| Article ID | Journal | Published Year | Pages | File Type |
|---|---|---|---|---|
| 6286015 | Neuroscience Research | 2016 | 7 Pages |
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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Authors
Masaru Kurosawa, Gen Matsumoto, Hiroyuki Sumikura, Hiroyuki Hatsuta, Shigeo Murayama, Takashi Sakurai, Tomomi Shimogori, Nobutaka Hattori, Nobuyuki Nukina,