Microscopy research and technique, 2005-07, Vol.67 (3-4), p.114-120
2005
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- Autor(en) / Beteiligte
- Titel
- Molecular pathology and pathogenesis of inclusion-body myositis
- Ist Teil von
- Microscopy research and technique, 2005-07, Vol.67 (3-4), p.114-120
- Ort / Verlag
- Hoboken: Wiley Subscription Services, Inc., A Wiley Company
- Erscheinungsjahr
- 2005
- Quelle
- Wiley Online Library All Journals
- Beschreibungen/Notizen
- We summarize the molecular phenotype, diagnostic criteria, and the newest advances related to seeking the pathogenic mechanism(s) of sporadic inclusion‐body myositis (s‐IBM), a muscle disease usually of persons over age 50. On the basis of our research, several processes seem to be important in relation to the still‐speculative pathogenesis: 1) increased transcription and accumulation of amyloid‐β precursor protein (AβPP), and accumulation of its proteolytic fragment Aβ; 2) abnormal accumulation of cholesterol, caveolin‐1, and apolipoprotein E; 3) oxidative stress; 4) accumulations of intramuscle fiber multiprotein aggregates; and 5) evidence that unfolded/misfolded proteins participate in s‐IBM pathogenesis. Our basic hypothesis is that overexpression of AβPP within the aging muscle fibers is an early upstream event causing a subsequent pathogenic cascade. Microsc. Res. Tech. 67:114–120, 2005. © 2005 Wiley‐Liss, Inc.
- Sprache
- Englisch
- Identifikatoren
- ISSN: 1059-910XeISSN: 1097-0029DOI: 10.1002/jemt.20186Titel-ID: cdi_proquest_miscellaneous_68503186
- Format
- –
- Schlagworte
- Aging - metabolism, Aging - pathology, Amyloid beta-Protein Precursor - genetics, Amyloid beta-Protein Precursor - metabolism, amyloid-β, amyloid-β precursor protein, Apolipoproteins E - metabolism, Caveolin 1 - metabolism, Cholesterol - metabolism, Humans, misfolded proteins, Muscle Fibers, Skeletal - metabolism, Muscle Fibers, Skeletal - ultrastructure, Mutation, Myositis, Inclusion Body - etiology, Myositis, Inclusion Body - metabolism, Myositis, Inclusion Body - pathology, Oxidative Stress, phosphorylated tau, protein aggregates, Protein Folding