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rdf:type |
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lifeskim:mentions |
umls-concept:C0002395,
umls-concept:C0017262,
umls-concept:C0030685,
umls-concept:C0038435,
umls-concept:C0078939,
umls-concept:C0085403,
umls-concept:C0205263,
umls-concept:C0332294,
umls-concept:C0391871,
umls-concept:C0521390,
umls-concept:C0611285,
umls-concept:C0680255,
umls-concept:C1283071,
umls-concept:C1333196,
umls-concept:C1720655,
umls-concept:C1947974,
umls-concept:C1963578,
umls-concept:C2700455
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pubmed:issue |
7
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pubmed:dateCreated |
1995-12-28
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pubmed:abstractText |
Paired helical filament (PHF) tau is the principal component of neurofibrillary tangles, a characteristic feature of the neurodegenerative pathology in Alzheimer's disease (AD). Post-translational modification of tau, especially phosphorylation, has been considered a major factor in aggregation and diminished microtubule interactions of PHF-tau. Recently, it has been recognized that PHF-tau is also subject to non-enzymatic glycation, with formation of advanced glycation end products (AGEs). We now show that as a consequence of glycation, PHF-tau from AD and AGE-tau generate oxygen free radicals, thereby activating transcription via nuclear factor-kappa B, increasing amyloid beta-protein precursor and release of approximately 4 kD amyloid beta-peptides. These data provide insight into how PHF-tau disturbs neuronal function, and add to a growing body of evidence that oxidant stress contributes to the pathogenesis of AD.
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pubmed:grant |
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pubmed:language |
eng
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pubmed:journal |
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pubmed:citationSubset |
IM
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pubmed:chemical |
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pubmed:status |
MEDLINE
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pubmed:month |
Jul
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pubmed:issn |
1078-8956
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pubmed:author |
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pubmed:issnType |
Print
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pubmed:volume |
1
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pubmed:owner |
NLM
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pubmed:authorsComplete |
N
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pubmed:pagination |
693-9
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pubmed:dateRevised |
2007-11-14
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pubmed:meshHeading |
pubmed-meshheading:7585153-Alzheimer Disease,
pubmed-meshheading:7585153-Amyloid beta-Protein Precursor,
pubmed-meshheading:7585153-Animals,
pubmed-meshheading:7585153-Animals, Newborn,
pubmed-meshheading:7585153-Cerebral Cortex,
pubmed-meshheading:7585153-Cytochrome c Group,
pubmed-meshheading:7585153-Feedback,
pubmed-meshheading:7585153-Gene Expression Regulation,
pubmed-meshheading:7585153-Glycosylation,
pubmed-meshheading:7585153-Humans,
pubmed-meshheading:7585153-Interleukin-6,
pubmed-meshheading:7585153-Neuroblastoma,
pubmed-meshheading:7585153-Oxidative Stress,
pubmed-meshheading:7585153-Protein Processing, Post-Translational,
pubmed-meshheading:7585153-Rats,
pubmed-meshheading:7585153-Reactive Oxygen Species,
pubmed-meshheading:7585153-Superoxide Dismutase,
pubmed-meshheading:7585153-Temporal Lobe,
pubmed-meshheading:7585153-Transfection,
pubmed-meshheading:7585153-Tumor Cells, Cultured,
pubmed-meshheading:7585153-tau Proteins
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pubmed:year |
1995
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pubmed:articleTitle |
Non-enzymatically glycated tau in Alzheimer's disease induces neuronal oxidant stress resulting in cytokine gene expression and release of amyloid beta-peptide.
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pubmed:affiliation |
Department of Physiology, Columbia University, College of Physicians and Surgeons, New York, New York 10032, USA.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.,
Research Support, Non-U.S. Gov't
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