Abstract:
: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 non-hyperphosphorylated 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.
journal_name
FEBS Lettjournal_title
FEBS lettersauthors
Liu F,Zaidi T,Iqbal K,Grundke-Iqbal I,Merkle RK,Gong CXdoi
10.1016/s0014-5793(02)02228-7keywords:
subject
Has Abstractpub_date
2002-02-13 00:00:00pages
101-6issue
1-3eissn
0014-5793issn
1873-3468pii
S0014579302022287journal_volume
512pub_type
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