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Inclusion body myositis, sporadic

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... [Pg.661]

Sporadic inclusion-body myositis (s-EBM) plus genetico-diabetoid-2 dysimmune peripheral neuropathy, the latter very treatable with IVIG (see below). [Pg.34]

Oxidative damage to cells is a common phenomenon, and quality control of modified proteins is important to maintain normal cellular functions. In the cytoplasm, nucleus, and endoplasmic reticulum, the proteasome is involved in the removal of various types of proteins such as ubiquinated, misfolded, or unfolded proteins, and oxidized proteins. Abnormal inhibition of proteasome may contribute to neuro-degenerative diseases such as Alzheimer disease, Parkinson disease, Lewy body dementia, and Huntington disease [31-40]. Neuromuscular diseases, such as sporadic inclusion-body myositis (s-IBM) share several phenotypes described in the brain tissues of Alzheimer and Parkinson disease patients [41]. One such similarity to Alzheimer disease is the accumulation of amyloid-P (AP), phosphory-lated tau (p-tau), and ubiquitin, which are often found within these aggregates [42, 43]. In s-IBM patients, significant proteasome abnormalities were identified including, increased 26 S proteasome expression and abnormal accumulation of 26S proteasome, but reduced proteasome activities [44]. The inverse relationship between increased expression... [Pg.91]

Fratta P, Engel WK, McFerrin J et al. (2005) Protea-some inhibition and aggresome formation in sporadic inclusion-body myositis and in amyloid-beta precursor protein-overexpressing cultured human muscle fibers. Am J Pathol 167(2), 517-526. [Pg.95]

Santorelli FM, SdaccoM, Tanji K et al. (1996) Multiple mitochondrial DNA deletions in sporadic inclusion body myositis a study of 56 patients. Ann Neurol 39 (6), 789-795. [Pg.96]

Pathogenesis of sporadic inclusion-body myositis role of aging and muscle-fiber degeneration, and accumulation of the same proteins as in Alzheimer and Parkinson brains... [Pg.111]

Mirabella M, Alvarez RB, Bilak M et al. (1996) Difference in expression of phosphorylated tau epitopes between sporadic inclusion-body myositis and hereditary inclusion-body myopathies. J Neuropathol Exp Neurol 55, 774-786. [Pg.136]

Vattemi G, Nogalska A, King Engel W et al. (2009) Amyloid-beta42 is preferentially accumulated in muscle fibers of patients with sporadic inclusion-body myositis. Acta Neuropathol 117, 569-574. [Pg.136]

Vattemi G, Kefi M, Engel WK et al. (2003) Nicastrin, a novel protein partidpating in amyloid-beta production, is overexpressed in sporadic inclusion-body myositis muscle. Neurology 60, A315. [Pg.137]

Askanas V, Engel WK, Yang CC etal. (1998) Light and electron microscopic immunolocaUzation of preseni-lin 1 in abnormal muscle fibers of patients with sporadic inclusion-body myositis and autosomal-recessive indusion-body myopathy. Am J Pathol 152, 889-895. [Pg.137]

Wojcik S, Engel WK, Yan R et al. (2007) NOGO is increased and binds to BACEl in sporadic inclusion-body myositis and in A beta PP-overexpressing cultured human musde fibers. Acta Neuropathol 114, 517-526. [Pg.137]

Choi YC, Park GT, Kim TS et al. (2003) Sporadic inclusion body myositis correlates with increased expression and cross-linking by transglutaminases 1 and 2. J Biol Chem 275, 8703-8710. [Pg.137]

Lunemann JD, Schmidt J, Schmid D et al. (2007) Beta-amyloid is a substrate of autophagy in sporadic inclusion body myositis. Ann Neurol 61, 476 83. [Pg.137]

Nogalska A, Terracciano C, D Agostino C et al. (2009) p62/SQSTMl is overexpressed and prominently accumulated in inclusions of sporadic inclusion-body myositis musde fibers, and can help differentiating it from polymyositis and dermatomyositis. Acta Neuropathol 118, 407-413. [Pg.137]

Ozturk A, McFerrin J, Engel W et al. (2004) HSP70 chaperone machinery in sporadic-inclusion-body myositis musde fibers. Neurology 62, A154. [Pg.137]

Askanas V, Sarkozi E, Alvarez RB et al. (1996) Superoxide dismutase-1 gene and protein in vacuolated muscle fibers of sporadic inclusion-body myositis, hereditary inclusion-body myopathy, and cultured human muscle after beta-amyloid precursor protein gene transfer. Neurology 46, A487. [Pg.137]

Broccolini A, Engel WK, Alvarez RB et al. (1998) Possible pathogenic role of malondialdehyde, a toxic product of Upid peroxidation, in sporadic inclusion-body myositis. Neurology 50, A367-A368. [Pg.138]

Broccolini A Mirault MB, Engel WK et al. (1999) Abnormal accumulation of seleno-glutathion peroxidase-1 and catalase and their mRNAs in sporadic inclusion-body myositis. Neurology 52 (Suppl. 2), A333. [Pg.138]

Nogalska A, Engel W, Askanas V. (2007) Abnormalities of peroxisome proliferator-activated receptor gamma in sporadic inclusion-body myositis muscle fibers. Ann Neurol 62, S13. [Pg.138]

D Agostino C, Nogalska A, Engel WKetal. (2011) In sporadic inclusion-body myositis muscle fibres TDP-43-positive inclusions are less frequent and robust than p62-inclusions, and are not associated with paired helical filaments. Neuropathol Appl Neurobiol 37, 315-320. [Pg.138]

Guerin C, SinnreichM, Karpati G. (2008) Transcri-tional dysregulation in muscle fibers in sporadic inclusion body myositis (slBM). Neurology 7 (Suppl. 3), A304. [Pg.139]


See other pages where Inclusion body myositis, sporadic is mentioned: [Pg.453]    [Pg.14]    [Pg.56]    [Pg.56]    [Pg.110]    [Pg.111]    [Pg.114]    [Pg.116]    [Pg.118]    [Pg.122]    [Pg.126]    [Pg.128]    [Pg.130]    [Pg.132]    [Pg.134]    [Pg.136]    [Pg.137]    [Pg.140]    [Pg.141]   
See also in sourсe #XX -- [ Pg.22 , Pg.34 , Pg.113 , Pg.130 ]




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