Sporadic Inclusion-body Myositis and Its Similarities to Alzheimer Disease Brain: Recent Approaches to Diagnosis and Pathogenesis, and Relation to Aging

References

• Yunis EJ, Samaha FJ. Inclusion body myositis. Lab Invest 1971;25:240 — 8.
   PubMedGoogle Scholar
• Askanas V, Engel WK. New advances in inclusion-body myo-sitis. Curr Opin Rheumatol 1993;5:732 — 41.
   PubMedGoogle Scholar
• Askanas V, Engel WK. Newest approaches to diagnosis and pathogenesis of sporadic inclusion-body myositis and heredi-tary inclusion-body myopathies, including molecular-patho-logic similarities to Alzheimer disease. In: Askanas V, Serratrice G, Engel WK, eds. Inclusion-Body Myositis and Myopathies. United Kingdom: Cambridge University Press; 1998:3–78.
   Google Scholar
• Askanas V, Engel WK. Recent progress and classification of the hereditary inclusion-body myopathies. Acta Myologica 1997;1:21 —5.
   Google Scholar
• Askanas V, Engel WK. New advances in the understanding of sporadic inclusion-body myositis and hereditary inclusion-body myopathies. Curr Opin Rheumatol 1995;7:486 —96.
   PubMedGoogle Scholar
• Shapiro J, DeGirolami U, Martin S, Goyal R. Inflammatory myopathy causing pharyngeal dysphagia: a new entity. Ann Otol Rhinol Laryngol 1996;105:331 — 5.
   PubMedGoogle Scholar
• Engel WK, Haginoya K, Alvarez RB, Sabetian K, Bajoghli M, Askanas V. Sporadic inclusion-body myositis (s-IBM) in an HTLV-I-positive Iranian Muslim. Neurology 1997;48:124.
   Google Scholar
• Engel WK, Askanas V. Treatment of inclusion-body myositis and hereditary inclusion-body myopathy with reference to pathogenic mechanisms. Personal experience. In: Askanas V, Serratrice G, Engel WK, eds. Inclusion-Body Myositis and Myopathies. United Kingdom: Cambridge University Press; 1998:351 — 82.
   Google Scholar
• Cupler El, 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;119:1887–93.
   PubMed Web of Science ®Google Scholar
• Schlesinger I, Soffer D, Lossos A, Meiner Z, Argov Z. Inclu-sion body myositis: atypical clinical presentations. Eur Neurol 1996;36:89–93.
   Google Scholar
• Abarbanel JM, Lichtenfeld Y, Zirkin H, Louzon Z, Osimani A, Farkash P, et al. Inclusion body myositis in post-poliomye-litis muscular atrophy. Acta Neurol Scand 1988;78:81–4.
   PubMedGoogle Scholar
• Dalakas MC, Illa I, Leon-Monzon M. Viruses, immunodefi-ciency, and inclusion-body myositis. In: Askanas V, Serratrice G, Engel WK, eds. Inclusion-Body Myositis and Myopathies. United Kingdom: Cambridge University Press; 1998:275–90.
   Google Scholar
• Kula RW, Engel WK, Line BR. Scanning for soft-tissue amy-loid. Lancet 1977;i:92–3.
   Google Scholar
• Askanas V, Engel WK, Alvarez RB, Frangione B, Ghiso J, Vidal R. Unusual pathologic features of sporadic inclusion-body myositis (s-IBM) accompanied by muscle blood-vessel amyloidosis in an African-American patient with cardiac amyloidosis, homozygous for the transthyretin (TTR) Ile-122 allele. Ann Neurol 1998;44:460.
   Google Scholar
• Jacobson DR, Pastore RD, Yaghoubian R, Kane I, Gallo G, Buck FS, et al. Variant-sequence transthyretin (isoleucine 122) in late-onset cardiac amyloidosis in black Americans. N Engl J Med 1997;336:466–73.
   PubMed Web of Science ®Google Scholar
• Felice KJ, Grunnet ML. Inclusion body myositis associated with a severe unilateral levodopa-responsive upper extremity tremor. Muscle Nerve 1996;19:787–9.
