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

Using recombinant human tau protein phosphorylated by a brain extract and the glycogen synthase kinase-3β 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,...

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Bibliographic Details
Published in:Brain research. Molecular brain research. 2000-05, Vol.78 (1), p.181-185
Main Authors: Torreilles, François, Roquet, Françoise, Granier, Claude, Pau, Bernard, Mourton-Gilles, Chantal
Format: Article
Language:English
Subjects:
AD2
Alzheimer
Alzheimer Disease - metabolism
Amino Acid Sequence
Anti-PHF-tau antibody
Antibodies, Monoclonal - immunology
Antibody Specificity
Anticoagulants - pharmacology
Biological and medical sciences
Brain Chemistry
Calcium-Calmodulin-Dependent Protein Kinases - metabolism
Degenerative and inherited degenerative diseases of the nervous system. Leukodystrophies. Prion diseases
Glycogen Synthase Kinase 3
glycogen synthase kinase 3^b
Glycogen Synthase Kinases
Heparin - pharmacology
Humans
Medical sciences
Multiple peptide synthesis
Neurology
Neurons - chemistry
Neurons - enzymology
Phosphorylation
Protein Binding - drug effects
Protein Binding - immunology
Tau protein
tau Proteins - chemistry
tau Proteins - immunology
tau Proteins - metabolism
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Summary:Using recombinant human tau protein phosphorylated by a brain extract and the glycogen synthase kinase-3β 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.
ISSN:0169-328X
1872-6941
DOI:10.1016/S0169-328X(00)00073-5