Altered glycosylation of acetylcholinesterase in Creutzfeldt-Jakob disease
Altered glycosylation of acetylcholinesterase in Creutzfeldt-Jakob disease
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DOI：
10.1111/j.1471-4159.2005.03514.x
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发表时间：
2006-01-01
影响因子：
4.7
通讯作者：
Sáez-Valero, J
中科院分区：
文献类型：
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作者：
Silveyra, MX;Cuadrado-Corrales, N;Sáez-Valero, J
脑蛋白糖基化模式的变化与克雅氏病（CJD）有关。我们通过凝集素结合测定研究了乙酰胆碱酯酶（AChE）的糖基化状态。我们的数据显示，与年龄匹配的对照相比，明确和可能散发的克雅氏病病例的腰椎脑脊液中乙酰胆碱酯酶活性较低。我们还首次表明，克雅氏病脑脊液和大脑中的 AChE 糖基化发生了改变。与阿尔茨海默病不同的是，在阿尔茨海默病中，AChE 分子形式的糖基化和水平都发生了改变，而克雅氏病中 AChE 的异常糖基化似乎与该酶分子形式的变化无关。这些发现表明，克雅氏病中乙酰胆碱酯酶 (AChE) 糖基化的改变可能是影响朊病毒蛋白以及其他蛋白质的糖基化机制总体扰动的结果。这些变化的诊断潜力仍有待探索。
Changes in the glycosylation pattern of brain proteins have been associated with Creutzfeldt-Jakob disease (CJD). We have investigated the glycosylation status of acetylcholinesterase (AChE) by lectin binding assay. Our data show that in lumbar CSF from definite and probable sporadic CJD cases AChE activity is lower compared with that in age-matched controls. We also show, for the first time, that AChE glycosylation is altered in CJD CSF and brain. Unlike Alzheimer's disease, in which an alteration in both the glycosylation and levels of AChE molecular forms is observed, the abnormal glycosylation of AChE in CJD appears to be unrelated to changes in molecular forms of this enzyme. These findings suggest that altered AChE glycosylation in CJD may be a consequence of the general perturbation of the glycosylation machinery that affects prion protein, as well as other proteins. The diagnostic potential of these changes remains to be explored.