Abstract
The same proteins accumulate in the brains of patients with sporadic or hereditary Alzheimer’s disease and in the muscle fibres of patients with sporadic inclusion-body myositis (s-IBM) and hereditary inclusion-body myopathy (h-IBM). The pathogenic mechanisms underlying both disorders may be similar. Therefore, IBM may serve as an easily accessible peripheral model for the aetiology of Alzheimer’s disease1.
Access this chapter
Tax calculation will be finalised at checkout
Purchases are for personal use only
Preview
Unable to display preview. Download preview PDF.
References
Askanas V, Engel WK (1998) Does overexpression of betaAPP in aging muscle have a pathogenic role and a relevance to Alzheimer’s disease? Clues from inclusion body myositis, cultured human muscle, and transgenic mice. Am J Pathol 153: 1673–1677.
Dalakas MC (1995) Update on the use of intravenous immune globulin in the treatment of patients with inflammatory muscle disease. J Clin Immunol 15: 70S–75S.
Dalakas MC, Sonies BC, Lopez-Devine J et al. (1996) Dysphagia as a frequent manifestation in patients with inclusion body myositis. Neurology 46: Suppl.
Chou SM (1993) Inclusion body myositis. Bailli¨¨res Clin Neurol 2: 557–577.
Dalakas MC (1991) Polymyositis, dermatomyositis and inclusion-body myositis. N Engl J Med 325: 1487–1498.
Sekul EA, Dalakas MC (1993) Inclusion body myositis: new concepts. Semin Neurol 13: 256–263.
Koffman BM, Rugiero M, Dalakas MC (1998) Immune-mediated conditions and antibodies associated with sporadic inclusion body myositis. Muscle Nerve 21: 115–117.
Askanas V, Engel WK (1998) Sporadic inclusion-body myositis and its similarities to Alzheimer disease brain. Recent approaches to diagnosis and pathogenesis, and relation to aging. Scand J Rheumatol 27: 389–405.
Bilak M, Askanas V, Engel WK (1993) Strong immunoreactivity of alpha 1antichymotrypsin co-localizes with beta-amyloid protein and ubiquitin in vacuolated muscle fibers of inclusion-body myositis. Acta Neuropathol 85: 378–382.
Askanas V, Bilak M, Engel WK et al. (1993) Prion protein is abnormally accumulated in inclusion-body myositis. Neuroreport 5: 25–28.
Roses AD (1996) Apolipoprotein E alleles as risk factors in Alzheimer’s disease. Annu Rev Med 47: 387–400.
Sandbrink R, Hartmann T, Masters CL et al. (1996) Genes contributing to Alzheimer’s disease. Mol Psychiatry 1:27–40.
Garlepp MJ, Tabarias H, van Bockxmeer FM et al. (1995) Apolipoprotein E epsilon 4 in inclusion body myositis. Ann Neurol 38: 957–959.
Lampe JB, Goßrau G, Gestrich B et al. (1999) Prion gene and apolipoprotein E in sporadic inclusion-body myositis. Ann Neurol 46: 485.
Harrington CR, Anderson JR, Chan KK (1995) Apolipoprotein E type epsilon 4 allele frequency is not increased in patients with sporadic inclusion-body myositis. Neurosci Lett 183: 35–38.
Goldfarb LG, Petersen RB, Tabaton M et al. (1992) Fatal familial insomnia and familial Creutzfeldt-Jakob disease: disease phenotype determined by a DNA polymorphism. Science 258: 806–808.
Laplanche JL, Delasnerie-Laupretre N, Brandel JP et al. (1994) Molecular genetics of prion diseases in France. French Research Group on Epidemiology of Human Spongiform Encephalopathies. Neurology 44: 2347–2351.
Deslys JP, Marce D, Dormont D (1994) Similar genetic susceptibility in iatrogenic and sporadic Creutzfeldt- Jakob disease. J Gen Virol 75: 23–27.
Palmer MS, Dryden AJ, Hughes JT et al. (1991) Homozygous prion protein genotype predisposes to sporadic Creutzfeldt- Jakob disease. Nature 352: 340–342.
Salvatore M, Genuardi M, Petraroli R et al. (1994) Polymorphisms of the prion protein gene in Italian patients with Creutzfeldt-Jakob disease. Hum Genet 94: 375–379.
Schulz-Schaeffer WJ, Giese A, Windl O et al. (1996) Polymorphism at codon 129 of the prion protein gene determines cerebellar pathology in Creutzfeldt-Jakob disease. Clin Neuropathol 15:353–357.
Hill AF, Desbruslais M, Joiner S et al. (1997) The same prion strain causes vCJD and BSE. Nature 389: 448–450.
Lampe J, Kitzler H, Walter MC et al. (1999) Methionine homozygosity at prion gene codon 129 may predispose to sporadic inclusion-body myositis. Lancet 353: 465–466.
