[1]. [1]Chou SM. Myxovirus-like structures in a case of human chronic polymyositis. Science. 1967;158:1453–1455. MEDLINE
[2]. [2]Yunis EJ, Samaha FJ. Inclusion body myositis. Lab Invest. 1971;25:240–248. MEDLINE
[3]. [3]Pruitt JN, Showalter CJ, Engel AG. Sporadic inclusion body myositis: counts of different types of abnormal fibers. Ann Neurol. 1996;39:139–143. MEDLINE |
CrossRef
[4]. [4]Dalakas MC. Muscle biopsy findings in inflammatory myopathies. Rheum Dis Clin North Am. 2002;28:779–798. |
CrossRef
[5]. [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]. [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]. [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. MEDLINE |
CrossRef
[8]. [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. MEDLINE |
CrossRef
[9]. [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. Abstract | Full Text |
Full-Text PDF (374 KB)
|
CrossRef
[10]. [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. Abstract | Full Text |
Full-Text PDF (537 KB)
|
CrossRef
[11]. [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. MEDLINE |
CrossRef
[12]. [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.
CrossRef
[13]. [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.
CrossRef
[14]. [14]Greenberg SA, Pinkus GS, Amato AA, Pinkus JL. Myeloid dendritic cells in inclusion-body myositis and polymyositis. Muscle Nerve. 2007;35:17–23.
CrossRef
[15]. [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.
CrossRef
[16]. [16]Karpati G, Pouliot Y, Carpenter S. Expression of immunoreactive major histocompatibility complex products in human skeletal muscles. Ann Neurol. 1988;23:64–72. MEDLINE |
CrossRef
[17]. [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]. [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. MEDLINE
[19]. [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. MEDLINE
[20]. [20]Fyhr IM, Oldfors A. Upregulation of fas/fas-ligand in inclusion body myositis. Ann Neurol. 1998;43:127–130. MEDLINE |
CrossRef
[21]. [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. Abstract | Full Text |
Full-Text PDF (392 KB)
|
CrossRef
[22]. [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.
CrossRef
[23]. [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. MEDLINE |
CrossRef
[24]. [24]Germain RN. MHC-dependent antigen processing and peptide presentation: providing ligands for T lymphocyte activation. Cell. 1994;76:287–299. MEDLINE |
CrossRef
[25]. [25]Greenberg SA, Bradshaw EM, Pinkus JL, et al. Plasma cells in muscle in inclusion body myositis and polymyositis. Neurology. 2005;65:1782–1787.
CrossRef
[26]. [26]Greenberg SA, Sandoudou D, Haslett JN, Kohane IS, Kunkel LM, Beggs AH. Molecular profiles of inflammatory myopathies. Neurology. 2002;59:1170–1182. MEDLINE
[27]. [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.
CrossRef
[28]. [28]Dalakas MC, Illa I, Gallardo E, Juarez C. Inclusion body myositis and paraproteinemia: incidence and immunopathologic correlations. Ann Neurol. 1997;41:100–104. MEDLINE |
CrossRef
[29]. [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.
CrossRef
[30]. [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.
CrossRef
[31]. [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. MEDLINE
[32]. [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. Abstract | Full Text |
Full-Text PDF (543 KB)
|
CrossRef
[33]. [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. Abstract |
Full-Text PDF (860 KB)
|
CrossRef
[34]. [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. MEDLINE |
CrossRef
[35]. [35]Dalakas MC. Molecular immunology and genetics of inflammatory muscle diseases. Arch Neurol. 1998;55:1509–1512. MEDLINE |
CrossRef
[36]. [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. Abstract | Full Text |
Full-Text PDF (219 KB)
|
CrossRef
[37]. [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. MEDLINE |
CrossRef
[38]. [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]. [39]Dalakas MC. Sporadic inclusion body myositis – diagnosis, pathogenesis and therapeutic strategies. Nat Clin Pract. 2006;2:437–445.
[40]. [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. MEDLINE |
CrossRef
[41]. [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. MEDLINE
[42]. [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.
CrossRef
[43]. [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. MEDLINE |
CrossRef
[44]. [44]Pahl HL. Activators and target genes of Rel/NF-κB transcription factors. Oncogene. 1999;18:6853–6866. MEDLINE |
CrossRef
[45]. [45]Askanas V, Engel WK. Molecular pathology and pathogenesis of inclusion-body myositis. Microsc Res Tech. 2005;67:114–120.
