Premium
τ Protein from Alzheimer's Disease Patients Is Glycated at Its Tubulin‐Binding Domain
Author(s) -
Ledesma M. Dolores,
Bonay Pedro,
Avila Jesús
Publication year - 1995
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.1995.65041658.x
Subject(s) - glycation , gene isoform , alzheimer's disease , tubulin , chemistry , tau protein , biochemistry , peptide , glycosylation , cleavage (geology) , biology , microbiology and biotechnology , receptor , microtubule , disease , medicine , paleontology , fracture (geology) , gene
Glycated residues of τ 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 τ 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 τ 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 τ protein, its modification could result in a decrease in the interaction of τ with tubulin.