   PubMedGoogle Scholar
• Jensen ML, Wieting M, Andary MT, Fankhauser MJ, Jones MJ. Inclusion body myositis and transitional cell carcinoma of the bladder: significant resolution of symptoms after tumor excision. Arch Phys Med Rehabil 1997;78:327–9.
   Google Scholar
• Alexander JA, Huebner CJ. Hepatitis C and inclusion body myositis. Am J Gastroenterol 1996;91:1845–7.
   PubMedGoogle Scholar
• Ytterberg SR, Roelofs RI, Mahowald ML. Inclusion body myositis and renal cell carcinoma: report of two cases and review of the literature. Arthritis Rheum 1993;36:416–21.
   Google Scholar
• Koffman BM, Rugiero M, Dalakas MC. Immune-mediated conditions and antibodies associated with sporadic inclusion body myositis. Muscle Nerve 1998;21:115–7.
   Google Scholar
• Mastaglia FL, Phillips BA, Zilko P. Treatment of inflamma-tory myopathies. Muscle Nerve 1997;20:651–64.
   PubMed Web of Science ®Google Scholar
• Oddis CV. Therapy for myositis. Curr Opin Rheumatol 1993;5:742–8.
   PubMedGoogle Scholar
• Sayers ME, Chou SM, Calabrese LH. Inclusion-body myosi-tis: analysis of 32 cases. J Rheumatol 1992;19: 1385–9.
   Google Scholar
• Dalakas MC, Sonies B, Dambrosia J, Sekul E, Cupler E, Sivakumar K. Treatment of inclusion-body myositis with IVIg: a double-blind, placebo-controlled study. Neurology 1997;48:712–6.
   PubMed Web of Science ®Google Scholar
• Griggs RC, Rose M. Evaluation of treatment for sporadic inclusion-body myositis. In: Askanas V, Serratrice G, Engel WK, eds. Inclusion-Body Myositis and Myopathies. United Kingdom: Cambridge University Press; 1998:331–50.
   Google Scholar
• Engel WK, Cunningham GG. Rapid examination of muscle tissue - an improved trichrome method for fresh-frozen biopsy sections. Neurology 1963;13:919–23.
   PubMed Web of Science ®Google Scholar
• Eisen A, Berry K, Gibson S. Inclusion body myositis (IBM): myopathy or neuropathy? Neurology 1983;33:1109–14.
   Google Scholar
• Lindberg C, Oldfors A, Hedström A. Inclusion body myositis: peripheral nerve involvement. Combined morphological and electrophysiological studies on peripheral nerves. J Neurol Sci 1990;99:327–38.
   Google Scholar
• Schröder JM, Molnar M. Mitochondrial abnormalities and peripheral neuropathy in inflammatory myopathy, especially inclusion body myositis. Mol Cell Biochem 1997;174:277–81.
   Google Scholar
• Luciano CA, Dalakas MC. Inclusion body myositis: no evi-dence for a neurogenic component. Neurology 1997;48:29–33.
   PubMedGoogle Scholar
• Oldfors A, Moslemi A.-R, Fyhr I.-M, Holme E, Larsson N.-G, Lindberg C. Mitochondrial DNA deletions in muscle fibers in inclusion body myositis. J Neuropathol Exp Neurol 1995;54:581–7.
   Google Scholar
• Santorelli FM, Sciacco M, Tanji K, Shanske S, Vu TH, Golzi V, et al. Multiple mitochondrial DNA deletions in sporadic inclusion body myositis: a study of 56 patients. Ann Neurol 1996;39:789–95.
   PubMedGoogle Scholar
• Oldfors A, Moslemi A.-R, Holme E, Lindberg C. Mitochon-drial alterations in sporadic inclusion-body myositis. In: Askanas V, Serratrice G, Engel WK, eds. Inclusion-Body Myositis and Myopathies. United Kingdom: Cambridge Uni-versity Press; 1998:306–17.
   Google Scholar
• Desnuelle C, Paquis V, Paul R, Engel WK, Saunieres A, Alvarez RB, et al. Mitochondrial DNA analysis in muscle of patients with sporadic inclusion-body myositis and hereditary inclusion-body myopathy. In: Askanas V, Serratrice G, Engel WK, eds. Inclusion-Body Myositis and Myopathies. United Kingdom: Cambridge University Press; 1998:318–28.