CrossRef
[46]. [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. MEDLINE |
CrossRef
[47]. [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. MEDLINE |
CrossRef
[48]. [48]Chou SM. Inclusion body myositis: a chronic persistent mumps myositis?. Hum Pathol. 1986;17:765–777. MEDLINE |
CrossRef
[49]. [49]Nishino H, Engel AG, Rima BK. Inclusion body myositis: the mumps virus hypothesis. Ann Neurol. 1989;25:260–264. MEDLINE |
CrossRef
[50]. [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.
CrossRef
[51]. [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.
CrossRef
[52]. [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. MEDLINE |
CrossRef
[53]. [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. MEDLINE |
CrossRef
[54]. [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. Abstract |
CrossRef
[55]. [55]Christen U, von Herrath MG. Initiation of autoimmunity. Curr Opin Immunol. 2004;16:759–767. MEDLINE |
CrossRef
[56]. [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. MEDLINE |
CrossRef
[57]. [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.
CrossRef
[58]. [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]. [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.
CrossRef
[60]. [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. MEDLINE |
CrossRef
[61]. [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. MEDLINE |
CrossRef
[62]. [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. MEDLINE |
CrossRef
[63]. [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. MEDLINE
[64]. [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]. [65]Lunemann JD, Schmidt J, Dalakas MC, Munz C. Macroautophagy as a pathomechanism in sporadic inclusion body myositis. Autophagy. 2007;3:384–386. MEDLINE
[66]. [66]Karpati G, Carpenter S. Pathology of the inflammatory myopathies. Baillieres Clin Neurol. 1993;2:527–556. MEDLINE
[67]. [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.
CrossRef
[68]. [68]Carpenter S, Karpati G, Heller I, Eisen A. Inclusion body myositis: a distinct variety of idiopathic inflammatory myopathy. Neurology. 1978;28:8–17. MEDLINE
[69]. [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. MEDLINE
[70]. [70]Griggs RC, Askanas V, DiMauro S, et al. Inclusion body myositis and myopathies. Ann Neurol. 1995;38:705–713. MEDLINE |
CrossRef
[71]. [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. Abstract | Full Text |
Full-Text PDF (825 KB)
|
CrossRef
[72]. [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. MEDLINE |
CrossRef
[73]. [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. MEDLINE
[74]. [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. |
CrossRef
[75]. [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]. [76]Li J, Yin C, Okamoto H, et al. Proteomic analysis of inclusion body myositis. J Neuropathol Exp Neurol. 2006;65:826–833. MEDLINE |
CrossRef
[77]. [77]Hutchinson DO, Jongbloed B. Two-dimensional gel electrophoresis in inclusion body myositis. J Clin Neurosci, in press.
[78]. [78]Johnston JA, Ward CL, Kopito RR. Aggresomes: a cellular response to misfolded proteins. J Cell Biol. 1998;143:1883–1898. MEDLINE |
CrossRef
[79]. [79]Kopito RR. Aggresomes, inclusion bodies and protein aggregation. Trends Cell Biol. 2000;10:524–530. MEDLINE |
CrossRef
[80]. [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. MEDLINE
[81]. [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. MEDLINE
[82]. [82]Bence NF, Sampat RM, Kopito RR. Impairment of the ubiquitin-proteasome system by protein aggregation. Science. 2001;292:1552–1555. MEDLINE |
CrossRef
[83]. [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. MEDLINE |
CrossRef
[84]. [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. MEDLINE |
CrossRef
[85]. [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. MEDLINE |
CrossRef
[86]. [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. MEDLINE
[87]. [87]Mayer RJ, Landon M, Lowe J. Ubiquitin and the molecular pathology of human disease. New York: Plenum Press; 1998;.
[88]. [88]Varshavsky A. The ubiquitin system. Trends Biochem Sci. 1997;22:383–387. MEDLINE |
CrossRef
[89]. [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]. [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. MEDLINE |
CrossRef
[91]. [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. Abstract | Full Text |
Full-Text PDF (1205 KB)
|
CrossRef
[92]. [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. MEDLINE |
CrossRef
[93]. [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]. [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. MEDLINE
[95]. [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. MEDLINE
[96]. [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. MEDLINE
[97]. [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. MEDLINE |
CrossRef
[98]. [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. MEDLINE |
CrossRef
[99]. [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. MEDLINE |
CrossRef
[100]. [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. MEDLINE
[101]. [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. Abstract | Full Text |
Full-Text PDF (429 KB)
|
CrossRef
[102]. [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]. [103]Vetrivel KS, Thinakaran G. Amyloidogenic processing of beta-amyloid precursor protein in intracellular compartments. Neurology. 2006;66:S69–S73.
