Application of synthetic phospho- and unphospho- peptides to identify phosphorylation sites in a subregion of the tau molecule, which is modified in Alzheimer's disease
✍ Scribed by W.-K. Liu; W. T. Moore; R. T. Williams; F. L. Hall; Shu-Hui Yen
- Publisher
- John Wiley and Sons
- Year
- 1993
- Tongue
- English
- Weight
- 582 KB
- Volume
- 34
- Category
- Article
- ISSN
- 0360-4012
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✦ Synopsis
Phospho-and unphospho-peptides were used to define the essential sequence for a tau epitope, which is recognized by Tau-1 antibody and phosphorylated in Alzheimer's disease (AD). The epitope was mapped within the amino acid residues 192-199 of tau and was phosphorylated by the p34cdc2/p58cyc'i" A proline directed kinase (PDPK), but not by purified mitogen activated protein kinase ( ~4 2 ~" ~~) .
Addition of phosphate to the last serine of the epitope was the most effective in abolishing the reactivity of the epitope to Tau-1 antibody. Our results suggest that one and possibly more members of the PDPK family may play a role in the pathogenesis of AD.