Neuromuscular Disorders
Volume 18, Issue 1 , Pages 6-16 , January 2008

Sporadic inclusion body myositis: a continuing puzzle

Received 3 August 2007 ,Revised 29 October 2007 ,Accepted 7 November 2007.

References 

  1. Chou SM. Myxovirus-like structures in a case of human chronic polymyositis. Science. 1967;158:1453–1455
  2. Yunis EJ, Samaha FJ. Inclusion body myositis. Lab Invest. 1971;25:240–248
  3. Pruitt JN, Showalter CJ, Engel AG. Sporadic inclusion body myositis: counts of different types of abnormal fibers. Ann Neurol. 1996;39:139–143
  4. Dalakas MC. Muscle biopsy findings in inflammatory myopathies. Rheum Dis Clin North Am. 2002;28:779–798
  5. Askanas V, Engel WK. Newest approaches to diagnosis and pathogenesis of sporadic inclusion-body myositis and hereditary inclusion-body myopathies, including molecular-pathologic similarities to Alzheimer disease. In:  Askanas V,  Serratrice G,  Engel WK editor. Inclusion-body myositis and myopathies. Cambridge: Cambridge University; 1998;p. 3–78
  6. Toepfer M, Fischer P, Muller-Felber W, Pongratz D. Correlation between the number of vacuolated amyloid-positive fibers and the duration and stage of disease in Inclusion Body Myositis. Eur J Neurol. 1995;2:31
  7. Arahata K, Engel AG. Monoclonal antibody analysis of mononuclear cells in myopathies. I: Quantitation of subsets according to diagnosis and sites of accumulation and demonstration and counts of muscle fibers invaded by T cells. Ann Neurol. 1984;16:193–208
  8. Schmidt J, Rakocevic G, Raju R, Dalakas MC. Upregulated inducible co-stimulator (ICOS) and ICOS-ligand in inclusion body myositis muscle: significance for CD8+ T cell cytotoxicity. Brain. 2004;127:1182–1190
  9. Bender A, Behrens L, Engel AG, Hohlfeld R. T-cell heterogeneity in muscle lesions of inclusion body myositis. J Neuroimmunol. 1998;84:86–91
  10. Fyhr IM, Moslemi AR, Mosavi AA, Lindberg C, Tarkowski A, Oldfors A. Oligoclonal expansion of muscle infiltrating T cells in inclusion body myositis. J Neuroimmunol. 1997;79:185–189
  11. Muntzing K, Lindberg C, Moslemi AR, Oldfors A. Inclusion body myositis: clonal expansions of muscle-infiltrating T cells persist over time. Scand J Immunol. 2003;58:195–200
  12. Amemiya K, Granger RP, Dalakas MC. Clonal restriction of T-cell receptor expression by infiltrating lymphocytes in inclusion body myositis persists over time. Studies in repeated muscle biopsies. Brain. 2000;123:2030–2039
  13. Dimitri D, Benveniste O, Dubourg O, et al. Shared blood and muscle CD8+ T-cell expansions in inclusion body myositis. Brain. 2006;129:986–995
  14. Greenberg SA, Pinkus GS, Amato AA, Pinkus JL. Myeloid dendritic cells in inclusion-body myositis and polymyositis. Muscle Nerve. 2007;35:17–23
  15. Appleyard ST, Dunn MJ, Dubowitz V, Rose ML. Increased expression of HLA ABC class I antigens by muscle fibres in Duchenne muscular dystrophy, inflammatory myopathy, and other neuromuscular disorders. Lancet. 1985;1:361–363
  16. Karpati G, Pouliot Y, Carpenter S. Expression of immunoreactive major histocompatibility complex products in human skeletal muscles. Ann Neurol. 1988;23:64–72
  17. Figarella-Branger PJ, Bianco N, Devictor B, Toga M. Inflammatory and non-inflammatory inclusion body myositis: characterisation of the mononuclear cells and expression of the immunoreactive class 1 Major Histocompatibility complex product. Acta Neuropathol. 1990;79:528–536
