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

W. ‐K Liu, W. T. Moore, R. T. Williams, F. L. Hall, Shu‐Hui ‐H Yen

Research output: Contribution to journalArticlepeer-review

59 Scopus citations

Abstract

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/p58cyclin A proline directed kinase (PDPK), but not by purified mitogen activated protein kinase (p42mapk). 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. © 1993 Wiley‐Liss, Inc.

Original languageEnglish (US)
Pages (from-to)371-376
Number of pages6
JournalJournal of Neuroscience Research
Volume34
Issue number3
DOIs
StatePublished - Feb 15 1993

ASJC Scopus subject areas

  • Cellular and Molecular Neuroscience

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