τ Protein from Alzheimer's Disease Patients Is Glycated at Its Tubulin‐Binding Domain

Publisher Website
Google Scholar
Abstract
Glycated residues of tau protein from paired helical filaments isolated from the brains of Alzheimer's disease patients were localized by doing a proteolytic cleavage of the protein, fractionation of the resulting peptides, and identification of those peptides using specific antibodies. The most suitable residues for glycation, lysines, present at the tubulin-binding motif of tau protein, seem to be preferentially modified compared with those lysines present at other regions. Among these modified lysines, those located in the sequence comprising residues 318-336 (in the largest human tau isoform) were found to be glycated, as determined by the reaction with an antibody that recognizes a glycated peptide containing this sequence. Because those lysines are present in a tubulin binding motif of tau protein, its modification could result in a decrease in the interaction of tau with tubulin.

This publication has 0 references indexed in Scilit: