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神经退行性疾病:致病性突变产生的淀粉样蛋白孔道

Neurodegenerative disease: amyloid pores from pathogenic mutations.

作者信息

Lashuel Hilal A, Hartley Dean, Petre Benjamin M, Walz Thomas, Lansbury Peter T

机构信息

Center for Neurologic Diseases, Brigham and Women's Hospital and Department of Neurology, Harvard Medical School, 65 Landsdowne Street, Cambridge, Massachusetts 02139, USA.

出版信息

Nature. 2002 Jul 18;418(6895):291. doi: 10.1038/418291a.

Abstract

Alzheimer's and Parkinson's diseases are associated with the formation in the brain of amyloid fibrils from beta-amyloid and alpha-synuclein proteins, respectively. It is likely that oligomeric fibrillization intermediates (protofibrils), rather than the fibrils themselves, are pathogenic, but the mechanism by which they cause neuronal death remains a mystery. We show here that mutant amyloid proteins associated with familial Alzheimer's and Parkinson's diseases form morphologically indistinguishable annular protofibrils that resemble a class of pore-forming bacterial toxins, suggesting that inappropriate membrane permeabilization might be the cause of cell dysfunction and even cell death in amyloid diseases.

摘要

阿尔茨海默病和帕金森病分别与大脑中由β-淀粉样蛋白和α-突触核蛋白形成的淀粉样原纤维有关。致病的可能是寡聚纤维化中间体(原纤维),而非原纤维本身,但其导致神经元死亡的机制仍是个谜。我们在此表明,与家族性阿尔茨海默病和帕金森病相关的突变淀粉样蛋白会形成形态上难以区分的环状原纤维,类似于一类可形成孔道的细菌毒素,这表明不适当的膜通透性可能是淀粉样疾病中细胞功能障碍甚至细胞死亡的原因。

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