Tau glycation is involved in aggregation of the protein but not in the formation of filaments.
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.
Ledesma
M D
MD
Centro de Biología Molecular Severo Ochoa (C.S.I.C./U.A.M.). Universidad Autónoma de Madrid, Cantoblanco, Spain.
Pérez
M
M
Colaco
C
C
Avila
J
J
D000544:Alzheimer Disease / Q000378:metabolism* / Q000473:pathology; D000595:Amino Acid Sequence; D019281:Dimerization; D006025:Glycosaminoglycans / Q000378:metabolism; D006031:Glycosylation; D006801:Humans; D008854:Microscopy, Electron; D008870:Microtubules / Q000737:chemistry / Q000378:metabolism; D008969:Molecular Sequence Data; D016874:Neurofibrillary Tangles / Q000737:chemistry* / Q000378:metabolism* / Q000648:ultrastructure; D010455:Peptides / Q000138:chemical synthesis; D011108:Polymers / Q000378:metabolism; D016875:tau Proteins / Q000737:chemistry* / Q000378:metabolism*
D006025:Glycosaminoglycans; D010455:Peptides; D011108:Polymers; D016875:tau Proteins