Polymerization of tau peptides into fibrillar structures. The effect of FTDP-17 mutations

• Published in: FEBS letters Vol. 446; no. 1; pp. 199 - 202
• Main Authors: Arrasate, Monserrat, Pérez, Mar, Armas-Portela, Rosario, Ávila, Jesús
• Format: Journal Article
• Language: English
• Published: England Elsevier B.V 05.03.1999
• Subjects: Amino Acid Sequence; Animals; Dimerization; FTDP-17, frontotemporal dementia and Parkinsonism linked to chromosome 17; MES, 2-(N-morpholino) ethanesulphonic acid; Microtubules - chemistry; Molecular Sequence Data; Mutation; PHF, paired helical filament; Polymer; Protein Folding; Tau; tau Proteins - chemistry; tau Proteins - genetics; Taupathy; τ, Tau; Taupathy; MES, 2-( N-morpholino) ethanesulphonic acid; Tau; Polymer; τ, Tau; FTDP-17, frontotemporal dementia and Parkinsonism linked to chromosome 17; PHF, paired helical filament
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(99)00210-0

The peptides corresponding to the four repeats found in the microtubule binding region of tau protein were synthesized and their ability for self-aggregation in presence of heparin or chondroitin sulfate was measured. Mainly, only the peptide containing the third tau repeat is able to form polymers in a high proportion. Additionally, the peptide containing the second repeat aggregates with a very low efficiency. However, when this peptide contains the mutation (P301L), described in a fronto temporal dementia, it is able to form polymers at a higher extent. Finally, it is suggested to have a role for the first and fourth tau repeats. It could be to decrease the ability of the third tau repeat for self-aggregation in the presence of heparin.