The DOI matches its Crossref record; 47 of the 47 references it cites were found in a registry or an index.
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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Cites
Impairment of the Ubiquitin-Proteasome System by Protein Aggregation
Bence, N., Sampat, R. M., & Kopito, R. R. (2001) · Science · doi:10.1126/science.292.5521.1552 · Cited by 2,209
Aggresomes: A Cellular Response to Misfolded Proteins
Johnston, J. A., Ward, C. L., & Kopito, R. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1883 · Cited by 2,148
Aggresomes, inclusion bodies and protein aggregation
Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,942
The 26S Proteasome: A Molecular Machine Designed for Controlled Proteolysis
Voges, D., Zwickl, P., & Baumeister, W. (1999) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.68.1.1015 · Cited by 1,608
Cellular Defenses against Unfolded Proteins
Sherman, M. Y., & Goldberg, A. L. (2001) · Neuron · doi:10.1016/s0896-6273(01)00177-5 · Cited by 996
Epoxomicin, a potent and selective proteasome inhibitor, exhibits in vivo antiinflammatory activity
Meng, L., Mohan, R., Kwok, B. H. B., Elofsson, M., Sin, N., & Crews, C. M. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10403 · Cited by 938
Impaired Proteasome Function in Alzheimer's Disease
Keller, J. N., Hanni, K. B., & Markesbery, W. R. (2000) · Journal of Neurochemistry · doi:10.1046/j.1471-4159.2000.0750436.x · Cited by 848
Antigen processing by the proteasome
Kloetzel, P. (2001) · Nature Reviews Molecular Cell Biology · doi:10.1038/35056572 · Cited by 638
Rapid examination of muscle tissue
Engel, W. K., & Cunningham, G. G. (1963) · Neurology · doi:10.1212/wnl.13.11.919 · Cited by 585
Self-citationAltered proteasomal function in sporadic Parkinson’s disease
St. P. McNaught, K., Belizaire, R., Isacson, O., Jenner, P., & Olanow, C. W. (2003) · Experimental Neurology · doi:10.1006/exnr.2002.8050 · Cited by 573
Research works printed but not linked: 1
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Ngo, J. K., & Davies, K. J. A. (2011) · doi:10.1002/9781444398311.ch5
Self-citationImmunobiology of Autoimmune Inflammatory Myopathies
Dalakas, M. C. (2007) · Elsevier eBooks · doi:10.1016/b978-012088592-3/50089-x
Peth, A. (2007) · edoc Publication server (Humboldt University of Berlin) · doi:10.18452/15686
Review Sporadic inclusion body myositis: a continuing puzzle
Needham, M., & Mastaglia, F. L. (2007)
Wiley, C. A. (2007) · Yearbook of Pathology and Laboratory Medicine · doi:10.1016/s1077-9108(08)70407-9
Monis, G. F., Skinner, M. M., Eberhard, J., Connors, L. H., & Trinkaus‐Randall, V. (2007) · CRC Press eBooks · doi:10.1201/9781420043358.ch7
Role of the Ubiquitin-Proteasome Pathway in Skeletal Muscle
Kitajima, Y., & Suzuki, N. (2017) · Springer eBooks · doi:10.1007/978-981-10-3292-9_2 · Cited by 1
An Older Woman with Progressive Muscle Weakness
Bertorini, T. E. (2008) · Neuromuscular Case Studies · doi:10.1016/b978-0-7506-7332-7.50101-x
(2006) · Current Opinion in Rheumatology · doi:10.1097/bor.0b013e328010f1cd
Lembersky, D. (2009) · VCU Scholars Compass (Virginia Commonwealth University) · doi:10.25772/wskn-jt96
Askanas, V., Engel, W. K., & Wojcik, S. P. (2005) · Aktualności Neurologiczne
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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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