Dec 10, 1998

Tau glycation is involved in aggregation of the protein but not in the formation of filaments

Cellular and Molecular Biology
M D LedesmaJ Avila


A tau peptide, peptide 2R, with capacity for self assembly into filaments was used as a model to test the role of glycation on tau assembly or aggregation. Our results indicate that glycation of that peptide facilitates dimer formation but not assembly into filaments. However, glycation of tau results in the bundling of the tau filaments formed by glycosaminoglycan-induced polymerisation. These results suggest a role of glycation in the formation of covalent links among pre-formed filaments but not in the assembly of those filaments.

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Mentioned in this Paper

Familial Alzheimer Disease (FAD)
Covalent Interaction
Neurofibrillary Degeneration (Morphologic Abnormality)
Electron Microscopy
Protein Glycosylation
Tau Proteins

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