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
-
- Kasahara Sou
- Department of Neurology, Brain Research Institute, Niigata University
-
- Ishihara Tomohiko
- Department of Neurology, Brain Research Institute, Niigata University
-
- Koike Yuka
- Department of Neurology, Brain Research Institute, Niigata University
-
- Sugai Akihiro
- Department of Neurology, Brain Research Institute, Niigata University
-
- Onodera Osamu
- Department of Neurology, Brain Research Institute, Niigata University
Bibliographic Information
- Other Title
-
- 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
Search this article
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
-
- Rinsho Shinkeigaku
-
Rinsho Shinkeigaku 60 (2), 109-116, 2020
Societas Neurologica Japonica