The DOI matches its Crossref record; 35 of the 35 references it cites were found in a registry or an index.
p62 positive, TDP-43 negative, neuronal cytoplasmic and intranuclear inclusions in the cerebellum and hippocampus define the pathology of C9orf72-linked FTLD and MND/ALS
Open accessAbstract
Neuronal cytoplasmic inclusions (NCIs) containing phosphorylated TDP-43 (p-TDP-43) are the pathological hallmarks of motor neuron disease/amyotrophic lateral sclerosis (MND/ALS) and FTLD-TDP. The vast majority of NCIs in the brain and spinal cord also label for ubiquitin and p62, however, we have previously reported a subset of TDP-43 proteinopathy patients who have unusual and abundant p62 positive, TDP-43 negative inclusions in the cerebellum and hippocampus. Here we sought to determine whether these cases carry the hexanucleotide repeat expansion in C9orf72. Repeat primer PCR was performed in 36 MND/ALS, FTLD-MND/ALS and FTLD-TDP cases and four controls. Fourteen individuals with the repeat expansion were detected. In all the 14 expansion mutation cases there were abundant globular and star-shaped p62 positive NCIs in the pyramidal cell layer of the hippocampus, the vast majority of which were p-TDP-43 negative. p62 positive NCIs were also abundant in the cerebellar granular and molecular layers in all cases and in Purkinje cells in 12/14 cases but they were only positive for p-TDP-43 in the granular layer of one case. Abundant p62 positive, p-TDP-43 negative neuronal intranuclear inclusions (NIIs) were seen in 12/14 cases in the pyramidal cell layer of the hippocampus and in 6/14 cases in the cerebellar granular layer. This unusual combination of inclusions appears pathognomonic for C9orf72 repeat expansion positive MND/ALS and FTLD-TDP which we believe form a pathologically distinct subset of TDP-43 proteinopathies. Our results suggest that proteins other than TDP-43 are binding p62 and aggregating in response to the mutation which may play a mechanistic role in neurodegeneration.
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“This finding is broadly consistent with a connection between TDP-43 pathology and retrotransposon activation because such proteinopathy is commonly observed in C9orf72 familial ALS”
From The Role of Retrotransposons and Endogenous Retroviruses in Age-Dependent Neurodegenerative Disorders (2024) · cites this paper as Al-Sarraj et al. 2011
In the citing paper
“In the most commonly inherited form of ALS and FTD due to mutations in the C9orf72 gene (described below), SQSTM1 accumulates together with ubiquitin in neurons and glia [119–121] as well as muscle fibers [122].”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [119]
In the citing paper
“Antibodies specific for each dipeptide repeat (DPR) also stain SQSTM1-positive inclusions, including the star-like inclusions unique to C9orf72-related disease, suggesting that DPRs are targeted for clearance by the UPS and/or autophagy [119,169–171] (Figure 1).”
From Autophagy and ALS: mechanistic insights and therapeutic implications (2022) · cites this paper as [119]
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Metadata
- Authors
- Al-Sarraj, S., King, A., Troakes, C., Smith, B., Maekawa, S., Bodi, I., Rogelj, B., Al-Chalabi, A., Hortobágyi, T., & Shaw, C. E.
- Affiliations
- King's College London (GB)
- Corresponding author
- King, Andrew
- Venue
- Acta Neuropathologica
- Published
- 2011-11-19
- Volume
- 122
- Issue
- 6
- Pages
- 691-702
- ISSN
- 0001-6322 (ISSN-L)
- 1432-0533
- OpenAlex
- W2066002405
- Cited by
- 475
- References
- 35
- Citations by year
- 2026: 9 · 2025: 9 · 2024: 22 · 2023: 24 · 2022: 23 · 2021: 23 · 2020: 40 · 2019: 27 · 2018: 24 · 2017: 39 · 2016: 38 · 2015: 41 · 2014: 42 · 2013: 63 · 2012: 45
- FWCI
- 31.22
- Type
- journal article
- Language
- en
- Open access
- green
- hdl.handle.net
- Licence
- other-oa
- www.springer.com/tdm (tdm)
- Locations
- Acta Neuropathologica (publishedVersion)
- PubMed (publishedVersion)
- University of Debrecen Electronic Archive (University of Debrecen) (submittedVersion, other-oa)
- Research Portal (King's College London) (submittedVersion)
- Funders
- Wellcome Trust (089701)
- Medical Research Council (MC_G1000733)
- Topics
- Health Sciences › Medicine › Clinical Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Genetic Neurodegenerative Diseases
- Life Sciences › Neuroscience › Cellular and Molecular Neuroscience › Alzheimer's disease research and treatments
- Keywords
- p62, TDP-43, C9orf72, hexanucleotide repeat expansion, amyotrophic lateral sclerosis, motor neuron disease, frontotemporal lobar degeneration, FTLD-TDP, neuronal cytoplasmic inclusions, neuronal intranuclear inclusions, cerebellum, hippocampus, Purkinje cells, neurodegeneration, protein aggregation
- MeSH terms
- Sequestosome-1 Protein, C9orf72 Protein, Adult, Aged, Aged, 80 and over, Amyotrophic Lateral Sclerosis, Inclusion Bodies, Cerebellum, DNA, DNA-Binding Proteins, Female, Hippocampus, Humans, Male, Middle Aged, Mutation, Neurons, Proteins, Purkinje Cells, Case-Control Studies, Pyramidal Cells, DNA Repeat Expansion, Intranuclear Inclusion Bodies, Adaptor Proteins, Signal Transducing, Frontotemporal Lobar Degeneration
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