Subgroup differences in “brain-type” transferrin and alpha-synuclein in Parkinson's disease and multiple system atrophy

Subgroup differences in “brain-type” transferrin and alpha-synuclein in Parkinson's disease and multiple system atrophy
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帕金森病和多系统萎缩中“脑型”转铁蛋白和α-突触核蛋白的亚组差异

DOI:
10.1093/jb/mvw015
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发表时间:
2016
期刊:
The Journal of Biochemistry
影响因子:
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通讯作者:
et. al
et. al
中科院分区:
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文献类型:
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作者:
A Yoshihara;M Fukatsu;K Hoshi;Y Hashimoto;et. al

文献摘要

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先前在脑脊液(CSF)中发现了两种转铁蛋白(Tf)聚糖亚型;一种似乎来源于血清(Tf-2),另一种来源于脉络丛,一种产生CSF的组织(Tf-1)。为了分析与两种亚型相关的代谢差异,将它们的比率(Tf-2/Tf-1)定义为Tf指数。在这里,我们报告的tauopathies包括阿尔茨海默病患者的Tf指数(2.29 ± 0.64)与神经系统对照组(2.07 ± 0.87)相似(P= 0.147)。而帕金森病(PD)和多系统萎缩(MSA)患者的Tf指数(3.38 ± 1.87)高于对照组(2.07 ± 0.87),P值分别< 0.001和0.024。TF指数PD和MSA没有出现正态分布。事实上,去趋势正态分位数-分位数图分析显示存在一个独立的亚组,显示PD和MSA的Tf指数较高。PD亚组CSF α-synuclein水平(38.3 ± 17.8 ng/ml)明显高于其他亚组(25.3 ± 11.3 ng/ml,P= 0.012)。这些结果表明,PD(和MSA)包括两个亚组,它们显示CSF转铁蛋白和α-突触核蛋白的不同代谢。
Two transferrin (Tf) glycan-isoforms were previously found in cerebrospinal fluid (CSF); one appears to be derived from serum (Tf-2) and the other from choroid plexus, a CSF-producing tissue (Tf-1). To analyse metabolic differences associated with the two isoforms, their ratio (Tf-2/Tf-1) was defined as the Tf index. Here we report that Tf indices of patients with tauopathies including Alzheimer’s disease (2.29 + 0.64) were similar to those of neurological controls (2.07 + 0.87) (P= 0.147). In contrast, Tf indices with Parkinson’s disease (PD, 3.38 ± 1.87) and multiple system atrophy (MSA, 3.15 ± 1.72) were higher than those of the controls (2.07 ± 0.87), theP-values being < 0.001 and 0.024, respectively. Tf indices of PD and MSA did not appear to be normally distributed. Indeed, detrended normal Quantile–Quantile plot analysis revealed the presence of an independent subgroup showing higher Tf indices in PD and MSA. The subgroup of PD showed higher levels of CSF α-synuclein (38.3 ± 17.8 ng/ml) than the rest (25.3 ± 11.3 ng/ml,P= 0.012). These results suggest that PD (and MSA) includes two subgroups, which show different metabolism of CSF transferrin and α-synuclein.