Are advanced glycation end-products associated with amyloidosis in Alzheimer's disease?
Recent studies have suggested that advanced glycation end-products (AGE) of the Maillard reaction are associated with amyloidosis in Alzheimer's disease. To evaluate this possibility, the present immunohistochemical study was undertaken to locate AGE in cerebral cortices of Alzheimer's disease, using a monoclonal antibody specific for AGE-proteins. Deposits of beta-amyloid protein within cores of classic senile plaques and vascular walls in amyloid angiopathy showed no AGE-positive reaction, while primitive plaques, coronas of classic plaques and some glial cells were positive for AGE. These findings are inconsistent with the suggestion that AGE may be involved primarily in amyloidosis in Alzheimer's disease.
Kimura
T
T
Division of Clinical Research, National Kikuchi Hospital, Kumamoto, Japan.
Takamatsu
J
J
Araki
N
N
Goto
M
M
Kondo
A
A
Miyakawa
T
T
Horiuchi
S
S
D000368:Aged; D000369:Aged, 80 and over; D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D000686:Amyloidosis / Q000378:metabolism* / Q000473:pathology; D000911:Antibodies, Monoclonal; D001921:Brain / Q000473:pathology*; D001923:Brain Chemistry / Q000502:physiology*; D005947:Glucose / Q000378:metabolism*; D006624:Hippocampus / Q000378:metabolism / Q000473:pathology; D006801:Humans; D007150:Immunohistochemistry
D000911:Antibodies, Monoclonal; D005947:Glucose