   Google Scholar
• Askanas V, Engel WK, Alvarez RB. Light- and electronmi-croscopic localization of 13-amyloid protein in muscle biopsies of patients with inclusion-body myositis. Am J Pathol 1992;141: 31–6.
   Google Scholar
• Mendell JR, Sahenk Z, Gales T, Paul L. Amyloid filaments in inclusion body myositis. Arch Neurol 1991;48:1229–34.
   PubMedGoogle Scholar
• Askanas V, Engel WK, Alvarez RB. Enhanced detection of congo-red-positive amyloid deposits in muscle fibers of inclu-sion-body myositis and brain of Alzheimer disease using fluo-rescence technique. Neurology 1993;43:1265–7.
   Google Scholar
• Askanas V, Alvarez RB, Mirabella M, Engel WK. Use of anti-neurofilament antibody to identify paired-helical filaments in inclusion-body myositis. Ann Neurol 1996;39:389–91.
   PubMedGoogle Scholar
• Askanas V, Serdaroglu P, Engel WK, Alvarez RB. Immuno-cytochemical localization of ubiquitin in inclusion-body myo-sitis allows its light-microscopic distinction from polymyositis. Neurology 1992;42:460–1.
   PubMedGoogle Scholar
• Prayson RA, Cohen ML. Ubiquitin immunostaining and inclusion body myositis: study of 30 patients with inclusion body myositis. Hum Pathol 1997;28:887–92.
   PubMedGoogle Scholar
• Askanas V, Engel WK, Mirabella M. Idiopathic inflamma-tory myopathies: inclusion-body myositis, polymyositis, and dermatomyositis. Curr Opin Neurol 1994;7:448–56.
   Google Scholar
• Askanas V, Engel WK, Bilak M, Alvarez RB, Selkoe DJ. Twisted tubulofilaments of inclusion-body myositis muscle resemble paired helical filaments of Alzheimer brain and con-tain hyperphosphorylated tau. Am J Pathol 1994;144:177–87.
   Google Scholar
• Mirabella M, Alvarez RB, Bilak M, Engel WK, Askanas V. Difference in expression of phosphorylated tau epitopes between sporadic inclusion-body myositis and hereditary inclusion-body myopathies. J Neuropathol Exp Neurol 1996;55:774–86.
   Google Scholar
• Askanas V, Alvarez RB, Engel WK. 13-amyloid precursor epi-topes in muscle fibers of inclusion-body myositis. Ann Neurol 1993;34: 551–60.
   Google Scholar
• Askanas V, Engel WK, Yang C.-C, Alvarez RB, Lee VM-Y, Wisniewski T. Light and electron microscopic immunolocali-zation of Presenilin 1 in abnormal muscle fibers of patients with sporadic inclusion-body myositis and autosomal-reces-sive inclusion-body myopathy. Am J Pathol 1998;152: 889–95.
   Google Scholar
• Villanova M, Kawai M, Lubke U, Oh SJ, Perry G, Six J, et al. Rimmed vacuoles of inclusion body myositis and oculophar-yngeal muscular dystrophy contain amyloid precursor protein and lysosomal markers. Brain Res 1993;603:343–7.
   PubMedGoogle Scholar
• Selkoe DJ. Normal and abnormal biology of the 13-amyloid precursor protein. Annu Rev Neurosci 1994;17:489–517.
   PubMed Web of Science ®Google Scholar
• Ksiezak-Reding H, Dickson DW, Davies P, Yen S-H. Recognition of tau epitopes by anti-neurofilament antibodies that bind to Alzheimer neurofibrillary tangles. Proc Natl Acad Sci U.S.A. 1987;84:3410–4.
   Google Scholar
• Schmidt ML, Lee VM-Y, Trojanowski JQ. Relative abun-dance of tau and neurofilament epitopes in hippocampal neu-rofibrillary tangles. Am J Pathol 1990;136:1069–75.
   Google Scholar
• Vickers JC, Delacourte A, Morrison JH. Progressive transfor-mation of the cytoskeleton associated with normal aging and Alzheimer's disease. Brain Res 1992;594:273–8.
   Google Scholar
• Askanas V, Alvarez RB, Sarkozi E, Bilak M, Mirabella M, Tome FMS, et al. Partial expression in oculopharyngeal mus-cular dystrophy (OPMD) muscle fibers of the intracellular phenotype of sporadic inclusion-body myositis (s-IBM). Neu-rology 1997;48:331.
