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tau蛋白与阿尔茨海默病的神经原纤维病理改变

Tau protein and the neurofibrillary pathology of Alzheimer's disease.

作者信息

Goedert M

机构信息

MRC Laboratory of Molecular Biology, Cambridge, United Kingdom.

出版信息

Ann N Y Acad Sci. 1996 Jan 17;777:121-31. doi: 10.1111/j.1749-6632.1996.tb34410.x.

DOI:10.1111/j.1749-6632.1996.tb34410.x
PMID:8624074
Abstract

Abundant neurofibrillary tangles, neuropil threads and senile plaque neurites constitute the neurofibrillary pathology of Alzheimer's disease. They form in the nerve cells that undergo degeneration in the disease, in which their regional distribution correlates with the degree of dementia. Each lesion contains the paired helical filament (PHF) as its major component. PHFs are composed of the microtubule-associated protein tau in a hyperphosphorylated state. PHF-tau is hyperphosphorylated on all six adult brain isoforms. As a consequence, tau is unable to bind to microtubules and is believed to self-assemble into the PHF. Several candidate protein kinases and protein phosphatases have been identified through in vitro experiments.

摘要

大量神经原纤维缠结、神经毡丝和老年斑神经突构成了阿尔茨海默病的神经原纤维病理改变。它们在该疾病中发生变性的神经细胞内形成,其区域分布与痴呆程度相关。每个病变都以双螺旋丝(PHF)作为主要成分。PHF由处于高度磷酸化状态的微管相关蛋白tau组成。PHF-tau在所有六种成人脑异构体上均高度磷酸化。因此,tau无法与微管结合,并被认为会自行组装成PHF。通过体外实验已鉴定出几种候选蛋白激酶和蛋白磷酸酶。

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