Binding specificity of monoclonal antibody AD2: influence of the phosphorylation state of tau

Brain Res Mol Brain Res. 2000 May 31;78(1-2):181-5. doi: 10.1016/s0169-328x(00)00073-5.

Abstract

Using recombinant human tau protein phosphorylated by a brain extract and the glycogen synthase kinase-3beta in the absence or the presence of heparin, we showed that phosphorylation-dependent antibody AD2 recognition only requires phosphorylated Ser-396. By the Spot multiple peptide synthesis method, we showed that Tyr-394, Ser(P)-396 and Pro-397 are critical for AD2 binding. A decrease in the binding of AD2 was observed with increasing phosphorylation of residues in the vicinity of Ser(P)-396.

MeSH terms

  • Alzheimer Disease / metabolism
  • Amino Acid Sequence
  • Antibodies, Monoclonal / immunology*
  • Antibody Specificity*
  • Anticoagulants / pharmacology
  • Brain Chemistry
  • Calcium-Calmodulin-Dependent Protein Kinases / metabolism
  • Glycogen Synthase Kinase 3
  • Glycogen Synthase Kinases
  • Heparin / pharmacology
  • Humans
  • Neurons / chemistry
  • Neurons / enzymology
  • Phosphorylation
  • Protein Binding / drug effects
  • Protein Binding / immunology
  • tau Proteins / chemistry
  • tau Proteins / immunology*
  • tau Proteins / metabolism*

Substances

  • Antibodies, Monoclonal
  • Anticoagulants
  • tau Proteins
  • Heparin
  • Glycogen Synthase Kinases
  • Calcium-Calmodulin-Dependent Protein Kinases
  • Glycogen Synthase Kinase 3