Protein myositis

The rabbits had no abnormality clearly attributable to II other than purulent, Indurative myositis at the site of Injection In nine of 10 animals. Inasmuch as the solutions injected were not stated to have been sterilized, the myositis is not astonishing. The stomachs of the three dogs all had fibrosed mucous membranes at the cardiac and/or pyloric regions. The plasmas of these dogs had subnormal concentrations of albumin and total protein and low albumin globulin ratios. 

The alphaviruses are a group of 26 icosahedral, positive-sense RNA viruses primarily transmitted by mosquitoes [64]. These 700-A-diameter viruses are some of the simplest of the membrane-enveloped viruses, and members of this group cause serious tropical diseases with characteristic symptoms such as myositis, fever, rash, encephalitis, and polyarthritis [65]. The structures of two different alphavirus-Fab complexes have been determined by cryo-TEM Ross River virus (RR) and Sindbis virus (SIN) [66]. The amino acid sequences of the RR and SIN virus structural and nonstructural proteins are 49 and 64% identical, respectively [67]. The viral RNA genome and 240 copies of the capsid protein form the nucleocapsid core [68-73], and the El and E2 glycoproteins form heterodimers that associate as 80 trimeric spikes on the viral surface. Native SIN and RR lack the E3 glycoprotein because it disassociates from the spike complex after its display on the plasma membrane surface [74, 75]. El has a putative fusion domain that may facilitate host membrane penetration [76, 77]. E2 contains most of the neutralizing epitopes and is also probably involved in host cell recognition [78-80]. 

Mixed connective tissue disease (MCTD). Systemic autoimmune disease with features of systemic lupus erythematosus, systemic sclerosis, and dermatomyositis/polymyositis and high-titred autoantibodies against Ul-RNP specific proteins. See also myositis, autoimmune. 

Myositis, autoimmune. Rare systemic inflammatory myopathies, including primary polymyositis, primary dermatomyositis, myositis associated with malignancy, childhood dermatomyositis, and myositis with multisystem autoimmune disease (e.g. mixed connective tissue disease, systemic sclerosis). Autoantibodies against aminoacyl-tRNA synthetases (e.g. anti-Jo-1), signal recognition particle (e.g. anti-SRP54), nuclear helicase (anti-Mi-2), tRNA and tRNA-protein complexes (e.g. anti-Mas), and translation factor (anti-KJ) have been described as myositis specific. 

In rats administered myrrh at doses of 1000 mg/kg orally, 500 mg/kg intramuscularly, or 250 mg/kg intraperitoneally for 2 weeks, animals exhibited the following symptoms depression, soft feces, jaundice, ruffled hair, hepatone-phropathy, hemorrhagic myositis and patchy peritonitis (at the injection site), and death. These were accompanied by increases in serum ALP and ALT activities, bilirubin, and creatinine concentrations, and decreases in total protein and albumin levels, and macrocytic anemia and leukopenia. Doses of 500 mg/kg administered orally or 250 mg/kg administered intramuscularly were not lethal, and when given daily for 1 week the effects were less marked (Omer et al. 1999). 

This presentation may be difficult to distinguish from antibiotic-resistant infectious pneumonia as sputum production, fever (25), and increased C-reactive protein (CRP) levels (24) are frequent. Pneumomediastinum and subcutaneous emphysema are occasional features (26,228,241). DAD is usually present at SLB (25,228,253,256), although NSIP is also described (25,234). Rapidly progressive ILD occurs more often in DM than in PM, at least in Asian populations, and is most frequent in patients with less prominent myositis (25,26,228,253,256). A novel antibody in CADM, anti-CADM-140 may be associated with rapidly progressive ILD (262). In 35.7% to 84.4% of cases, ILD is chronic, with insidious dyspnea and cough... 

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... 

Askanas V, Engel WK. (2003) Proposed pathogenetic cascade of inclusion-body myositis importance of amyloid-beta, misfolded proteins, predisposing genes, and aging. Curr Opin Rheumatol 15(6), 737-744. 

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. 

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... 

Askanas V, Engel WK, Nogalska A. (2009) Inclusion body myositis a degenerative muscle disease associated with intra-muscle fiber multi-protein aggregates, proteasome inhibition, endoplasmic reticulum stress and decreased lysosomal degradation. Brain Pathol 19, 493-506. 

Askanas V, Engel WK. (2006) Inclusion-body myositis a myodegenerative conformational disorder associated with Abeta, protein misfolding, and proteasome inhibition. Neurology 66, S39-S48. 

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. 

Askanas V, Bilak M, Engel WK et al. (1993) Prion protein is abnormally accumulated in inclusion-body myositis. Neuroreport 5, 25-28. 

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. 

Wilczynski GM Engel WK, Askanas V. (2000) Association of active extracellular signal-regulated protein kinase with paired helical filaments of indusion-body myositis muscle suggests its role in indusion-body myositis tau phosphorylation. Am J Pathol 156, 1835-1840. 

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. 

Broccolini A, Engel WK, Alvarez RB et al. (2000) Paired helical filaments of inclusion-body myositis muscle contain RNA and survival motor neuron protein. Am J Pathol 156, 1151-1155. 

Sarkozi E, Askanas V, Johnson SA et al. (1993) beta-Amyloid precursor protein mRNA is increased in inclusion-body myositis muscle. Neuroreport 4, 815-818. 

Nogalska A Wojcik S, Engel WK et al. (2007) Endoplasmic reticulum stress induces myostatin precursor protein and NF-kappaB in cultured human muscle fibers relevance to inclusion body myositis. Exp Neurol 204, 610-618. 

Wojdk S, Nogalska A, McFerrin J et al. (2007) Myos-tatin precursor protein is increased and associates with amyloid-beta precursor protein in inclusion-body myositis culture model. Neuropathol Appl Neu-... 

Kumamoto T, Ueyama H, Tsumura H et al. (2004) Expression of lysosome-related proteins and genes in the skeletal musdes of inclusion body myositis. Acta Neuropathol 107, 59-65. 

Muth IE, Barthel K, Bahr M et al. (2009) Proinflam -matory cell stress in sporadic inclusion body myositis muscle overexpression of aB-crystallin is associated with amyloid precursor protein and accumulation of p-amyloid. J Neurol Neurosurg Psychiatry 80, 1344-1349. 

Wojcik S, Paciello O, Engel WK et al. (2007) In sporadic inclusion-body myositis muscle fiber cytoplasm, cytochrome c aggregates with a-synudein and amyloid-beta precursor protein, but does not activate caspase-3. Neuromuscul Disord 17, 853. 

Ferrer I, Carmona M, Blanco R et al. (2005) involvement of clusterin and the aggresome in abnormal protein deposits in myofibrillar myopathies and inclusion body myositis. Brain Pathol 15, 101-108. 

Kovacs GG, Lindeck-Pozza B, Chimelli L et al. (2004) Creutzfeldt-Jakob disease and inclusion body myositis abundant disease-associated prion protein in muscle. Ann Neurol 55(1), 121-125. 

Abdo WF, van Mierlo T, Hengstman GJ et al. (2009) Increased plasma amyloid-beta42 protein in sporadic inclusion body myositis. Acta Neuropathol 118(3), 429-431. 

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