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
- 巻
- 70
- 号
- 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
- ID情報
-
- DOI : 10.1002/jemt.20448
- ISSN : 1059-910X
- Web of Science ID : WOS:000247864500013