ADVANCED GLYCATION ENDPRODUCTS ARE ASSOCIATED WITH HIRANO BODIES IN ALZHEIMERS-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 b eta-amyloid plaques are 'advanced glycation endproducts' (AGE). Using a polyclonal antibody against AGE in frozen sections of fixed brain ti ssue from Alzheimer's disease patients, AGE were identified in a furth er characteristic protein deposit in AD, namely in Hirano bodies. AGE are localized to ovoid, spherical, and rod-like Hirano bodies in the h ippocampus, particularly numerous in the stratum lacunosum-moleculare of CA1. Since Hirano bodies are known to contain mainly cytoskeletal a nd cytoplasmic components and are localized within the soma of neurons our study suggests that AGE formation and intracellular protein cross linking represent early stages during neuronal degeneration. (C) 1998 Elsevier Science B,V. All rights reserved.