Advanced glycation endproducts are associated with Hirano bodies in Alzheimer's disease

• Published in: Brain research 1998-06, Vol.796 (1), p.307-310
• Main Authors: Münch, Gerald, Cunningham, Anne M, Riederer, Peter, Braak, Eva
• Format: Article
• Language: English
• Subjects: Advanced glycation endproduct; Alzheimer Disease - metabolism; Alzheimer Disease - pathology; Alzheimer's disease; Biological and medical sciences; Cadaver; Crosslinking; Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases; Glycation End Products, Advanced - metabolism; Hippocampus - metabolism; Hippocampus - pathology; Hirano body; Humans; Immunologic Techniques; Inclusion Bodies - metabolism; Inclusion Bodies - ultrastructure; Medical sciences; Neurology; Neurons - metabolism; Neurons - ultrastructure; Oxidative stress
• ISSN: 0006-8993; 1872-6240
• DOI: 10.1016/S0006-8993(98)00328-X

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 β-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.