| Literature DB >> 26302676 |
Masaru Kurosawa1, Gen Matsumoto2, Hiroyuki Sumikura3, Hiroyuki Hatsuta3, Shigeo Murayama3, Takashi Sakurai4, Tomomi Shimogori5, Nobutaka Hattori6, Nobuyuki Nukina7.
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.Entities:
Keywords: Alzheimer's disease; Amyotrophic lateral sclerosis; Dephosphorylation; Postmortem change; Protein degradation; Selective autophagy
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Year: 2015 PMID： 26302676 DOI： 10.1016/j.neures.2015.08.002
Source DB: PubMed Journal: Neurosci Res ISSN： 0168-0102 Impact factor: 3.304