   Google Scholar
• Glenner GG, Wong CW. Alzheimer's disease. Initial report of the purification and characteristics of a novel cerebrovascular amyloid protein. Biochem Biophys Res Commun 1984;120:885–90.
   PubMed Web of Science ®Google Scholar
• Masters CL, Simms G, Weinman NA, Multhaup G, McDonald BL, Beyreuther K. Amyloid plaque core protein in Alzheimer's disease and Down's syndrome. Proc Natl Acad Sci U.S.A. 1985;82:4245–9.
   PubMed Web of Science ®Google Scholar
• Selkoe DJ, Abraham CR, Podlisny MB, Duffy LK. Isolation of low molecular weight proteins from amyloid plaque fibers in Alzheimer's disease. J Neurochem 1986;146:1820–34.
   Google Scholar
• Kang J, Lermaine HG, Unterbeck A, Salbaum JM, Masters CL, Grzeschik KH, et al. The precursor of Alzheimer's dis-ease amyloid A4 protein resembles a cell-surface receptor. Nature 1987;325:733–6.
   PubMed Web of Science ®Google Scholar
• Robakis NK, Ramakrishna N, Wolfe G, Wisniewski HM. Molecular cloning and characterization of a cDNA encoding the cerebrovascular and neuritic plaque amyloid peptides. Proc Natl Acad Sci U.S.A. 1987;84:4190–4.
   PubMed Web of Science ®Google Scholar
• Askanas V, Engel WK, Alvarez RB. Strong immunoreactivity of 13-amyloid precursor protein, including the 13-amyloid pro-tein sequence, at human neuromuscular junctions. Neurosci Lett 1992;143: 96–100.
   Google Scholar
• Leclerc A, Tome FMS, Fardeau M. Ubiquitin and 13-amyloid-protein in inclusion-body myositis (IBM), familial IBM-like disorder and oculopharyngeal muscular dystrophy: an immu-nocytochemical study. Neuromuscul Disord 1993;3: 283–91.
   Google Scholar
• Figarella-Branger D, Baeta-Machado A, Putzu G, Pellissier JF. Inclusion-body myositis: pathologic changes. In: Askanas V, Serratrice G, Engel WK, eds. Inclusion-Body Myositis and Myopathies. United Kingdom: Cambridge Uni-versity Press; 1998:137–55.
   Google Scholar
• Tanzi RE, Hyman BT. Studies of amyloid beta-protein precur-sor expression in Alzheimer's disease. Ann NY Acad Sci 1991;640:149–54.
   PubMedGoogle Scholar
• Sarkozi E, Askanas V, Johnson SA, Engel WK, Alvarez RB. 13-amyloid precursor protein mRNA is increased in inclusion-body myositis muscle. Neuroreport 1993;4: 815–8.
   Google Scholar
• Marz J. Boring in on 13-amyloid's role in Alzheimer's. Science 1992;255:688–9.
   PubMedGoogle Scholar
• Goedert M. Tau protein and the neurofibrillary pathology of Alzheimer's disease. Trends Neurosci 1993;16(11):460–5.
   PubMed Web of Science ®Google Scholar
• Kosik KS. The molecular and cellular biology of tau. Brain Pathol 1993;3:39–43.
   PubMed Web of Science ®Google Scholar
• Mandelkow EM, Mandelkow E. Tau as a marker for Alzhei-mer's disease. Trends Biochem Sci 1993;18:480–3.
   PubMedGoogle Scholar
• Trojanowski JQ, Lee VM-Y. Phosphorylation of neuronal cytoskeletal proteins in Alzheimer's disease and lewy body dementias. Ann NY Acad Sci U.S.A. 1994;747:92–109.
   PubMedGoogle Scholar
• Goedert M, Spillantini MG, Jakes R, et al. Molecular dissec- tion of the paired helical filament. Neurobiol Aging 1995;16:325–34.
   PubMedGoogle Scholar
• Goedert M, Spillantini MG, Cairns NJ, Crowther RA. Tau proteins of Alzheimer paired helical filaments: abnormal phosphorylation of all six brain isoforms. Neuron 1992;8:159–68.