  18. Wiendl H, Mitsdoerffer M, Schneider D, et al. Muscle fibres and cultured muscle cells express the B7. 1/2-related inducible co-stimulatory molecule, ICOSL: implications for the pathogenesis of inflammatory myopathies. Brain. 2003;126:1026–1035
  19. Murata K, Dalakas MC. Expression of the costimulatory molecule BB-1, the ligands CTLA-4 and CD28, and their mRNA in inflammatory myopathies. Am J Pathol. 1999;155:453–460
  20. Fyhr IM, Oldfors A. Upregulation of fas/fas-ligand in inclusion body myositis. Ann Neurol. 1998;43:127–130
  21. Li M, Dalakas MC. Expression of human IAP-like protein in skeletal muscle: a possible explanation for the rare incidence of muscle fiber apoptosis in T-cell mediated inflammatory myopathies. J Neuroimmunol. 2000;106:1–5
  22. Behrens L, Bender A, Johnson MA, Hohlfeld R. Cytotoxic mechanisms in inflammatory myopathies: co-expression of Fas and protective Bcl-2 in muscle fibres and inflammatory cells. Brain. 1997;120:929–938
  23. Schneider C, Gold R, Dalakas MC, et al. MHC class I-mediated cytotoxicity does not induce apoptosis in muscle fibers nor in inflammatory T cells: studies in patients with polymyositis, dermatomyositis, and inclusion body myositis. J Neuropathol Exp Neurol. 1996;55:1205–1209
  24. Germain RN. MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell. 1994;76:287–299
  25. Greenberg SA, Bradshaw EM, Pinkus JL, et al. Plasma cells in muscle in inclusion body myositis and polymyositis. Neurology. 2005;65:1782–1787
  26. Greenberg SA, Sandoudou D, Haslett JN, Kohane IS, Kunkel LM, Beggs AH. Molecular profiles of inflammatory myopathies. Neurology. 2002;59:1170–1182
  27. Raju R, Dalakas MC. Gene expression profile in the muscles of patients with inflammatory myopathies: effect of therapy with IVIg and biologic validation of clinical relevant genes. Brain. 2005;128:1887–1896
  28. Dalakas MC, Illa I, Gallardo E, Juarez C. Inclusion body myositis and paraproteinemia: incidence and immunopathologic correlations. Ann Neurol. 1997;41:100–104
  29. Figarella-Branger D, Civatte M, Bartoli C, Pellissier JF. Cytokines, chemokines, and cell adhesion molecules in inflammatory myopathies. Muscle Nerve. 2003;28:659–682
  30. Bao SS, King NJ, dos Remedios CG. Elevated MHC class I and II antigens in cultured human embryonic myoblasts following stimulation with gamma-interferon. Immunol Cell Biol. 1990;68:235–241
  31. Michaelis D, Goebels N, Hohlfeld R. Constitutive and cytokine-induced expression of human leukocyte antigens and cell adhesion molecules by human myotubes. Am J Pathol. 1993;143:1142–1149
  32. Pavlath GK. Regulation of class I MHC expression in skeletal muscle: deleterious effect of aberrant expression on myogenesis. J Neuroimmunol. 2002;125:42–50
  33. Lundberg I, Brengman JM, Engel AG. Analysis of cytokine expression in muscle in inflammatory myopathies, Duchenne dystrophy, and non-weak controls. J Neuroimmunol. 1995;63:9–16
  34. Lepidi H, Frances V, Figarella-Branger D, Bartoli C, Machado-Baeta A, Pellissier JF. Local expression of cytokines in idiopathic inflammatory myopathies. Neuropathol Appl Neurobiol. 1998;24:73–79
  35. Dalakas MC. Molecular immunology and genetics of inflammatory muscle diseases. Arch Neurol. 1998;55:1509–1512
  36. Raju R, Vasconcelos O, Granger R, Dalakas M. Expression of IFN-γ-inducible chemokines in inclusion body myositis. J Neuroimmunol. 2003;141:125–131
  37. Goldgaber D, Harris HW, Hla T. Interleukin 1 regulates synthesis of amyloid beta-protein precursor mRNA in human endothelial cells. Proc Natl Acad Sci USA. 1989;86:7606–7610
