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tau蛋白糖基化参与蛋白质聚集,但不参与细丝形成。

Tau glycation is involved in aggregation of the protein but not in the formation of filaments.

作者信息

Ledesma M D, Pérez M, Colaco C, Avila J

机构信息

Centro de Biología Molecular Severo Ochoa (C.S.I.C./U.A.M.). Universidad Autónoma de Madrid, Cantoblanco, Spain.

出版信息

Cell Mol Biol (Noisy-le-grand). 1998 Nov;44(7):1111-6.

PMID:9846893
Abstract

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.

摘要

一种具有自组装成细丝能力的tau肽(肽2R)被用作模型,以测试糖基化对tau组装或聚集的作用。我们的结果表明,该肽的糖基化促进二聚体形成,但不促进组装成细丝。然而,tau的糖基化导致由糖胺聚糖诱导的聚合作用形成的tau细丝发生束集。这些结果表明糖基化在预先形成的细丝之间形成共价连接中起作用,但在这些细丝的组装中不起作用。

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