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Role of glycosylation in hyperphosphorylation of tau in Alzheimer's disease
- Source :
- FEBS letters. 512(1-3)
- Publication Year :
- 2002
-
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.
- Subjects :
- Glycosylation
Neurofibrillary degeneration
Tau protein
Biophysics
Hyperphosphorylation
tau Proteins
macromolecular substances
Biochemistry
Acetylglucosamine
03 medical and health sciences
chemistry.chemical_compound
0302 clinical medicine
Structural Biology
Alzheimer Disease
mental disorders
Genetics
Humans
Phosphorylation
Protein kinase A
Molecular Biology
030304 developmental biology
Hexoses
0303 health sciences
biology
Lectin
Neurofibrillary Tangles
Cell Biology
Nucleotidyltransferases
In vitro
N-Acetylneuraminic Acid
Cell biology
Blot
carbohydrates (lipids)
chemistry
biology.protein
lipids (amino acids, peptides, and proteins)
Tau
Alzheimer’s disease
Protein Processing, Post-Translational
030217 neurology & neurosurgery
Subjects
Details
- ISSN :
- 00145793
- Volume :
- 512
- Issue :
- 1-3
- Database :
- OpenAIRE
- Journal :
- FEBS letters
- Accession number :
- edsair.doi.dedup.....ecea1d11f44bbe95be004855909c0044