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Proteasome Inhibition and Aggresome Formation in Sporadic Inclusion-Body Myositis and in Amyloid-β Precursor Protein-Overexpressing Cultured Human Muscle Fibers
Open accessAbstract
The 26S proteasome system is involved in eliminating various proteins, including ubiquitinated misfolded/unfolded proteins, and its inhibition results in cellular accumulation of protein aggregates. Intramuscle-fiber ubiquitinated multiprotein-aggregates are characteristic of sporadic inclusion-body myositis (s-IBM) muscle fibers. Two major types of aggregates exist, containing either amyloid-beta (Abeta) or phosphorylated tau (p-tau). We have now asked whether abnormalities of the 26S proteasome contribute to s-IBM pathogenesis and whether the multiprotein aggregates have features of aggresomes. Using cultured human muscle fibers we also studied the effect of amyloid-beta precursor protein (AbetaPP) overexpression on proteasome function and the influence of proteasome inhibition on aggresome formation. We report that in s-IBM muscle biopsies 26S proteasome subunits were immunodetected in the gamma-tubulin-associated aggresomes, which also contained Abeta, p-tau, ubiquitin, and HSP70. In addition, a) expression of proteasome subunits was greatly increased, b) the 20Salpha proteasome subunit co-immunoprecipitated with AbetaPP/Abeta, and c) the three major proteasomal proteolytic activities were reduced. In cultured muscle fibers, AbetaPP-overexpressing fibers displayed diminished proteasomal proteolytic activities, and addition of proteasome inhibitor strikingly increased aggresome formation. Accordingly, proteasome dysfunction in s-IBM muscle fibers may play a role in accumulation of misfolded, potentially cytotoxic proteins and may be induced by increased intracellular AbetaPP/Abeta.
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“In muscle, an association between proteasome abnormalities and muscle disease has also been reported (Fratta et al., 2005; Askanas and Engel, 2006).”
From Inducible Rpt3, a Proteasome Component, Knockout in Adult Skeletal Muscle Results in Muscle Atrophy (2020) · cites this paper as Fratta et al., 2005
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Dalakas, M. C. (2011) · doi:10.1002/9781444398311.ch8 · Cited by 5
Mitochondrial dynamics in degenerative disease and disease models
Merzetti, E. M., & Staveley, B. E. (2013) · Neuroscience Discovery · doi:10.7243/2052-6946-1-8 · Cited by 5
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Inclusion body myositis pathomechanism and therapy
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Brady, S., Healy, E. G., Machado, P., Parton, M. J., Holton, J. L., & Hanna, M. G. (2014) · Clinical Practice · doi:10.2217/cpr.14.54 · Cited by 2
The Amyloid _-Protein and Alzheimer's Disease
Teplow, D. B., Yang, M., Roychaudhuri, R., Pang, E. S., Huynh, T. V., Chen, M., & Beroukhim, S. (2012) · Frontiers in neuroscience · doi:10.1201/b11986-2 · Cited by 2
Askanas, V., Engel, W. K., & Nogalska, A. (2011) · Wiley eBooks · doi:10.1002/9781444398311.ch7 · Cited by 2
Self-citationClearance of intracellular aggregation-prone protein fragments
Gillis, J. (2009) · UvA-DARE (University of Amsterdam)
Metadata
- Authors
- Fratta, P., Engel, W. K., McFerrin, J., Davies, K. J. A., Lin, S. W., & Askanas, V.
- Affiliations
- University of Southern California (US)
- Corresponding author
- Askanas, Valerie
- Venue
- The American Journal of Pathology
- Publisher
- Elsevier BV
- Published
- 2005-08
- Volume
- 167
- Issue
- 2
- Pages
- 517-526
- ISSN
- 0002-9440 (ISSN-L)
- PMC
- PMC1603556
- OpenAlex
- W1987807233
- Cited by
- 111
- References
- 47
- Citations by year
- 2025: 1 · 2024: 5 · 2022: 3 · 2021: 3 · 2020: 4 · 2018: 1 · 2017: 2 · 2016: 3 · 2015: 4 · 2014: 5 · 2013: 7 · 2012: 6
- FWCI
- 9.56
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- American Journal Of Pathology (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- UCL Discovery (University College London) (submittedVersion)
- Funders
- Muscular Dystrophy Association (AG16768)
- Myositis Association
- National Institutes of Health
- National Institute on Aging (AG 16768, R37AG016768)
- Topics
- Health Sciences › Medicine › Rheumatology › Inflammatory Myopathies and Dermatomyositis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- sporadic inclusion body myositis, proteasome inhibition, aggresomes, 26S proteasome, amyloid precursor protein, amyloid-beta, phosphorylated tau, protein aggregates, misfolded protein accumulation, HSP70, ubiquitin, proteasome dysfunction
- MeSH terms
- Cells, Cultured, Humans, Amyloid beta-Protein Precursor, tau Proteins, Muscle Fibers, Skeletal, HSP70 Heat-Shock Proteins, Myositis, Inclusion Body, Ubiquitin, Proteasome Endopeptidase Complex, Proteasome Inhibitors
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