Immunolocalization of Smurf1 in Hirano bodies
Abstract
The Smad ubiquitination regulatory factor 1 (Smurf1) is one of the E3 ubiquitin ligases and is related to multiple biological processes. Despite the various roles played by this protein, there is no report on the function of Smurf1 in neurodegeneration. Hirano bodies (HBs) are intracellular structures within neuronal processes and were first described in the hippocampus of individuals with amyotrophic lateral sclerosis and the parkinsonism-dementia complex of Guam. In addition, the number of HBs increases in the brains of patients with Alzheimer's disease (AD) compared with age-matched non-demented control individuals. In this study, we immunohistochemically demonstrated that Smurf1 localized in HBs in the brains of patients with AD by using plural anti-Smurf1 antibodies, and Smurf1 co-localized with HBs marker proteins by using confocal microscopy. Moreover, we demonstrated that Smurf1 localized in HB-like F-actin aggregates in a cell culture system via treatment with the actin-stabilizing toxin jasplakinolide (jpk). Smurf1 represents a novel protein component of HBs, to be included in an expanding list of HB-associated proteins.
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Actin-rich paracrystalline inclusions, so-called Hirano bodies, are found in brain histopathological samples of Alzheimer's disease and related tauopathies.
“In agreement with the disease relevance of the Tau/actin interaction, actin-rich paracrystalline inclusions, so-called Hirano bodies, are found in brain histopathological samples of AD and related tauopathies24, 25.”
From Multivalent cross-linking of actin filaments and microtubules through the microtubule-associated protein Tau (2017) · cites this paper as [25]
Cites
Numbers of Hirano bodies in the hippocampus of normal and demented people with Alzheimer's disease
Gibson, P. H., & Tomlinson, B. E. (1977) · Journal of the Neurological Sciences · doi:10.1016/0022-510x(77)90193-9 · Cited by 118 · see citing works
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Cabrales Fontela, Y., Kadavath, H., Biernat, J., Riedel, D., Mandelkow, E., & Zweckstetter, M. (2017) · Nature Communications · doi:10.1038/s41467-017-02230-8 · Cited by 148 · see citing works
- Authors
- Makioka, K., Yamazaki, T., Takatama, M., Ikeda, M., & Okamoto, K.
- Affiliations
- Gunma University (JP)
- ORCID
- Okamoto, Koichi
- Venue
- Journal of the Neurological Sciences
- Publisher
- Elsevier BV
- Published
- 2014-01
- Volume
- 336
- Issue
- 1-2
- Pages
- 24-28
- ISSN
- 0022-510X (ISSN-L)
- OpenAlex
- W2163401136
- Cited by
- 14
- References
- 1
- Citations by year
- 2025: 1 · 2024: 2 · 2022: 3 · 2021: 1 · 2020: 1 · 2019: 1 · 2018: 1 · 2017: 1 · 2016: 1 · 2015: 2
- FWCI
- 0.69
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Journal of the Neurological Sciences (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Ministry of Education, Culture, Sports, Science and Technology
- Ministry of Health, Labour and Welfare
- Topics
- Health Sciences › Medicine › Physiology › Alzheimer's disease research and treatments
- Health Sciences › Medicine › Neurology › Amyotrophic Lateral Sclerosis Research
- Life Sciences › Neuroscience › Neurology › Neuroinflammation and Neurodegeneration Mechanisms
- Keywords
- Smurf1, Hirano bodies, Alzheimer's disease, E3 ubiquitin ligase, neurodegeneration, jasplakinolide, amyotrophic lateral sclerosis, parkinsonism-dementia complex of Guam, protein colocalization
- MeSH terms
- Aged, Aged, 80 and over, Alzheimer Disease, Inclusion Bodies, Female, HeLa Cells, Hippocampus, Humans, Male, Middle Aged, Ubiquitin-Protein Ligases
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