   PubMed Web of Science ®Google Scholar
• Mandelkow EM, Biernat J, Drewes G, Gustke N, Trinczek B, Mandelkow E. Tau domains, phosphorylation, and interac-tions with microtubules. Neurobiol Aging 1995;16:355–63.
   PubMed Web of Science ®Google Scholar
• Smith MA, Taneda S, Richey PL, et al. Advanced maillard reaction end products are associated with Alzheimer disease pathology. Proc Natl Acad Sci U.S.A. 1994;91:5710–4.
   PubMed Web of Science ®Google Scholar
• Strittmatter WJ, Weisgraber KH, Huang DY, Dong L.-M, Salvesen GS, Pericak-Vance M, et al. Binding of human apo-lipoprotein E to synthetic amyloid 13 peptide: isoform-specific effects and implications for late-onset Alzheimer disease. Proc Natl Acad Sci U.S.A. 1993;90: 8098–102.
   Google Scholar
• Saunders AM, Strittmatter WJ, Schmechel D, St. George-Hyslop PH, Pericak-Vance MA, Joo SH, et al. Association of apolipoprotein E allele E4 with late-onset familial and sporadic Alzheimer's disease. Neurology 1993;43: 1467–72.
   Google Scholar
• Namba Y, Tomonaga M, Kawasaki H, Otomo E, Ikeda K. Apolipoprotein E immunoreactivity in cerebral amyloid deposits and neurofibrillary tangles in Alzheimer's disease and kuru plaque amyloid in Creutzfeldt-Jakob disease. Brain Res 1991;541:163–6.
   Google Scholar
• Wisniewski T, Frangione B. Apolipoprotein E: a pathological chaperone protein in patients with cerebral and systemic amy-loid. Neurosci Lett 1992;135:235–8.
   PubMed Web of Science ®Google Scholar
• Askanas V, Mirabella M, Engel WK, Alvarez RB, Weisgraber KH. Apolipoprotein E immunoreactive deposits in inclusion-body muscle diseases. Lancet 1994;343:364–5.
   Google Scholar
• Mirabella M, Alvarez RB, Engel WK, Weisgraber KH, Askanas V. Apolipoprotein E and apolipoprotein E messen-ger RNA in muscle of inclusion-body myositis and myopa-thies. Ann Neurol 1996;40:864–72.
   Google Scholar
• Garlepp MJ, Tabarias H, van Bockxmeer FM, Zilko PJ, Laing B, Mastaglia FL. Apolipoprotein E E4 in inclusion body myo-sitis. Ann Neurol 1995;38:957–9.
   PubMedGoogle Scholar
• Harrington CR, Anderson JR, Chan KK. Apolipoprotein E type E4 allele frequency is not increased in patients with sporadic inclusion-body myositis. Neurosci Lett 1995;183: 35–8.
   Google Scholar
• Askanas V, Engel WK, Mirabella M, Weisgraber KH, Saunders AM, Roses AD, et al. Apolipoprotein E alleles in sporadic inclusion-body myositis and hereditary inclusion-body myopathy. Ann Neurol 1996;40:264.
   PubMedGoogle Scholar
• Hershko A, Ciechanover A. The ubiquitin system for protein degradation. Annu Rev Biochem 1992;61:761–807.
   PubMed Web of Science ®Google Scholar
• Jentsch S. Ubiquitin-dependent protein degradation: A cellu-lar perspective. Trends Cell Biol 1992;2:98–103.
   PubMedGoogle Scholar
• Mitch WE, Goldberg AL. Mechanisms of muscle wasting. The role of the ubiquitin-proteasome pathway. New Engl J Med 1996;335:1897–905.
   PubMed Web of Science ®Google Scholar
• Lowe J, Mayer RJ, Landon M. Ubiquitin in neurodegenera-tive diseases. Brain Pathol 1993;3:55–65.
   Google Scholar
• Askanas V, Serdaroglu P, Engel WK, Alvarez RB. Immunolo-calization of ubiquitin in muscle biopsies of patients with inclusion-body myositis and oculopharyngeal muscular dys-trophy. Neurosci Lett 1991;130:73–6.
   PubMedGoogle Scholar
• Albrecht S, Bilbao JM. Ubiquitin expression in inclusion-body myositis. Arch Pathol Lab Med 1993;117:789–93.
