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• W1499492064 abstract "Sporadic inclusion-body myositis (s-IBM), the most common muscle disease of older persons, is of unknown cause and there is no enduring treatment. Its pathogenesis is complex and multifactorial. While it is agreed that both degeneration and mononuclear-cell inflammation are components of the s-IBM pathology, how each relates to the pathogenesis remains unsettled. We suggest that the intra-muscle-fiber degenerative component plays the primary role, leading to muscle-fiber destruction and clinical weakness. In this chapter we describe the multiple proteins that are accumulated in the form of aggregates within s-IBM muscle fibers, and we describe the most recent research advances directed toward a better understanding of mechanisms causing the protein misfolding and aggregation. We illustrate that, among other factors, abnormal aggregation of proteins is associated with their inadequate disposal, and these factors are combined with, and perhaps provoked by, an aging intracellular milieu. Other important and provocative phenomena present within s-IBM muscle fibers include endoplasmic reticulum stress and the unfolded protein response, and mitochondrial abnormalities: their possible roles in the s-IBM pathogenesis are discussed. Also considered are the intriguing pathologic similarities between s-IBM muscle fibers and the brains of patients with Alzheimer and Parkinson diseases, which are the most common neurodegenerative diseases associated with aging. Finally, we discuss possible treatment strategies aimed at ameliorating a degenerative component, since anti-inflammatory treatments thus far have been ineffective." @default.
• W1499492064 created "2016-06-24" @default.
• W1499492064 creator A5008326837 @default.
• W1499492064 creator A5029701142 @default.
• W1499492064 creator A5060033281 @default.
• W1499492064 date "2011-12-19" @default.
• W1499492064 modified "2023-09-27" @default.
• W1499492064 title "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" @default.
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