Direct interaction of soluble human recombinant tau protein with Abeta 1-42 results in tau aggregation and hyperphosphorylation by tau protein kinase II.
We report here that aggregated beta-amyloid (Abeta) 1-42 promotes tau aggregation in vitro in a dose-dependent manner. When Abeta-mediated aggregated tau was used as a substrate for tau protein kinase II (TPK II), an 8-fold increase in the rate of TPK II-mediated tau phosphorylation was observed. The extent of TPK ... II-dependent tau phosphorylation increased as a function of time and Abeta 1-42 concentration, and hyperphosphorylated tau was found to be decorated with an Alzheimer's disease-related phosphoepitope (P-Thr-231). In HEK 293 cells co-expressing CT-100 amyloid precursor protein and tau, the release of Abeta 1-42 from these cells was impaired. Taken together, these in vitro results suggest that Abeta 1-42 promotes both tau aggregation and hyperphosphorylation.
Mesh Terms:
Alzheimer Disease, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Animals, Cattle, Cell Line, Cyclin-Dependent Kinase 5, Dose-Response Relationship, Drug, Epitopes, Genes, Reporter, Humans, Kidney, Macromolecular Substances, Peptide Fragments, Phosphorylation, Protein Binding, Protein-Serine-Threonine Kinases, Recombinant Fusion Proteins, Recombinant Proteins, Solubility, tau Proteins
Alzheimer Disease, Amyloid beta-Peptides, Amyloid beta-Protein Precursor, Animals, Cattle, Cell Line, Cyclin-Dependent Kinase 5, Dose-Response Relationship, Drug, Epitopes, Genes, Reporter, Humans, Kidney, Macromolecular Substances, Peptide Fragments, Phosphorylation, Protein Binding, Protein-Serine-Threonine Kinases, Recombinant Fusion Proteins, Recombinant Proteins, Solubility, tau Proteins
FEBS Lett.
Date: Mar. 13, 2002
PubMed ID: 11943163
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