   PubMedGoogle Scholar
• Serdaroglu P, Askanas V, Engel WK. Immunocytochemical localization of ubiquitin at human neuromuscular junctions. Neuropathol Appl Neurobiol 1992;18:232–6.
   PubMed Web of Science ®Google Scholar
• Cenciarelli C, Hou D, Hsu K.-C, Rellahan BL, Wiest DL, Smith HT, et al. Activation-induced ubiquitination of the T cell antigen receptor. Science 1992;257:795–7.
   Google Scholar
• Carrell RW, Travis J. Serpins: the superfamily of plasma ser-ine protease inhibitors. In: Barret A, Salvesen G, eds. Protease Inhibitors. Amsterdam: Elsevier; 1987:403–20.
   Google Scholar
• Abraham CR, Selkoe DJ, Potter H. Immunochemical identi-fication of the serine protease inhibitor al -antichymotrypsin in the brain amyloid deposits of Alzheimer's disease. Cell 1988;52:487–501.
   Google Scholar
• Abraham CR, Shirahama T, Potter H. ai -antichymotrypsin is associated solely with amyloid deposits containing the I3-pro-tein. Amyloid and cell localization of ai-antichymotrypsin. Neurobiol Aging 1990;11: 223–39.
   Google Scholar
• Bilak M, Askanas V, Engel WK. Abnormalities of the serine proteases chymotrypsin (CT) and cathepsin G and their inhi-bitor (serpin) ai -antichymotrypsin (ai -ACT) in muscle biop-sies of inclusion-body myositis. J Neuropathol Exp Neurol 1993;52:277.
   Google Scholar
• Hardy J. Amyloid, the presenilins and Alzheimer's disease. TINS 1997;20:154–9.
   PubMed Web of Science ®Google Scholar
• Murphy, Jr GM, Forno LS, Ellis WG, Nochlin D, Levy-Lahad E, et al. Antibodies to presenilin proteins detect neurofibril-lary tangles in Alzheimer's disease. Am J Pathol 1996;149:1839–46.
   Google Scholar
• Wisniewski T, Dowjat W, Permanne B, Palha J, Kumar A, Gallo G, et al. Presenilin-1 is associated with Alzheimer's dis-ease amyloid. Am J Pathol 1997;151:601–10.
   PubMedGoogle Scholar
• Busciglio J, Hartmann H, Lorenzo A, Wong C, Buamann K, Sommer B, et al. Neuronal localization of presenilin-1 and association with amyloid plaques and neurofibrillary tangles in Alzheimer's disease. J Neurosci 1997;17:5101–7.
   PubMedGoogle Scholar
• Levey Al, Heilman CJ, Lah JJ, Nash NR, Rees HD, Wakai M, et al. Presenilin-1 protein expression in familial and sporadic Alzheimer's disease. Ann Neurol 1997;41:742–53.
   PubMedGoogle Scholar
• Askanas V, Bilak M, Engel WK, Alvarez RB, Tome FMS, Leclerc A. Prion protein is abnormally accumulated in inclu-sion-body myositis. Neuroreport 1993;5:25–8.
   PubMedGoogle Scholar
• Prusiner SB, Hsiao KK. Human prion diseases. Ann Neurol 1994;35:385–95.
   PubMed Web of Science ®Google Scholar
• Askanas V, Bilak M, Engel WK, Leclerc A, Tome FMS. Prion protein is strongly immunolocalized at the postsynaptic domain of human normal neuromuscular junctions. Neurosci Lett 1993;159:111–4.
   Google Scholar
• Askanas V, Sarkozi E, Bilak M, Alvarez RB, Engel WK. Human muscle macrophages express I3-amyloid precursor and prion proteins and their mRNAs. Neuroreport 1995;6: 1045–9.
   Google Scholar
• Sarkozi E, Askanas V, Engel WK. Abnormal accumulation of prion protein mRNA in muscle fibers of patients with spora-dic inclusion-body myositis and hereditary inclusion-body myopathy. Am J Pathol 1994;145:1280–4.
   Google Scholar
• Mikol J, Engel AG. Inclusion body myositis. In: Engel AG, Franzini-Armstrong C, eds. Myology: Basic and Clinical, vol 2. New York: McGraw-Hill, Inc.; 1994:1384–98.
