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PMID: 8052661 Published · ppublish English Journal Article Research Support, Non-U.S. Gov't Research Support, U.S. Gov't, P.H.S.

Glycated tau protein in Alzheimer disease: a mechanism for induction of oxidant stress.

Proceedings of the National Academy of Sciences of the United States of America ·Vol. 91 ·No. 16 ·1994-08-02 ·Pages 7787-91

Yan SD, Chen X, Schmidt AM, Brett J, Godman G, Zou YS, Scott CW, Caputo C, Frappier T, Smith MA

Abstract

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.

MeSH Terms
Alzheimer Disease/metabolism,pathology Brain/pathology Glycation End Products, Advanced/isolation & purification,metabolism Humans Immunohistochemistry Neuroblastoma/metabolism Neurofibrillary Tangles/ultrastructure Reactive Oxygen Species/metabolism Recombinant Proteins/metabolism Tumor Cells, Cultured tau Proteins/genetics,isolation & purification,metabolism
Chemicals
Glycation End Products, Advanced Reactive Oxygen Species Recombinant Proteins tau Proteins
Authors & Affiliations
10 authors, click to expand affiliations / ORCID
Yan S D
Department of Physiology, Columbia University, College of Physicians and Surgeons, New York, NY 10032.
Chen X
Schmidt A M
Brett J
Godman G
Zou Y S
Scott C W
Caputo C
Frappier T
Smith M A
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Article Info
Journal
Proceedings of the National Academy of Sciences of the United States of America
Abbr.
Proc Natl Acad Sci U S A
ISSN
0027-8424
DOI
10.1073/pnas.91.16.7787
Published
1994-08-02
Pages
7787-91
Language
English
Region
United States
NLM ID
7505876
PMCID
PMC44487
Subset
IM
Grants
NHLBI NIH HHS · HL21006 · United States
NHLBI NIH HHS · HL42507 · United States
NHLBI NIH HHS · HL42833 · United States
External Links
PubMed source DOI: 10.1073/pnas.91.16.7787 PMC Full Text View journal details
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