期刊
FEBS LETTERS
卷 512, 期 1-3, 页码 101-106出版社
ELSEVIER SCIENCE BV
DOI: 10.1016/S0014-5793(02)02228-7
关键词
tau; glycosylation; phosphorylation; Alzheimer's disease; neurofibrillary degeneration; lectin
资金
- NCRR NIH HHS [2-P41-RR05351-06] Funding Source: Medline
- NIA NIH HHS [AG08076, AG16760, AG05892] Funding Source: Medline
- NIMH NIH HHS [MH/NS 31862] Funding Source: Medline
- NINDS NIH HHS [NS18105] Funding Source: Medline
In Alzheimer's disease (AD) brain, microtubule-associated protein tau is abnormally modified by hyperphosphorylation and glycosylation, and is aggregated as neurofibrillary tangles of paired helical filaments. To investigate the role of tau glycosylation in neurofibrillary pathology, we isolated various pools of tau protein from AD brain which represent different stages of tau pathology. We found that the nonhyperphosphorylated tau from AD brain but not normal brain tau was glycosylated. Monosaccharide composition analyses and specific lectin blots suggested that the tau in AD brain was glycosylated mainly through N-linkage. In vitro phosphorylation indicated that the glycosylated tau was a better substrate for cAMP-dependent protein kinase than the deglycosylated tau. These results suggest that the glycosylation of tau is an early abnormality that can facilitate the subsequent abnormal hyperphosphorylation of tau in AD brain. (C) 2002 Federation of European Biochemical Societies. Published by Elsevier Science B.V. All rights reserved.
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