CrossRef
[104]. [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]. [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. MEDLINE
[106]. [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]. [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. MEDLINE |
CrossRef
[108]. [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. MEDLINE |
CrossRef
[109]. [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]. [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. MEDLINE
[111]. [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]. [112]Banwell BL, Engel AG. AlphaB-crystallin immunolocalization yields new insights into inclusion body myositis [see comment]. Neurology. 2000;54:1033–1041. MEDLINE
[113]. [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. MEDLINE |
CrossRef
[114]. [114]Butterfield DA. β-amyloid-associated free radical oxidative stress and neurotoxicity: implications for Alzheimer’s disease. Chem Res Toxicol. 1997;10:495–506.
CrossRef
[115]. [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. MEDLINE |
CrossRef
[116]. [116]Oldfors A, Moslemi AR, Jonasson L, Ohlsson M, Kollberg G, Lindberg C. Mitochondrial abnormalities in inclusion-body myositis. Neurology. 2006;66:S49–S55.
CrossRef
[117]. [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. Abstract | Full Text |
Full-Text PDF (340 KB)
|
CrossRef
[118]. [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. MEDLINE |
CrossRef
[119]. [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. MEDLINE |
CrossRef
[120]. [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. MEDLINE |
CrossRef
[121]. [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]. [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.
CrossRef
[123]. [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.
CrossRef
[124]. [124]Oldfors A, Larsson NG, Lindberg C, Holme E. Mitochondrial DNA deletions in inclusion body myositis. Brain. 1993;116:325–336.
[125]. [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. MEDLINE |
CrossRef
[126]. [126]Giresi PG, Stevenson EJ, Theilhaber J, et al. Identification of a molecular signature of sarcopenia. Physiol Genomics. 2005;21:253–263.
CrossRef
[127]. [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]. [128]van der Vlies D, Woudenberg J, Post JA. Protein oxidation in aging: endoplasmic reticulum as a target. Amino Acids. 2003;25:397–407. MEDLINE |
CrossRef
[129]. [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]. [130]Weyand CM, Fulbright JW, Goronzy JJ. Immunosenescence, autoimmunity, and rheumatoid arthritis. Exp Gerontol. 2003;38:833–841. MEDLINE |
CrossRef
[131]. [131]Garlepp MJ, Laing B, Zilko PJ, Ollier W, Mastaglia F. HLA associations with inclusion body myositis. Clin Exp Immunol. 1994;98:40–45. MEDLINE
[132]. [132]Needham M, Mastaglia FL, Garlepp MJ. Genetics of inclusion-body myositis. Muscle Nerve. 2007;35:549–561.
CrossRef
[133]. [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.
CrossRef
[134]. [134]Needham M, Mastaglia FL. Inclusion Body Myosits: current pathogenic concepts, diagnostic and therapeutic approaches. Lancet Neurol. 2007;6:620–631. Abstract | Full Text |
Full-Text PDF (348 KB)
|
CrossRef
[135]. [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. MEDLINE |
CrossRef
[136]. [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]. [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]. [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. Abstract | Full Text |
Full-Text PDF (79 KB)
|
CrossRef
[139]. [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. MEDLINE |
CrossRef
[140]. [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. Full Text |
Full-Text PDF (48 KB)
|
CrossRef
[141]. [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. Abstract | Full Text |
Full-Text PDF (386 KB)
[142]. [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. MEDLINE |
CrossRef
[143]. [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. Abstract | Full Text |
Full-Text PDF (560 KB)
|
CrossRef
[144]. [144]Tiidus PM. Influence of estrogen on skeletal muscle damage, inflammation, and repair. Exerc Sport Sci Rev. 2003;31:40–44. MEDLINE |
CrossRef
[145]. [145]Tiidus PM. Estrogen and gender effects on muscle damage, inflammation, and oxidative stress. Can J Appl Physiol. 2000;25:274–287. MEDLINE
[146]. [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. MEDLINE |
CrossRef
[147]. [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]. [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. MEDLINE |
CrossRef
[149]. [149]Gillespie KM. Type 1 diabetes: pathogenesis and prevention. CMAJ. 2006;175:165–170.
CrossRef