscul Disord. 2003;13:519–531
  58. Kaindl AM, Rüschendorf F, Krause S, et al. Missense mutations of ACTA1 cause dominant congenital myopathy with cores. J Med Genet. 2004;41:842–848
  59. Laing NG, Clarke NF, Dye DE, et al. Actin mutations are one cause of congenital fibre type disproportion. Ann Neurol. 2004;56:689–694

PII: S1071-9091(06)00095-7

doi: 10.1016/j.spen.2006.06.005

Seminars in Pediatric Neurology
Volume 13, Issue 2 , Pages 96-103 , June 2006

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