Premium
Immunohistochemical study with anti‐advanced glycation end‐products antibody in murine amyloidosis
Author(s) -
Hoshii Yoshinobu,
Kawano Hiroo,
Gondo Toshikazu,
Takahashi Mutsuo,
Ishihara Tokuhiro,
Higuchi Keiichi,
Hotiuchi Seikoh
Publication year - 1996
Publication title -
pathology international
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.73
H-Index - 74
eISSN - 1440-1827
pISSN - 1320-5463
DOI - 10.1111/j.1440-1827.1996.tb03542.x
Subject(s) - immunohistochemistry , pathology , amyloidosis , glycation , antibody , medicine , immunology , receptor
Advanced glycation end‐products (AGE) are formed In the late phase of the non‐enzymatic glycosylation reaction in conditions such as diabetes mellitus and aging. In amyloidosb, AGE have been twnd In the Aβ2M amyldd associated with long‐term hemodlalysls and in the β‐protein in Alzheimer's disease. Murine AApoAll and AA amyloidosls were examined lmmunohistochemically using anti‐AGE monodonal antibody, 6D12. AApoAll amyloid deposits studied in one smeaconm‐accelerated mouse P1 (SAMP1), congenic mice that have the amyloldogenic apollpoprotein A‐ll of SAMP1 mice, and AKR mice all reacted with blotinylated 6D12 by formic acid pretreatment, whereas AA amyloid deposits did not react with the antibody. The immunoreaction wlth anti‐apollpoprotein A‐II for amyloid deposits in senile mice was approximately homogeneous in intensity; on the other hand the reaction with biotinylated 6D12 was irregular in distribution and intensity over the amyloid deposits. These findings suggest that amyloid precursor proteins are not associated uniformly with AGE modification before deposition as amyloid; it Is more likely that the AGE modification progresses gradually and unevenly after amyloid deposition. Murine amyloldosis may be a useful model to elucidate the role of AGE in amyloidosis.