Lampe JB, Goßrau G, Walter MC et al. (2000) Prion gene genetics and sporadic inclusion-body myositis. Alzheimer’s Report 3 (Suppl. 1): S35.
Mendell JR, Sahenk Z, Gales T et al. (1991) Amyloid filaments in inclusion body myositis. Novel findings provide insight into nature of filaments. Arch Neurol 48: 1229–1234.
DeArmond SJ, Prusiner SB (1997) Prion diseases. In: Greenfield’s Neuropathology (Graham DI, Lantos PL, eds), pp235–280, 6th ed. Vol II: Arnold, London.
Hsiao K.H, Baker F, Crow TJ et al. (1989) Linkage of a prion protein missense variant to Gerstmann-Straussler syndrome. Nature 338: 342–345.
Rosenthal NP, Keesey J, Crandall B et al. (1976) Familial neurological disease associated with spongiform encephalopathy. Arch Neurol 33: 252–259.
Beck EP, Daniel M, Parry HP (1964) Degeneration of the cerebellar and hypothalamoneurohypophysial systems in sheep with scrapie; and its relationship to human system degenerations. Brain 87: 153–176.
Bosanquet FD, Daniel PM, Parry HB (1956) Myopthy in sheep. Its relationship to scrapie and to dermatomyositis and muscular dystrophy. Lancet ii: 737–746.
Hulland WH (1958) The skeletal muscle of sheep affected with scrapie. J Comp Pathol Ther 68: 264–274.
De Armond SJ, Prusiner SB (1995) Etiology and pathogenesis of prion diseases. Am J Pathol 146: 785–811.
Global Surveillance, Diagnosis and Therapy of Human Transmissible Spongiform Encephalopathies. Report of a WHO Consultation and WHO/EMC/ZDI/98.9. 1998.
Sarkozi E, Askanas V, Engel WK (1994) Abnormal accumulation of prion protein mRNA in muscle fibers of patients with sporadic inclusion-body myositis and hereditary inclusion-body myopathy. Am J Pathol 145: 1280–1284.
Askanas V, Bilak M,Engel WK et al. (1993) Prion protein is strongly immunolocalized at the postsynaptic domain of human normal neuromuscular junctions. Neurosci Lett 159: 111–114.
Westaway D., DeArmond SJ, Cayetano-Canlas J et al. (1994) Degeneration of skeletal muscle, peripheral nerves, and the central nervous system in transgenic mice overexpressing wild-type prion proteins. Cell 76: 117–129.
Mitrani-Rosenbaum S, Argov Z, Blumenfeld A et al. (1996) Hereditary inclusion body myopathy maps to chromosome 9p1-ql. Hum Mol Genet 5: 159–163.
Martinsson T., Darin N, Kyllerman M et al. (1999) Dominant hereditary inclusion-body myopathy gene (IBM3) maps to chromosome region 17p13.!. Am J Hum Genet 64: 1420–1406.
Mikol J, Engel AG (1994) Inclusion body myositis. In: Myology (Engel AG, Franzini Armstrong C, eds), pp. 1384–1398, McGraw-Hill, New York.
Griggs RC, Askanas V, DiMauro S et al. (1995) Inclusion body myositis and myopathies. Ann Neurol 38: 705–713.
Hohlfeld R, Goebels N, Engel AG (1993) Cellular mechanisms in inflammatory myopathies. Bailli¨¨res Clin Neurol 2: 617–635.
Fyhr IM, Moslemi AR, Mosavi AA et al. (1997) Oligoclonal expansion of muscle infiltrating T cells in inclusion body myositis. J Neuroimmunol 79: 185–189.
Hohlfeld R. Engel AG (1991) Coculture with autologous myotubes of cytotoxic T cells isolated from muscle in inflammatory myopathies. Ann Neurol 29: 498–507.
Garlepp MJ (1993) Immunogenetics of inflammatory myopathies. Bailli¨¨res Clin Neurol 2: 579–297.
Garlepp MJ, Laing B, Zilko PJ (1994) HLA associations with inclusion body myositis. Clin Exp Immunol 98: 40–45.
Koffman BM, Sivakumar K, Simonis T et al. (1998) HLA allele distribution distinguishes sporadic inclusion body myositis from hereditary inclusion body myopathies. J Neuroimmunol 84: 139–142.
Rider LG, Gurley RC, Pandey JP et al. (1998) Clinical, serologic, and immunogenetic features of familial idiopathic inflammatory myopathy. Arthritis Rheum 41:710–719.
Lindberg C, Oldfors A, Tarkowski A (1995) Local T-cell proliferation and differentiation in inflammatory myopathies. Scand J Immunol 41: 421–426.
Kok CC, Croager EI, Witt CS et al. (1999) Mapping of a candidate region for susceptibility to inclusion body myositis in the human major histocompatibility complex. Immunogenetics 49: 508–516.
Goßrau G, Fiissel M, Walter MC et al. (2000) Histocompatibility antigens in sporadic inclusion-body myositis. Alzheimer’s Report 3 (Suppl 1): S58.
