ADVANCED GLYCATION END-PRODUCTS IN ALZHEIMERS-DISEASE AND OTHER NEURODEGENERATIVE DISEASES

Citation
N. Sasaki et al., ADVANCED GLYCATION END-PRODUCTS IN ALZHEIMERS-DISEASE AND OTHER NEURODEGENERATIVE DISEASES, The American journal of pathology, 153(4), 1998, pp. 1149-1155
Citations number
32
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Pathology
ISSN journal
0002-9440
Volume
153
Issue
4
Year of publication
1998
Pages
1149 - 1155
Database
ISI
SICI code
0002-9440(1998)153:4<1149:AGEIAA>2.0.ZU;2-R
Abstract
Advanced glycation end products (AGEs) have been implicated in the chr onic complications of diabetes mellitus and have been reported to play an important role in the pathogenesis of Alzheimer's disease. In this study, we examined the immunohistochemical localization of AGEs, amyl oid beta protein (A beta), apolipoprotein E (ApoE), and tau protein in senile plaques, neurofibrillary tangles (NFTs), and cerebral amyloid angiopathy (CAA) in Alzheimer's disease and other neurodegenerative di seases (progressive supranuclear palsy, Pick's disease, and Guamanian amyotrophic lateral sclerosis/Parkinsonism-dementia complex). In most senile plaques (including diffuse plaques) and CAA from Alzheimer's br ains, AGE and ApoE were observed together. However, approximately 5% o f plaques were AGE positive but AP negative, and the vessels without C AA often showed AGE immunoreactivity, In Alzheimer's disease, AGEs wer e mainly present in intracellular NFTs, whereas ApoE was mainly presen t in extracellular NFTs, Pick's bodies in Pick's disease and granulova cuolar degeneration in various neurodegenerative diseases were also AG E positive. In non-Alzheimer neurodegenerative diseases, senile plaque s and NFTs showed similar findings to those in Alzheimer's disease. Th ese results suggest that AGE may contribute to eventual neuronal dysfu nction and death as an important factor in the progression of various neurodegenerative diseases, including Alzheimer's disease.