   Google Scholar
• Garlepp MJ, Mastaglia FL. Inclusion body myositis. J Neurol Neurosurg Psychiatry 1996;60:251–5.
   PubMedGoogle Scholar
• Mantegazza R, Bernasconi P, Confalonieri P, Conelio F. Inflammatory myopathies and systemic disorders: a review of immunopathogenetic mechanisms and clinical features. J Neurol 1997;244:277–87.
   PubMedGoogle Scholar
• Hohlfeld R, Bender A, Engel AG. Inflammatory, nuclear, and mitochondrial abnormalities in inclusion-body myositis and inclusion-body myopathies. In: Askanas V, Serratrice G, Engel WK, eds. Inclusion-Body Myositis and Myopathies. United Kingdom: Cambridge University Press; 1998:263–74.
   Google Scholar
• De Bleecker JL, Engel AG. Immunocytochemical study of CD45 T cell isoforms in inflammatory myopathies. Am J Pathol 1995;146:1178–87.
   PubMedGoogle Scholar
• Bender A, Ernst N, Iglesias A, Dornmair K, Wekerle H, Hohlfeld R. T cell receptor repertoire in polymyositis: clonal expansion of autoaggressive CD8 + T cells. J Exp Med 1995;181:1863–8.
   PubMed Web of Science ®Google Scholar
• Bender A, Behrens L, Engel AG, Hohlfeld R. T-cell heteroge-neity in muscle lesions of inclusion body myositis. J Neuroim-munol 1998;84:86–91.
   PubMedGoogle Scholar
• Fyhr I.-M, Moslemi A.-R, Mosavi AA, Lindberg C, Tarkowski A, Oldfors A. Oligoclonal expansion of muscle infiltrating T cells in inclusion body myositis. J Neuroimmu-nol 1997;79:185–9.
   Google Scholar
• Behrens L, Bender A, Johnson MA, Hohlfeld R. Cytotoxic mechanisms in inflammatory myopathies. Co-expression of Fas and protective Bc1-2 in muscle fibres and inflammatory cells. Brain 1997;120:929–38.
   Google Scholar
• Fyhr I.-M, Oldfors A. Upregulation of Fas/Fas ligand in inclusion body myositis. Ann Neurol 1998;43:127–30.
   Google Scholar
• Schneider C, Gold R, Dalakas MC, Schmied M, Lassmann H, Toyka KY, 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;55:1205–9.
   PubMedGoogle Scholar
• Mirabella M, Engel WK, Passinetti G, Finch CE, Askanas V. Denervation of adult human muscle fibers induces apoptosis, evidenced by fragmentation of nuclear DNA, and increased expression of the clusterin (ApoJ) gene. Neurology 1996;46:270.
   Google Scholar
• Cid MC, Grau J.-M, Casademont J, Tobias E, Picazo A, Coll-Vinent B, et al. Leucocyte /endothelial cell adhesion receptors in muscle biopsies from patients with idiopathic inflammatory myopathies (IIM). Clin Exp Immunol 1996;104:467–73.
   Google Scholar
• Tews DS, Goebel HH. Cytokine expression profile in idio-pathic inflammatory myopathies. J Neuropathol Exp Neurol 1996;55:342–7.
   PubMed Web of Science ®Google Scholar
• Tews DS, Goebel HH. Expression of cell adhesion molecules in inflammatory myopathies. J Neuroimmunol 1995;59:185–94.
   PubMed Web of Science ®Google Scholar
• Lundberg I, Ulfgren A.-K, Nyberg P, Andersson U, Klareskog L. Cytokine production in muscle tissue of patients with idiopathic inflammatory myopathies. Arthritis Rheum 1997;40:865–74.
   Google Scholar
• Haginoya K, Alvarez RB, Engel WK, Askanas V. Light- and electron-microscopic immunolocalization of interleukins 1, 113 and 6 in vacuolated muscle fibers of sporadic inclusion-body myositis (s-IBM). Neurology 1997;8:126.
   Google Scholar
• Kissel JT, Mendell JR, Rammohan KW. Microvascular deposition of complement membrane attack complex in der-matomyositis. New Engl J Med 1986;314:329–34.
