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来自血小板的α-突触核蛋白在帕金森病和多系统萎缩中丝氨酸129位点未发生磷酸化。

alpha-synuclein from platelets is not phosphorylated at serine 129 in Parkinson's disease and multiple system atrophy.

作者信息

Shults Clifford W, Barrett Jennifer M, Fontaine Deborah

机构信息

Department of Neurosciences, University of California, San Diego, La Jolla, CA 92093-0662, USA.

出版信息

Neurosci Lett. 2006 Sep 25;405(3):223-5. doi: 10.1016/j.neulet.2006.07.006. Epub 2006 Aug 9.

DOI:10.1016/j.neulet.2006.07.006
PMID:16901642
Abstract

Parkinson's disease (PD) and multiple system atrophy (MSA) are characterized pathologically by inclusions in the brain containing alpha-synuclein, which is phosphorylated at serine 129. alpha-Synuclein is present not only in the brain but also in platelets; platelets have previously been used to study mitochondrial function in PD. We undertook to determine whether alpha-synuclein extracted from platelets of patients with PD and MSA is phosphorylated at serine 129 and could be used as a peripheral marker of these disorders. Immunoblots indicated that platelet alpha-synuclein is not phosphorylated at serine 129 in PD and MSA.

摘要

帕金森病(PD)和多系统萎缩(MSA)在病理上的特征是大脑中含有在丝氨酸129处磷酸化的α-突触核蛋白的包涵体。α-突触核蛋白不仅存在于大脑中,也存在于血小板中;血小板此前已被用于研究PD中的线粒体功能。我们旨在确定从PD和MSA患者血小板中提取的α-突触核蛋白是否在丝氨酸129处磷酸化,以及是否可作为这些疾病的外周标志物。免疫印迹表明,PD和MSA患者血小板中的α-突触核蛋白在丝氨酸129处未磷酸化。

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Post mortem cerebrospinal fluid α-synuclein levels are raised in multiple system atrophy and distinguish this from the other α-synucleinopathies, Parkinson's disease and Dementia with Lewy bodies.
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