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

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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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<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

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