  38. Semino-Mora C, Dalakas M. Upregulation of IL-beta mRNA in inclusion body myositis (IBM) and co-expression with beta-amyloid precursor protein: a mechanism for amyloid deposits. Neurology. 1998;50:204
  39. Dalakas MC. Sporadic inclusion body myositis – diagnosis, pathogenesis and therapeutic strategies. Nat Clin Pract. 2006;2:437–445
  40. Nagaraju K, Casciola-Rosen L, Lundberg I, et al. Activation of the Endoplasmic Reticulum stress response in autoimmune myositis. Arthritis Rheum. 2005;52:1824–1835
  41. Vattemi G, Engel WK, McFerrin J, Askanas V. Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am J Pathol. 2004;164:1–7
  42. Askanas V, Engel WK. Inclusion-body myositis: a myodegenerative conformational disorder associated with Abeta, protein misfolding, and proteasome inhibition. Neurology. 2006;66:S39–S48
  43. Kaufman RJ. Stress signalling from the lumen of the endoplasmic reticulum: co-ordination of gene transcriptional and translational controls. Genes Dev. 1999;13:1211–1233
  44. Pahl HL. Activators and target genes of Rel/NF-κB transcription factors. Oncogene. 1999;18:6853–6866
  45. Askanas V, Engel WK. Molecular pathology and pathogenesis of inclusion-body myositis. Microsc Res Tech. 2005;67:114–120
  46. Yang CC, Askanas V, Engel WK, Alvarez RB. Immunolocalization of transcription factor NF-kB in inclusion-body myositis muscle and at normal human neuromuscular junctions. Neurosci Lett. 1998;254:77–80
  47. Nagaraju K, Raben N, Loeffler L, et al. Conditional up-regulation of MHC class I in skeletal muscle leads to self-sustaining autoimmune myositis and myositis-specific autoantibodies. Proc Natl Acad Sci USA. 2000;97:9209–9214
  48. Chou SM. Inclusion body myositis: a chronic persistent mumps myositis?. Hum Pathol. 1986;17:765–777
  49. Nishino H, Engel AG, Rima BK. Inclusion body myositis: the mumps virus hypothesis. Ann Neurol. 1989;25:260–264
  50. Fox SA, Ward BK, Robbins PD, Mastaglia FL, Swanson NR. Inclusion body myositis: investigation of the mumps virus hypothesis by polymerase chain reaction. Muscle Nerve. 1996;19:23–28
  51. Fox SA, Finklestone E, Robbins PD, Mastaglia FL, Swanson NR. Search for persistent enterovirus infection of muscle in inflammatory myopathies. J Neurol Sci. 1994;125:70–76
  52. Leon-Monzon M, Dalakas MC. Absence of persistent infection with enteroviruses in muscles of patients with inflammatory myopathies. Ann Neurol. 1992;32:219–222
  53. Jongen PJ, Zoll GJ, Beaumont M, Melchers WJ, van de Putte LB, Galama JM. Polymyositis and dermatomyositis: no persistence of enterovirus or encephalomyocarditis virus RNA in muscle. Ann Rheum Dis. 1993;52:575–578
  54. Leff RL, Love LA, Miller FW, et al. Viruses in idiopathic inflammatory myopathies: absence of candidate viral genomes in muscle. Lancet. 1992;339:1192–1195
  55. Christen U, von Herrath MG. Initiation of autoimmunity. Curr Opin Immunol. 2004;16:759–767
  56. Ozden S, Gessain A, Gout O, Mikol J. Sporadic Inclusion body myositis in a patient with human T-cell leukemia viurs type 1-Associated myelopathy. Clin Infect Dis. 2001;32:510–514
  57. Cupler EJ, Leon-Monzon M, Miller J, Semino-Mora C, Anderson TL, Dalakas MC. Inclusion body myositis in HIV-1 and HTLV-1 infected patients. Brain. 1996;119:1887–1893
  58. Dalakas MC, Rakocevic G, Shatunov A, Goldfarb L, Raju R, Salajegheh M. Inclusion body myositis with human immunodeficiency virus infection: four cases with clonal expansion of viral-specific T cells. Ann Neurol. 2007;
