Premium
Monoclonal antibody PHF‐1 recognizes tau protein phosphorylated at serine residues 396 and 404
Author(s) -
Otvos L.,
Feiner L.,
Lang E.,
Szendrei G. I.,
Goedert M.,
Lee V. MY.
Publication year - 1994
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.490390607
Subject(s) - chinese hamster ovary cell , phosphorylation , monoclonal antibody , serine , chemistry , epitope , microbiology and biotechnology , tau protein , biochemistry , antibody , biology , alzheimer's disease , receptor , immunology , medicine , pathology , disease
The microtubule‐associated protein τ is hyperphosphorylated in the paired helical filaments (PHFs) of Alzheimer's disease. Immunological and direct chemical studies have identified Ser 396 and Ser 404 as two of the phosphorylated sites. Previously, we have demonstrated, using synthetic τ peptides containing phosphorylated Ser 396 , that this site is recognized by the monoclonal antibody PHF‐1. The present sudy extends this observation by showing that PHF‐1 recognizes τ peptides containing either individually phosphorylated Ser 396 or Ser 404 , but that there is a >10‐fold increase in the sensitivity of detection of τ peptides by PHF‐1 when both serines are phosphorylated. The recognition of singly or doubly phosphorylated Ser 396 and Ser 404 in τ by PHF‐1 can also be demonstrated in Chinese hamster ovary cells transfected with full‐length wild‐type τ constructs or mutant constructs with Ala substituted for Ser 396 or Ser 404 . We conclude that the PHF‐1 epitope contains both phosphorylated Ser 396 and Ser 404 . © 1994 Wiley‐Liss, Inc.