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SOD1-interacting proteins: Roles of aggregation cores and protein degradation systems.
Une, Mio; Yamakawa, Miho; Watanabe, Yasuhiro; Uchino, Kazuyuki; Honda, Naoto; Adachi, Mayuka; Nakanishi, Mami; Umezawa, Akihiro; Kawata, Yasushi; Nakashima, Kenji; Hanajima, Ritsuko.
Afiliación
  • Une M; Division of Neurology, Department of Brain and Neurosciences, Faculty of Medicine, Tottori University, Yonago, Japan.
  • Yamakawa M; Division of Neurology, Department of Brain and Neurosciences, Faculty of Medicine, Tottori University, Yonago, Japan.
  • Watanabe Y; Division of Neurology, Department of Brain and Neurosciences, Faculty of Medicine, Tottori University, Yonago, Japan. Electronic address: yawatana@tottori-u.ac.jp.
  • Uchino K; Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, Japan.
  • Honda N; Division of Neurology, Department of Brain and Neurosciences, Faculty of Medicine, Tottori University, Yonago, Japan.
  • Adachi M; Division of Neurology, Department of Brain and Neurosciences, Faculty of Medicine, Tottori University, Yonago, Japan.
  • Nakanishi M; Division of Neurology, Department of Brain and Neurosciences, Faculty of Medicine, Tottori University, Yonago, Japan.
  • Umezawa A; Center for Regenerative Medicine, National Research Institute for Child Health and Development, Tokyo, Japan.
  • Kawata Y; Department of Chemistry and Biotechnology, Graduate School of Engineering, Tottori University, Tottori, Japan.
  • Nakashima K; Department of Neurology, National Hospital Organization, Matsue Medical Center, Matsue, Japan.
  • Hanajima R; Division of Neurology, Department of Brain and Neurosciences, Faculty of Medicine, Tottori University, Yonago, Japan.
Neurosci Res ; 170: 295-305, 2021 Sep.
Article en En | MEDLINE | ID: mdl-32726594
Cu/Zn superoxide dismutase (SOD1) mutations are associated with amyotrophic lateral sclerosis (ALS). SOD1-positive aggregates in motor neurons, as well as proteins that interact with the aggregates are presumably involved in ALS neurotoxicity. We used a proteomics approach to compare differences in protein expression in spinal cord homogenates from non-transgenic (NTG) and ALS model mice. Using the homogenates, we identified proteins that interacted with SOD1 seeds in vitro. We assessed differences in SOD1-interacting proteins in cell cultures treated with proteasome or autophagy inhibitor. In the first experiment, intermediate filamentous and small heat shock proteins were upregulated in glial cells. We identified 26 protein types that interacted with aggregation cores in ALS model homogenates, and unexpectedly, 40 proteins in were detected in NTG mice. In cell cultures treated with proteasome and autophagy inhibitors, we identified 16 and 11 SOD1-interacting proteins, respectively, and seven proteins in untreated cells. These SOD1-interacting proteins were involved in multiple cellular functions such as protein quality control, cytoskeletal organization, and pathways involved in growth factor signaling and their downstream cascades. The complex interactions between pathways could cause further dysregulation, ultimately leading to fatal cellular dysfunction in ALS.
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Superóxido Dismutasa / Esclerosis Amiotrófica Lateral Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Neurosci Res Asunto de la revista: NEUROLOGIA Año: 2021 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Irlanda
Texto completo
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Texto completo: 1 Colección: 01-internacional Base de datos: MEDLINE Asunto principal: Superóxido Dismutasa / Esclerosis Amiotrófica Lateral Tipo de estudio: Prognostic_studies Límite: Animals Idioma: En Revista: Neurosci Res Asunto de la revista: NEUROLOGIA Año: 2021 Tipo del documento: Article País de afiliación: Japón Pais de publicación: Irlanda