  59. Ozden S, Cochet M, Mikol J, Teixeira A, Gessain A, Pique C. Direct evidence for a chronic CD8+T-cell-mediated immune reaction to tax within the muscle of a human T-cell leukemia/lymphoma virus type-1-infected patient with sporadic inclusion body myositis. J Virol. 2004;78:10320–10327
  60. Dalakas MC, Rakocevic G, Shatunov A, Goldfarb L, Raju R, Salajegheh M. Inclusion body myositis with human immunodeficiency virus infection: four cases with clonal expansion of viral-specific T cells. Ann Neurol. 2007;61:466–475
  61. Villanova M, Kawai M, Lubke U, et al. Rimmed vacuoles of inclusion body myositis and oculopharyngeal muscular dystrophy contain amyloid precursor protein and lysosomal markers. Brain Res. 1993;603:343–347
  62. Sherriff FE, Joachim CL, Squier MV, Esiri MM. Ubiquitinated inclusions in inclusion-body myositis patients are immunoreactive for cathepsin D but not beta-amyloid. Neurosci Lett. 1995;194:37–40
  63. Tsuruta Y, Furuta A, Furuta K, Yamada T, Kira J, Iwaki T. Expression of the lysosome-associated membrane proteins in myopathies with rimmed vacuoles. Acta Neuropathol (Berl). 2001;101:579–584
  64. Kumamoto T, Ueyama H, Tsumura H, Toyoshima I, Tsuda T. Expression of lysosome-related proteins and genes in the skeletal muscles of inclusion body myositis. Acta Neuropathol. 2004;107:59–65
  65. Lunemann JD, Schmidt J, Dalakas MC, Munz C. Macroautophagy as a pathomechanism in sporadic inclusion body myositis. Autophagy. 2007;3:384–386
  66. Karpati G, Carpenter S. Pathology of the inflammatory myopathies. Baillieres Clin Neurol. 1993;2:527–556
  67. Greenberg SA, Pinkus JL, Amato AA. Nuclear membrane proteins are present within rimmed vacuoles in inclusion body myositis. Muscle Nerve. 2006;34:406–416
  68. Carpenter S, Karpati G, Heller I, Eisen A. Inclusion body myositis: a distinct variety of idiopathic inflammatory myopathy. Neurology. 1978;28:8–17
  69. Nalbantoglu J, Karpati G, Carpenter S. Conspicuous accumulation of a single-stranded DNA binding protein in skeletal muscle fibers in inclusion body myositis. Am J Pathol. 1994;144:874–882
  70. Griggs RC, Askanas V, DiMauro S, et al. Inclusion body myositis and myopathies. Ann Neurol. 1995;38:705–713
  71. Nakano S, Shinde A, Fujita K, Ito H, Kusaka H. Histone H1 is released from myonuclei and present in rimmed vacuoles with DNA in inclusion body myositis. Neuromuscul Disord. 2008;18:27–33
  72. Krause S, Hinderlich S, Amsili S, et al. Localization of UDP-GlcNAc 2-epimerase/ManAc kinase (GNE) in the Golgi complex and the nucleus of mammalian cells. Exp Cell Res. 2005;304:365–379
  73. Calado A, Tome FM, Brais B, et al. Nuclear inclusions in oculopharyngeal muscular dystrophy consist of poly(A) binding protein 2 aggregates which sequester poly(A) RNA. Hum Mol Genet. 2000;9:2321–2328
  74. Fidzianska A, Hausmanowa-Petrusewicz I. Architectural abnormalities in muscle nuclei. Ultrastructural differences between X-linked and autosomal dominant forms of EDMD. J Neurol Sci. 2003;210:47–51
  75. Fidzianska A, Rowinska-Marcinska K, Hausmanowa-Petrusewicz I. Coexistence of X-linked recessive Emery-Dreifuss muscular dystrophy with inclusion body myositis-like morphology. Acta Neuropathol. 2004;107:197–203
  76. Li J, Yin C, Okamoto H, et al. Proteomic analysis of inclusion body myositis. J Neuropathol Exp Neurol. 2006;65:826–833
  77. Hutchinson DO, Jongbloed B. Two-dimensional gel electrophoresis in inclusion body myositis. J Clin Neurosci, in press.
