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Proceedings of the National Academy of Sciences, Vol 91, 7787-7791, Copyright © 1994 by National Academy of Sciences
S Yan, X Chen, A Schmidt, J Brett, G Godman, Y Zou, CW Scott, C Caputo, T Frappier, MA Smith, G Perry, S Yen and D Stern
The stability of proteins that constitute the neurofibrillary tangles and
senile plaques of Alzheimer disease suggests that they would be ideal
substrates for nonenzymatic glycation, a process that occurs over long
times, even at normal levels of glucose, ultimately resulting in the
formation of advanced glycation end products (AGEs). AGE-modified proteins
aggregate, and they generate reactive oxygen intermediates. Using
monospecific antibody to AGEs, we have colocalized these AGEs with paired
helical filament tau in neurofibrillary tangles in sporadic Alzheimer
disease. Such neurons also exhibited evidence of oxidant stress: induction
of malondialdehyde epitopes and heme oxygenase 1 antigen. AGE-recombinant
tau generated reactive oxygen intermediates and, when introduced into the
cytoplasm of SH-SY5Y neuroblastoma cells, induced oxidant stress. We
propose that in Alzheimer disease, AGEs in paired helical filament tau can
induce oxidant stress, thereby promoting neuronal dysfunction.
ARTICLE
Glycated Tau Protein in Alzheimer Disease: A Mechanism for Induction of Oxidant Stress
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