Fyhr IM, Moslemi AR, Tarkowski A et al. (1996) Limited T-cell receptor V gene usage in inclusion body myositis. Scand J Immunol 43: 109–114.
Carpenter S, Karpati G, Heller I et al. (1978) Inclusion body myositis: a distinct variety of idiopathic inflammatory myopathy. Neurology 28: 8–17.
Chou SM (1986) Inclusion body myositis: a chronic persistent mumps myositis? Hum Pathol 17: 765–777.
Fox SA, Ward BK, Robbins PD et al. (1996) Inclusion body myositis: investigation of the mumps virus hypothesis by polymerase chain reaction. Muscle Nerve 19: 23–28.
Nishino H, Engel AG, Rima BK. (1989) Inclusion body myositis: the mumps virus hypothesis. Ann. Neurol. 25:260–264.
Cupler EJ, Leon-Monzon M, Miller J et al. (1996) Inclusion body myositis in HIV-1 and HTLV-1 infected patients. Brain 119: 1887–1893.
Schlesinger I, Soifer D, Lossos A et al. (1996) Inclusion body myositis: atypical clinical presentations. Eur Neurol 36: 89–93.
Abarbanel JM, Lichtenfeld Y, Zirkin H et al. (1988) Inclusion body myositis in post-poliomyelitis muscular atrophy. Acta Neurol Scand 78: 81–84.
Gajdusek DC (1996) Infectious amyloidosis: subacute spongiform encphalopathies as transmissible cerebral amyloidosis. In: Fields Virology (Fields BN, Knipe DM, Howley PM eds), pp. 2851–2900, Lippincott-Raven Publishers, Philadelphia.
Come JH, Fraser PE, Lansbury PT Jr. (1993) A kinetic model for amyloid formation in the prion diseases: importance of seeding. Proc Natl Acad Sci USA 90: 5959–5963.
Welch WJ, Gambetti P (1998) Chaperoning brain diseases. Nature 392: 23–24.
Banwell BL, Engel AG (2000) AlphaB-crystallin immunolocalization yields new insights into inclusion body myositis. Neurology 54:1033–1041.
Askanas V, Engel WK, Alvarez RB et al. (2000) Inclusion body myositis, muscle blood vessel and cardiac amyloidosis, and transthyretin Va1122I1e allele. Ann. Neurol. 47:544–549.
Askanas V, McFerrin J, Alvarez RB (1997) Beta APP gene transfer into cultured human muscle induces inclusion-body myositis aspects. Neuroreport 8: 2155–2158.
Fukuchi K, Pham D,Hart M et al. (1998) Amyloid-beta deposition in skeletal muscle of transgenic mice: possible model of inclusion body myopathy. Am J Pathol 153: 1687–1693.
Jin LW, Hearn MG, Ogburn CE et al. (1998) Transgenic mice over-expressing the C99 fragment of betaPP with an alpha-secretase site mutation develop a myopathy similar to human inclusion body myositis. Am J Pathol 153: 1679–1686.
Yang CC, Alvarez RB, Engel, WK et al. (1996) Increase of nitric oxide synthases and nitrotyrosine in inclusion-body myositis. Neuroreport 8: 153–158.
Askanas V, Engel WK (1998) Sporadic inclusion-body myositis and hereditary inclusion-body myopathies: diseases of oxidative stress and aging? Arch Neurol 55: 915–920.
Yang CC, Alvarez RB, Engel WK (1998) Nitric oxide-induced oxidative stress in autosomal recessive and dominant inclusion-body myopathies. Brain 121: 1089–1097.
Schroder JM, Molnar M (1997) Mitochondrial abnormalities and peripheral neuropathy in inflammatory myopathy, especially inclusion body myositis. Mol Cell Biochem 174: 277–281.
Askanas V, Engel WK, Alvarez RB (1992) Light and electron microscopic localization of beta-amyloid protein in muscle biopsies of patients with inclusion-body myositis. Am J Pathol 141:31–36.
Author information
Authors and Affiliations
Editor information
Editors and Affiliations
Rights and permissions
Copyright information
© 2001 Springer Science+Business Media New York
About this chapter
Cite this chapter
Lampe, J.B., Walter, M.C., Reichmann, H. (2001). Neurodegeneration-Associated Proteins and Inflammation in Sporadic Inclusion-Body Myositis. In: Tolnay, M., Probst, A. (eds) Neuropathology and Genetics of Dementia. Advances in Experimental Medicine and Biology, vol 487. Springer, Boston, MA. https://doi.org/10.1007/978-1-4615-1249-3_18
Download citation
DOI: https://doi.org/10.1007/978-1-4615-1249-3_18
Publisher Name: Springer, Boston, MA
Print ISBN: 978-1-4613-5461-1
Online ISBN: 978-1-4615-1249-3
eBook Packages: Springer Book Archive