  78. Johnston JA, Ward CL, Kopito RR. Aggresomes: a cellular response to misfolded proteins. J Cell Biol. 1998;143:1883–1898
  79. Kopito RR. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 2000;10:524–530
  80. Ferrer I, Martin B, Castano JG, Lucas JJ, Moreno D, Olive M. 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
  81. Fratta P, Engel WK, McFerrin J, Davies KJA, Lin SW, Askanas V. Proteasome inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers. Am J Pathol. 2005;167:517–526
  82. Bence NF, Sampat RM, Kopito RR. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 2001;292:1552–1555
  83. Bennett EJ, Bence NF, Jayakumar R, Kopito RR. Global impairment of the ubiquitin-proteasome system by nuclear or cytoplasmic protein aggregates precedes inclusion body formation. Mol Cell. 2005;17:351–365
  84. Kruger R, Eberhardt O, Riess O, Schulz JB. Parkinson’s disease: one biochemical pathway to fit all genes?. Trends Mol Med. 2002;8:236–240
  85. Askanas V, Serdaroglu P, Engel WK, Alvarez RB. Immunolocalization of ubiquitin in muscle biopsies of patients with inclusion body myositis and oculopharyngeal muscular dystrophy. Neurosci Lett. 1991;130:73–76
  86. Paciello O, Wojcik S, Engel WK, McFerrin J, Askanas V. Parkin and its association with alpha-synuclein and AbetaPP in inclusion-body myositis and AbetaPP-overexpressing cultured human muscle fibers. Acta Myol. 2006;25:13–22
  87. Mayer RJ, Landon M, Lowe J. Ubiquitin and the molecular pathology of human disease. New York: Plenum Press; 1998;
  88. Varshavsky A. The ubiquitin system. Trends Biochem Sci. 1997;22:383–387
  89. Fratta P, Engel WK, Van Leeuwen FW, Hol EM, Vattemi G, Askanas V. Mutant ubiquitin UBB+1 is accumulated in sporadic inclusion-body myositis muscle fibers. Neurology. 2004;63:1114–1117
  90. Lindsten K, de Vrij FM, Verhoef LG, et al. Mutant ubiquitin found in neurodegenerative disorders is a ubiquitin fusion degradation substrate that blocks proteasomal degradation. J Cell Biol. 2002;157:417–427
  91. Van Leeuwen FW, Fischer DF, Kamel D, et al. Molecular misreading: a new type of transcript mutation expressed during aging. Neurobiol Aging. 2000;21:879–891
  92. Dahlgren KN, Manelli AM, Stine WB, Baker LK, Krafft GA, LaDu MJ. Oligomeric and fibrillar species of amyloid-beta peptides differentially affect neuronal viability. J Biol Chem. 2002;277:32046–32053
  93. Vattemi G, Checler F, Engel WK, Askanas V. Amyloid-β42 is preferentially deposited muscle biopsies of patients with sporadic Inclusion Body Myositis. Neurology. 2003;60:A333–A334
  94. Askanas V, McFerrin J, Alvarez RB, Baque S, Engel WK. Beta APP gene transfer into cultured human muscle induces inclusion-body myositis aspects. Neuroreport. 1997;8:2155–2158
  95. Jin LW, Hearn MG, Ogburn CE, et al. Transgenic mice over-expressing the C-99 fragment of betaPP with an alpha-secretase site mutation develop a myopathy similar to human inclusion body myositis. Am J Pathol. 1998;153:1679–1686
  96. Fukuchi K, Pham D, Hart M, Li L, Lindsey JR. Amyloid-beta deposition in skeletal muscle of transgenic mice: possible model of inclusion body myopathy. Am J Pathol. 1998;153:1687–1693
