Enhanced Antigen Retrieval of Amyloid β Immunohistochemistry: Re-evaluation of Amyloid β Pathology in Alzheimer Disease and Its Mouse Model

Hideaki Kai, Ryong Woon Shin, Koichi Ogino, Hiroyuki Hatsuta, Shigeo Murayama, Tetsuyuki Kitamoto

Research output: Contribution to journalArticle

16 Citations (Scopus)

Abstract

Senile plaques, extracellular deposits of amyloid β peptide (Aβ), are one of the pathological hallmarks of Alzheimer disease (AD). As the standard immunohistochemical detection method for Aβ deposits, anti-Aβ immunohistochemistry combined with antigen retrieval (AR) by formic acid (FA) has been generally used. Here, we present a more efficient AR for Aβ antigen. On brain sections of AD and its mouse model, a double combination of either autoclave heating in EDTA buffer or digestion with proteinase K plus FA treatment reinforced Aβ immunoreactivity. A further triple combination of digestion with proteinase K (P), autoclave heating in EDTA buffer (A), and FA treatment (F), when employed in this order, gave a more enhanced immunoreactivity. Our PAF method prominently visualized various forms of Aβ deposits in AD that have not been clearly detected previously and revealed numerous minute-sized plaques both in AD and the mouse model. Quantification of Aβ loads showed that the AR effect by the PAF method was 1.86-fold (in the aged human brain) and 4.64-fold (in the mouse brain) higher than that by the FA method. Thus, the PAF method could have the potential to be the most sensitive tool so far to study Aβ pathology in AD and its mouse model.

Original languageEnglish
Pages (from-to)761-769
Number of pages9
JournalJournal of Histochemistry and Cytochemistry
Volume60
Issue number10
DOIs
Publication statusPublished - 2012 Oct

Keywords

  • APP-SL mouse
  • Alzheimer disease
  • PAF method
  • amyloidβ
  • antigen retrieval
  • autoclave heating
  • formic acid
  • immunohistochemistry
  • minute plaque
  • proteinase K

ASJC Scopus subject areas

  • Anatomy
  • Histology

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