Premium
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
Author(s) -
Liu W.K.,
Moore W. T.,
Williams R. T.,
Hall F. L.,
Yen ShuHui
Publication year - 1993
Publication title -
journal of neuroscience research
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.72
H-Index - 160
eISSN - 1097-4547
pISSN - 0360-4012
DOI - 10.1002/jnr.490340315
Subject(s) - epitope , phosphorylation , kinase , cyclin dependent kinase 1 , antibody , serine , biochemistry , tau protein , alzheimer's disease , biology , protein kinase a , chemistry , microbiology and biotechnology , disease , medicine , genetics , gene , cell cycle , pathology
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 p34 cdc2 /p58 cyclin A proline directed kinase (PDPK), but not by purified mitogen activated protein kinase (p42 mapk ). 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.