Spatial relationship of AMY protein deposits and different species of Abeta peptides in amyloid plaques of the Alzheimer disease brain.
To further define the spatial relationship of "AMY" plaques detected by antibodies to an unidentified 100 kD AMY protein and amyloid plaques in Alzheimer disease (AD) brains, double immunofluorescence studies were performed with an anti-AMY antibody and a panel of antibodies to different species of Abeta peptides. We report substantial colocalization of AMY immunoreactive plaques with amyloid plaques labeled by antibodies to species of Abeta starting at position 3 with a pyroglutamate modified glutamic acid, however AMY immunoreactive deposits colocalized to a lesser degree with amyloid plaques labeled by antibodies to other variants of the Abeta peptide. Moreover, different immunohistochemical parameters influenced the extent to which colocalization of AMY deposits and Abeta immunoreactive plaques was demonstrable. We conclude that deposits of distinct species of Abeta peptides differentially colocalize with one another and with AMY plaques in the AD brain.
Schmidt
M L
ML
Center for Neurodegenerative Disease Research, Department of Pathology and Laboratory Medicine, University of Pennsylvania School of Medicine, Philadelphia 19104-4283, USA.
Saido
T C
TC
Lee
V M
VM
Trojanowski
J Q
JQ
D000368:Aged; D000544:Alzheimer Disease / Q000378:metabolism*; D016229:Amyloid beta-Peptides / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D006801:Humans; D008875:Middle Aged; D010446:Peptide Fragments / Q000378:metabolism*; D058225:Plaque, Amyloid / Q000378:metabolism*; D014018:Tissue Distribution
D016229:Amyloid beta-Peptides; D010446:Peptide Fragments