神经退行性病变传播的硫酸化密码。
The sulfation code for propagation of neurodegeneration.
机构信息
From the Department of Neurology and Neurobiology of Aging, Kanazawa University Graduate School of Medical Sciences, Kanazawa 920-8640, Japan
From the Department of Neurology and Neurobiology of Aging, Kanazawa University Graduate School of Medical Sciences, Kanazawa 920-8640, Japan.
出版信息
J Biol Chem. 2018 Jul 6;293(27):10841-10842. doi: 10.1074/jbc.H118.003970.
Abstract
Prion-like propagation of protein aggregates is thought to be an essential feature in many neurodegenerative diseases, but the mechanisms underlying transcellular transfer of protein aggregates remain unclear. Stopschinski now demonstrate that the cellular uptake of tau, Aβ, and α-synuclein aggregates mediated by heparan sulfate proteoglycans (HSPGs) varies with distinct glycosaminoglycan chain length and sulfation patterns. The results help us to understand how different protein aggregates propagate, leading to distinct neurodegenerative pathologies.
摘要
朊病毒样蛋白聚集物的传播被认为是许多神经退行性疾病的一个基本特征，但蛋白聚集物的细胞间转移的机制仍不清楚。Stopschinski 等人现在证明，通过硫酸乙酰肝素蛋白聚糖 (HSPG) 介导的 tau、Aβ 和 α-突触核蛋白聚集物的细胞摄取，随独特的糖胺聚糖链长度和硫酸化模式而变化。这些结果有助于我们理解不同的蛋白聚集物如何传播，导致不同的神经退行性病变。
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本文引用的文献
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