Accumulation of Triosephosphate Isomerase, with Sequence Homology to β Amyloid Peptides, in Vessel Walls of the Newborn Piglet Hippocampus
✍ Scribed by 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
- Publisher
- John Wiley and Sons
- Year
- 2007
- Tongue
- English
- Weight
- 690 KB
- Volume
- 70
- Category
- Article
- ISSN
- 1059-910X
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✦ Synopsis
Abstract
We investigated whether β‐amyloid (Aβ)‐like immunoreactivity was seen in the brains of newborn piglets. The immunoreactivity for Aβ(1‐42) and Aβ(1–40) proteins, but not Aβ 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‐α. The protein with a molecular mass of 27 kDa, which was recognized by the Aβ antibodies, was identified as triosephosphate isomerase (TPI) with sequence homology to Aβ 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 Aβ proteins were not seen in the piglet brains. These findings indicate that TPI with sequence homology to Aβ peptides accumulates in perivascular cells of the microglia/macrophage lineage located around arterial vessels of the newborn piglet hippocampus. Microsc. Res. Tech., 2007. © 2007 Wiley‐Liss, Inc.