   Google Scholar
• Spuler S, Engel AG. Unexpected sarcolemmal complement membrane attack complex deposits on nonnecrotic muscle fibers in muscular dystrophies. Neurology 1998;50:41–6.
   PubMed Web of Science ®Google Scholar
• Pruitt JN, Showalter CJ, Engel AG. Sporadic inclusion body myositis: counts of different types of abnormal fibers. Ann Neurol 1996;39:139–43.
   Google Scholar
• Askanas V, Engel WK. Sporadic inclusion-body myositis and hereditary inclusion-body myopathies. Diseases of oxidative stress and aging? Arch Neurol 1998;55:915–20.
   PubMedGoogle Scholar
• Hino S, Doi H. Mechanisms of HTLV-1 Transmission. In: Roman GC, Vernant J-C, Osame M, Hurst MJ, eds. HTLV-1 and the Nervous System. New York: Alan R. Liss, Inc.; 1989:495–501.
   Google Scholar
• Beckman JS, Koppenol WH. Nitric oxide, superoxide, and peroxynitrite: the good, the bad, and ugly. Am J Physiol 1996;271:C1424–37.
   PubMed Web of Science ®Google Scholar
• Yang C.-C, Alvarez RB, Engel WK, Askanas V. Increase of nitric oxide synthases and nitrotyrosine in inclusion-body myositis. Neuroreport 1996; 8:153 — 8.
   Google Scholar
• Yang C.-C, Alvarez RB, Engel WK, Heller SL, Askanas V. Nitric-oxide induced oxidative stress in autosomal recessive and dominant inclusion-body myopathies. Brain 1998;121:1089 —97.
   Google Scholar
• Broccolini A, Engel WK, Alvarez RB, Thomas CE, Yang C.- C, Askanas V. Possible pathogenic role of malondialdehyde, a toxic product of lipid peroxidation, in inclusion-body myosi-tis. Neurology 1998; 50:367 — 8.
   Google Scholar
• Yang C.-C, Askanas V, Engel WK, Alvarez RB. Immunoloca-lization of transcription factor NF-KB in inclusion-body myo-sitis muscle and at normal human neuromuscular junctions. Neurosci Lett 1998;254:1 —4.
   Google Scholar
• Butterfield DA. B-amyloid-associated free radical oxidative stress and neurotoxicity: implications for Alzheimer's disease. Chem Res Toxicol 1997;10:495 — 506.
   PubMedGoogle Scholar
• Askanas V. New developments in hereditary inclusion-body myopathies. Ann Neurol 1997;41:421 —2.
   PubMedGoogle Scholar
• Lippa CF, Saunders AM, Smith TW, Swearer JM, Drachman DA, Ghetti B, et al. Familial and sporadic Alzheimer's dis- ease: neuropathology cannot exclude a final common path-way. Neurology 1996;46:406— 12.
   PubMedGoogle Scholar
• Hyman BT. Alzheimer's disease or Alzheimer's diseases? Clues from molecular epidemiology. Ann Neurol 1996;40:135 —6.
   PubMedGoogle Scholar
• Askanas V, McFerrin J, Baque S, Alvarez RB, Sarkozi E, Engel WK. Transfer of fi-amyloid precursor protein gene using adenovirus vector causes mitochondrial abnormalities in cultured normal human muscle. Proc Natl Acad Sci U.S.A. 1996;93:1314 — 9.
   PubMedGoogle Scholar
• Askanas V, McFerrin J, Alvarez RB, Baque S, Engel WK. PAPP gene transfer into cultured human muscle induces inclu-sion-body myositis aspects. Neuroreport 1997;8: 2155 — 8.
   Google Scholar
• McFerrin J, Engel WK, Askanas V. Impaired innervation of cultured human muscle overexpressing PAPP experimentally and genetically: Relevance to inclusion-body myopathies. Neuroreport 1998;9:(in press).
   Google Scholar
• Askanas V, Engel WK, Alvarez RB. Fourteen newly recog-nized proteins at the human neuromuscular junctions — and their non-junctional accumulation in inclusion-body myositis. In: Richman DP, ed. Myasthenia Gravis and Related Dis-eases: Disorders of the Neuromuscular Junction, vol 841. New York: Ann NY Acad Sci; 1998:28 — 56.
   Google Scholar