  97. Sugarman MC, Yamasaki TR, Oddo S, et al. Inclusion body myositis-like phenotype induced by transgenic overexpression of beta APP in skeletal muscle. Proc Natl Acad Sci USA. 2002;99:6334–6339
  98. Askanas V, McFerrin J, Baque S, Alvarez RB, Sarkozi E, Engel WK. Transfer of beta-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle. Proc Natl Acad Sci USA. 1996;93:1314–1319
  99. Kitazawa M, Green KN, Caccamo A, LaFerla FM. Genetically augmenting Abeta42 levels in skeletal muscle exacerbates inclusion body myositis-like pathology and motor deficits in transgenic mice. Am J Pathol. 2006;168:1986–1997
  100. McFerrin J, Engel WK, Askanas V. Cultured inclusion-body myositis muscle fibers do not accumulate beta-amyloid precursor protein and can be innervated. Neurology. 1999;53:2184–2187
  101. Vattemi G, Engel WK, McFerrin J, Buxbaum JD, Pastorino L, Askanas V. Presence of BACE1 and BACE2 in muscle fibres of patients with sporadic inclusion-body myositis. Lancet. 2001;358:1962–1964
  102. Askanas V, Engel WK. Inclusion-body myositis: pathogenic role of amyloid-β, cholesterol, relation to aging and Alzheimer disease. Acta Myol. 2002;21:131–137
  103. Vetrivel KS, Thinakaran G. Amyloidogenic processing of beta-amyloid precursor protein in intracellular compartments. Neurology. 2006;66:S69–S73
  104. McFerrin J, Engel WK, Leclerc N, Askanas V. Combined influence of Amyloid-β Precursor Protein (AβPP) gene transfer and cholesterol excess on cultured normal human muscle fibers. Neurology. 2002;58:A489
  105. Jaworska-Wilczynska M, Wilczynski GM, Engel WK, Strickland DK, Weisgraber KH, Askanas V. Three lipoprotein receptors and cholesterol in inclusion-body myositis muscle. Neurology. 2002;58:438–445
  106. Kefi M, Vattemi G, Engel WK, Askanas V. Abnormal accumulation of caveolin-1 and its co-localization with cholesterol, amyloid-β and phosphorylated tau in inclusion-body myositis (IBM) muscle. Neurology. 2002;58:A391
  107. Kojro E, Gimpl G, Lammich S, Marz W, Fahrenholz F. Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha-secretase ADAM 10. Proc Natl Acad Sci USA. 2001;98:5815–5820
  108. Askanas V, Engel WK. Sporadic inclusion-body myositis and hereditary inclusion-body myopathies: diseases of oxidative stress and aging?. Arch Neurol. 1998;55:915–920
  109. Askanas V, Sarkozi E, Alvarez RB, McFerrin J, Siddique T, Engel WK. SOD1 gene and protein in vacuolated muscle fibers of s-IBM, h-IBM, and in cultured human muscle after bAPP gene transfer. Neurology. 1996;46:487
  110. Yang CC, Alvarez RB, Engel WK, Askanas V. Increase of nitric oxide synthases and nitrotyrosine in inclusion-body myositis. Neuroreport. 1996;8:153–158
  111. Tateyama M, Takeda A, Onodera Y, et al. Oxidative Stress and predominant Abeta42(43) deposition in myopathies with rimmed vacuoles. Acta Neuropathol. 2003;105:581–585
  112. Banwell BL, Engel AG. AlphaB-crystallin immunolocalization yields new insights into inclusion body myositis [see comment]. Neurology. 2000;54:1033–1041
  113. Broccolini A, Engel WK, Alvarez RB, Askanas V. Redox factor-1 in muscle biopsies of patients with inclusion-body myositis. Neurosci Lett. 2000;287:1–4
  114. Butterfield DA. β-amyloid-associated free radical oxidative stress and neurotoxicity: implications for Alzheimer’s disease. Chem Res Toxicol. 1997;10:495–506
