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Serine 403-phosphorylated p62/SQSTM1 immunoreactivity in inclusions of neurodegenerative diseases.
Kurosawa, Masaru; Matsumoto, Gen; Sumikura, Hiroyuki; Hatsuta, Hiroyuki; Murayama, Shigeo; Sakurai, Takashi; Shimogori, Tomomi; Hattori, Nobutaka; Nukina, Nobuyuki.
Affiliation
  • Kurosawa M; Laboratory for Structural Neuropathology, RIKEN Brain Science Institute, Saitama 351-0198, Japan; Laboratory for Molecular Mechanisms of Thalamus Development, RIKEN Brain Science Institute, Saitama 351-0198, Japan; Department of Cellular and Molecular Pharmacology, Juntendo University Graduate Schoo
  • Matsumoto G; Department of Neuroscience for Neurodegenerative Disorders, Juntendo University Graduate School of Medicine, Tokyo 113-8421, Japan; Laboratory for Structural Neuropathology, RIKEN Brain Science Institute, Saitama 351-0198, Japan; Laboratory for Molecular Mechanisms of Thalamus Development, RIKEN Bra
  • Sumikura H; Department of Neurology & Neuropathology, Tokyo Metropolitan Geriatric Hospital & Institute of Gerontology, Tokyo 173-0015, Japan.
  • Hatsuta H; Department of Neurology & Neuropathology, Tokyo Metropolitan Geriatric Hospital & Institute of Gerontology, Tokyo 173-0015, Japan.
  • Murayama S; Department of Neurology & Neuropathology, Tokyo Metropolitan Geriatric Hospital & Institute of Gerontology, Tokyo 173-0015, Japan.
  • Sakurai T; Department of Cellular and Molecular Pharmacology, Juntendo University Graduate School of Medicine, Tokyo 113-8421, Japan.
  • Shimogori T; Laboratory for Molecular Mechanisms of Thalamus Development, RIKEN Brain Science Institute, Saitama 351-0198, Japan.
  • Hattori N; Department of Neurology, Juntendo University Graduate School of Medicine, Tokyo 113-8421, Japan.
  • Nukina N; Department of Neuroscience for Neurodegenerative Disorders, Juntendo University Graduate School of Medicine, Tokyo 113-8421, Japan; Laboratory for Structural Neuropathology, RIKEN Brain Science Institute, Saitama 351-0198, Japan; Laboratory for Molecular Mechanisms of Thalamus Development, RIKEN Bra
Neurosci Res ; 103: 64-70, 2016 Feb.
Article in En | MEDLINE | ID: mdl-26302676
ABSTRACT
Protein inclusions in neurodegenerative diseases are associated with p62, which has an important role in autophagic clearance of polyubiquitinated proteins. Selective autophagy is regulated by S403-phosphorylation of p62, and S403-phosphorylated p62 (S403-phos-p62) accumulates in Atg5 conditional knockout (Atg5CKO) mice in which autophagosome formation is impaired. We performed immunohistochemical tests for the presence of S403-phos-p62 in postmortem brain of neurodegenerative disease cases, and found accumulations in amyotrophic lateral sclerosis and Alzheimer's disease tissues. In Atg5CKO and HD190QG (Huntington's disease model) mice, however, we found a postmortem decrease in S403-phos-p62 immunoreactivity, suggesting that post-mortem changes should be considered when interpreting human data.
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Huntington Disease / Intranuclear Inclusion Bodies / Adaptor Proteins, Signal Transducing / Alzheimer Disease / Heat-Shock Proteins / Amyotrophic Lateral Sclerosis Limits: Aged / Aged80 / Animals / Humans / Middle aged Language: En Journal: Neurosci Res Journal subject: NEUROLOGIA Year: 2016 Document type: Article
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Full text: 1 Collection: 01-internacional Database: MEDLINE Main subject: Huntington Disease / Intranuclear Inclusion Bodies / Adaptor Proteins, Signal Transducing / Alzheimer Disease / Heat-Shock Proteins / Amyotrophic Lateral Sclerosis Limits: Aged / Aged80 / Animals / Humans / Middle aged Language: En Journal: Neurosci Res Journal subject: NEUROLOGIA Year: 2016 Document type: Article