Molecular mechanism of amyotrophic lateral sclerosis (ALS) from the viewpoint of the formation and degeneration of transactive response DNA-binding protein 43 kDa (TDP-43) inclusions
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- Kasahara Sou
- Department of Neurology, Brain Research Institute, Niigata University
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- Ishihara Tomohiko
- Department of Neurology, Brain Research Institute, Niigata University
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- Koike Yuka
- Department of Neurology, Brain Research Institute, Niigata University
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- Sugai Akihiro
- Department of Neurology, Brain Research Institute, Niigata University
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- Onodera Osamu
- Department of Neurology, Brain Research Institute, Niigata University
Bibliographic Information
- Other Title
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- Transactive response DNA-binding protein 43 kDa（TDP-43）凝集体の形成と分解からみたamyotrophic lateral sclerosis（ALS）分子機構
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Description
<p>Sporadic amyotrophic lateral sclerosis (SALS) and many cases of familial ALS (FALS) demonstrate cytoplasmic transactive response DNA-binding protein 43 kDa (TDP-43)-positive inclusion bodies. Thus, TDP-43 plays a vital role in ALS pathogenesis. Functional analysis of the ALS causative genes advanced the elucidation of the mechanism associated with the formation and degradation of TDP-43 aggregates. Stress granules, which are non-membranous organelles, are attracting attention as sites of aggregate formation, with involvement of FUS and C9orf72. Concurrently, ALS causative genes related to the ubiquitin-proteasome and autophagy systems, which are aggregate degradation mechanisms, have also been reported. Therefore, therapeutic research based on the molecular pathology common to SALS and FALS has been advanced.</p>
Journal
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- Rinsho Shinkeigaku
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Rinsho Shinkeigaku 60 (2), 109-116, 2020
Societas Neurologica Japonica