Advanced glycation endproducts are associated with Hirano bodies in Alzheimer's disease.
One of the structural posttranslational modifications contributing to the formation of insoluble, and protease-resistant protein deposits in Alzheimer's disease (AD), such as neurofibrillary tangles (NFT) and beta-amyloid plaques are 'advanced glycation endproducts' (AGE). Using a polyclonal antibody against AGE in frozen sections of fixed brain tissue from Alzheimer's disease patients, AGE were identified in a further characteristic protein deposit in AD, namely in Hirano bodies. AGE are localized to ovoid, spherical, and rod-like Hirano bodies in the hippocampus, particularly numerous in the stratum lacunosum-moleculare of CA1. Since Hirano bodies are known to contain mainly cytoskeletal and cytoplasmic components and are localized within the soma of neurons our study suggests that AGE formation and intracellular protein crosslinking represent early stages during neuronal degeneration.
Münch
G
G
Biocenter of the University, Würzburg, Germany.
Cunningham
A M
AM
Riederer
P
P
Braak
E
E
D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D002102:Cadaver; D017127:Glycation End Products, Advanced / Q000378:metabolism*; D006624:Hippocampus / Q000378:metabolism / Q000473:pathology; D006801:Humans; D007158:Immunologic Techniques; D002479:Inclusion Bodies / Q000378:metabolism* / Q000648:ultrastructure; D009474:Neurons / Q000378:metabolism* / Q000648:ultrastructure
D017127:Glycation End Products, Advanced