MISC

2007年7月

Accumulation of triosephosphate isomerase, with sequence homology to beta amyloid peptides, in vessel walls of the newborn piglet hippocampus

MICROSCOPY RESEARCH AND TECHNIQUE
  • Takashi Kusaka
  • Masaki Ueno
  • Takanori Miki
  • Kenji Kanenishi
  • Yukiko Nagai
  • Cheng-Long Huang
  • Yasuo Okamoto
  • Takafumi Ogawa
  • Masayuki Onodera
  • Susumu Itoh
  • Ichiro Akiguchi
  • Haruhiko Sakamoto
  • 全て表示

70
7
開始ページ
648
終了ページ
655
記述言語
英語
掲載種別
DOI
10.1002/jemt.20448
出版者・発行元
WILEY-LISS

We investigated whether beta-amyloid (A beta)-like immunoreactivity was seen in the brains of newborn piglets. The immunoreactivity for A beta(1-42) and A beta(1-40) proteins, but not A beta precursor protein, was present in CD68-positive perivascular cells of the hippocampus and in parts of the meninges. It was colocalized with immunoreactivity for receptor for advanced glycation end product and tumor necrosis factor-alpha. The protein with a molecular mass of 27 kDa, which was recognized by the A beta antibodies, was identified as triosephosphate isomerase (TPI) with sequence homology to A beta peptides by N-terminal amino acid sequencing, mass fingerprint analysis using matrix-associated laser desorption/ionization mass spectrometry, and Western blotting. Western blotting assay also revealed that detectable expression of A beta proteins were not seen in the piglet brains. These findings indicate that TPI with sequence homology to A beta peptides accumulates in perivascular cells of the microglia/macrophage lineage located around arterial vessels of the newborn piglet hippocampus.

リンク情報
DOI
https://doi.org/10.1002/jemt.20448
Web of Science
https://gateway.webofknowledge.com/gateway/Gateway.cgi?GWVersion=2&SrcAuth=JSTA_CEL&SrcApp=J_Gate_JST&DestLinkType=FullRecord&KeyUT=WOS:000247864500013&DestApp=WOS_CPL
ID情報
  • DOI : 10.1002/jemt.20448
  • ISSN : 1059-910X
  • Web of Science ID : WOS:000247864500013

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