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Sporadic inclusion body myositis: possible pathogenesis inferred from biomarkers.
Open accessAbstract
PURPOSE OF REVIEW: The relevance of proteins that accumulate and aggregate in the muscle fibers of patients with sporadic inclusion body myositis (sIBM) is unknown. Many of these proteins also aggregate in other disorders, including Alzheimer's disease, leading to speculation that sIBM pathogenesis has similarities to neurodegenerative disorders. Our review will discuss current studies on these protein biomarkers and their utility in sIBM diagnosis. RECENT FINDINGS: Two 'classical' components of sIBM aggregates (amyloid beta and phospho-tau) have been re-evaluated. Three additional components of aggregates (TDP-43, p62, and LC3) have been identified. The sensitivity and specificity of these biomarkers has been explored. Two studies suggest that TDP-43 may have clinical utility in distinguishing sIBM from other inflammatory myopathies. SUMMARY: The fact that sIBM muscle accumulates multiple protein aggregates with no single protein appearing in every sIBM patient biopsy suggests that it is not presently possible to place pathogenic blame on any single protein (i.e. amyloid beta or TDP-43). Instead changes in protein homeostasis may lead to the accumulation of different proteins that have a propensity to aggregate in skeletal muscle. Therapies aimed at improving protein homeostasis, instead of targeting a specific protein that may or may not accumulate in all sIBM patients, could be useful future strategies for this devastating and enigmatic disorder.
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Expression of TDP-43 and FUS/TLS has been observed in muscle biopsy samples from patients with sporadic inclusion body myositis (sIBM).
“The expression of TDP-43 and fused in sarcoma/translocated in liposarcoma (FUS/TLS) has been observed in muscle biopsy samples from patients with sporadic inclusion body myositis (sIBM) (Weihl and Pestronk, 2010; Yamashita et al., 2013).”
From Proteasome dysfunction induces muscle growth defects and protein aggregation (2014) · cites this paper as Weihl and Pestronk, 2010
The Introduction section on TDP-43 reports sarcoplasmic TDP-43 inclusions in sIBM muscle, and the Biomarker specificity section reports TDP-43 in sIBM biopsies. Our copy does not report FUS/TLS expression in those biopsies, so it supports only the TDP-43 part of the claim. (LLM, conf=0.88)
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C URRENT OPINION Inclusion body myositis: update
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Metadata
- Authors
- Weihl, C. C., & Pestronk, A.
- Affiliations
- Washington University in St. Louis (US)
- Corresponding author
- Weihl, Conrad C
- Venue
- Current Opinion in Neurology
- Published
- 2010-10
- Volume
- 23
- Issue
- 5
- Pages
- 482-488
- ISSN
- 1350-7540 (ISSN-L)
- PMC
- PMC3606555
- OpenAlex
- W2077863341
- Cited by
- 51
- References
- 64
- Citations by year
- 2025: 1 · 2023: 1 · 2021: 1 · 2019: 4 · 2018: 3 · 2017: 4 · 2016: 5 · 2015: 7 · 2014: 10 · 2013: 6 · 2012: 6
- FWCI
- 0.55
- Type
- journal article
- Language
- en
- Open access
- green
- www.ncbi.nlm.nih.gov
- Locations
- Current Opinion in Neurology (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institutes of Health
- National Institute on Aging (K08AG026271, R01AG031867)
- Topics
- Health Sciences › Medicine › Rheumatology › Inflammatory Myopathies and Dermatomyositis
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Muscle Physiology and Disorders
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Keywords
- sporadic inclusion body myositis, protein aggregation, protein biomarkers, TDP-43, amyloid-beta, phosphorylated tau, p62, LC3, proteostasis, neurodegeneration, myositis, differential diagnosis, pathogenesis
- MeSH terms
- Humans, Biomarkers, Muscle Fibers, Skeletal, Myositis, Inclusion Body
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