  115. van der Walt JM, Nicodemus KK, Martin ER, et al. Mitochondrial polymorphisms significantly reduce the risk of Parkinson disease. Am J Hum Genet. 2003;72:804–811
  116. Oldfors A, Moslemi AR, Jonasson L, Ohlsson M, Kollberg G, Lindberg C. Mitochondrial abnormalities in inclusion-body myositis. Neurology. 2006;66:S49–S55
  117. Fayet G, Jansson M, Sternberg D, et al. Ageing muscle: clonal expansions of mitochondrial DNA point mutations and deletions cause focal impairment of mitochondrial function. Neuromuscul Disord. 2002;12:484–493
  118. Santorelli FM, Sciacco M, Tanji K, et al. Multiple mitochondrial DNA deletions in sporadic inclusion body myositis: a study of 56 patients. Ann Neurol. 1996;39:789–795
  119. Oldfors A, Moslemi AR, Fyhr IM, Holme E, Larsson NG, Lindberg C. Mitochondrial DNA deletions in muscle fibers in inclusion body myositis. J Neuropathol Exp Neurol. 1995;54:581–587
  120. Horvath R, Fu K, Johns T, Genge A, Karpati G, Shoubridge EA. Characterisation of the Mitochondrial DNA abnormalities in the skeletal muscle of patients with Inclusion Body Myositis. J Neuropathol Exp Neurol. 1998;57:396–403
  121. Oldfors A, Moslemi AR, Holme E, Lindberg C. Mitochondrial alterations in sporadic inclusion-body myositis. In:  Askanas V,  Serratrice G,  Engel WK editor. Inclusion-body myositis and myopathies. Cambridge University Press; 1998;p. 306–317
  122. Argov Z, Taivassalo T, De Stefano N, Genge A, Karpati G, Arnold DL. Intracellular phosphates in inclusion body myositis – a 31P magnetic resonance spectroscopy study. Muscle Nerve. 1998;21:1523–1525
  123. Lodi R, Taylor DJ, Tabrizi SJ, et al. Normal in vivo skeletal muscle oxidative metabolism in sporadic inclusion body myositis assessed by 31P-magnetic resonance spectroscopy. Brain. 1998;121:2119–2126
  124. Oldfors A, Larsson NG, Lindberg C, Holme E. Mitochondrial DNA deletions in inclusion body myositis. Brain. 1993;116:325–336
  125. Pak JW, Herbst A, Bua E, Gokey N, McKenzie D, Aiken JM. Mitochondrial DNA mutations as a fundamental mechanism in physiological declines associated with aging. Aging Cell. 2003;2:1–7
  126. Giresi PG, Stevenson EJ, Theilhaber J, et al. Identification of a molecular signature of sarcopenia. Physiol Genomics. 2005;21:253–263
  127. Serdaroglu P. Muscle diseases and aging. In:  Mastaglia FL,  Hilton-Jones D editor. Handbook of clinical neurology myopathies. Elsevier; 2007;p. 357–388
  128. van der Vlies D, Woudenberg J, Post JA. Protein oxidation in aging: endoplasmic reticulum as a target. Amino Acids. 2003;25:397–407
  129. Goronzy JJ, Weyand CM. Aging, autoimmunity and arthritis: T-cell senescence and contraction of T-cell repertoire diversity – catalysts of autoimmunity and chronic inflammation. Arthritis Res Ther. 2003;5:225–234
  130. Weyand CM, Fulbright JW, Goronzy JJ. Immunosenescence, autoimmunity, and rheumatoid arthritis. Exp Gerontol. 2003;38:833–841
  131. Garlepp MJ, Laing B, Zilko PJ, Ollier W, Mastaglia F. HLA associations with inclusion body myositis. Clin Exp Immunol. 1994;98:40–45
  132. Needham M, Mastaglia FL, Garlepp MJ. Genetics of inclusion-body myositis. Muscle Nerve. 2007;35:549–561
