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- W2980873062 abstract "Tau-glycan interaction mediates tau transcellular movement in the prion-like spread of tau pathology in Alzheimer's disease (AD). Previously, we have characterized 6-O-group as an important factor for tau-glycan interaction. The role of 3-O-sulfo group, in contrast, is much harder to study, due to the lack of efficient method for 3-O-desulfation and the high level of redundancy in heparan sulfate 3-O-sulfotransferases (HS3ST) in mammalian cells. With chemically defined heparan sulfate glycan array, the Tau-glycan interaction was explored in detail. SPR, NMR and heparan sulfate (HS) deficient cell lines were used to validate and further characterize the important role of 3-O-sulfo in tau-glycan interaction. Data from glycan array showed much higher tau-binding affinity with the presence of 3-O-sulfo group. SPR competition and cell surface binding assay in HS deficient cells further confirmed the important role of 3-O-sulfo group. 3-O-sulfo, a much less abundant sulfo group in HS, is likely to be an even more important determinant for the specificity of tau-HS interaction than 6-O-sulfo group. Our results have important implication not only for the fundamental biology of tauopathy but also for AD drug discovery aimed at disrupting the prion-like spread of tau pathology." @default.
- W2980873062 created "2019-10-25" @default.
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- W2980873062 date "2019-07-01" @default.
- W2980873062 modified "2023-10-18" @default.
- W2980873062 title "P4-521: 3-O-SULFO GROUP IS A KEY DETERMINANT IN TAU-GLYCAN INTERACTION" @default.
- W2980873062 doi "https://doi.org/10.1016/j.jalz.2019.08.068" @default.
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