  133. Sivakumar K, Semino-Mora C, Dalakas MC. An inflammatory, familial, inclusion body myositis with autoimmune features and a phenotype identical to sporadic inclusion body myositis. Studies in three families. Brain. 1997;120:653–661
  134. Needham M, Mastaglia FL. Inclusion Body Myosits: current pathogenic concepts, diagnostic and therapeutic approaches. Lancet Neurol. 2007;6:620–631
  135. Price P, Santoso L, Mastaglia F, et al. Two major histocompatibility complex haplotypes influence susceptibility to sporadic inclusion body myositis: critical evaluation of an association with HLA-DR3. Tissue Antigens. 2004;64:575–580
  136. O’Hanlon TP, Carrick DM, Arnett FC, et al. Immunogenetic risk and protective factors for the idiopathic inflammatory myopathies: distinct HLA-A, -B, -Cw, -CRB1 and -DQA1 allelic. Medicine. 2005;84:338–349
  137. Badrising UA, Schreuder GMT, Giphart MJ, et al. Associations with autoimmune disorders and HLA class I and II antigens in inclusion body myositis. Neurology. 2004;63:2396–2398
  138. Scott AP, Allcock R, Mastaglia F, Nishino I, Nonaka I, Laing N. Sporadic inclusion body myositis in Japanese is associated with the MHC ancestral haplotype 52.1. Neuromuscul Disord. 2006;16:311–315
  139. Price P, Campbell W, Allcock R, et al. The genetic basis for the association of the 8.1 ancestral haplotype (A1, B8, DR3) with multiple immunopathological diseases. Immunol Rev. 1999;167:257–274
  140. Scott A, Laing N, Mastaglia F, Needham M, Walter M, Dalakas M, et al. Recombinant mapping of MHC susceptibility region in sporadic Inclusion Body Myositis. Neuromuscul Disord. 2007;17:853–854
  141. von der Hagen M, Laval SH, Cree LM, et al. The differential gene expression profiles of proximal and distal muscle groups are altered in pre-pathological dysferlin-deficient mice. Neuromuscul Disord. 2005;15:863–877
  142. Arnardottir S, Borg K, Ansved T. Sporadic inclusion body myositis: morphology, regeneration, and cytoskeletal structure of muscle fibres. J Neurol Neurosurg Psychiatry. 2004;75:917–920
  143. Sugarman MC, Kitazawa M, Baker M, Caiozzo VJ, Querfurth HW, LaFerla FM. Pathogenic accumulation of APP in fast twitch muscle of IBM patients and a transgenic model. Neurobiol Aging. 2006;27:423–432
  144. Tiidus PM. Influence of estrogen on skeletal muscle damage, inflammation, and repair. Exerc Sport Sci Rev. 2003;31:40–44
  145. Tiidus PM. Estrogen and gender effects on muscle damage, inflammation, and oxidative stress. Can J Appl Physiol. 2000;25:274–287
  146. Dewing P, Chiang CW, Sinchak K, et al. Direct regulation of adult brain function by the male-specific factor SRY. Curr Biol. 2006;16:415–420
  147. Cantuti-Castelvetri I, Keller-McGandy C, Bouzou B, et al. Effects of gender on nigral gene expression and parkinson disease. Neurobiol Dis. 2007;
  148. van der Werf N, Kroese FGM, Rozing J, Hillebrands J-L. Viral infections as potential triggers of type 1 diabetes. Diabetes Metab Res Rev. 2007;23:169–183
  149. Gillespie KM. Type 1 diabetes: pathogenesis and prevention. CMAJ. 2006;175:165–170

PII: S0960-8966(07)00758-4

doi: 10.1016/j.nmd.2007.11.001

Neuromuscular Disorders
Volume 18, Issue 1 , Pages 6-16 , January 2008

Article Tools

* Image Usage & Resolution