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首页> 外文期刊>Neuropathology: official journal of the Japanese Society of Neuropathology >Sialylated and O-glycosidically linked glycans in prion protein deposits in a case of Gerstmann-Straussler-Scheinker disease.
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Sialylated and O-glycosidically linked glycans in prion protein deposits in a case of Gerstmann-Straussler-Scheinker disease.

机译：如果发生Gerstmann-Straussler-Scheinker病，病毒蛋白沉积物中的唾液酸化和O-糖苷连接的聚糖。

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摘要

Prion diseases are caused by an abnormal form of the prion protein (PrP(Sc)). We identified, with lectins, post-translational modifications of brain proteins due to glycosylation in a Gerstmann-Straussler-Scheinker (GSS) patient. The lectin Amaranthus leucocarpus (ALL), specific for mucin type O-glycosylated structures (Galss1,3 GalNAcalpha1,0 Ser/Thr or GalNAcalpha1,0 Ser/Thr), and Sambucus nigra agglutinin (SNA), specific for Neu5Acalpha2,6 Gal/GalNAc, showed positive labeling in all the prion deposits and in the core of the PrP(Sc) deposits, respectively, indicating specific distribution of O-glycosylated and sialylated structures. Lectins from Maackia amurensis (MAA, Neu5Acalpha2,3), Macrobrachium rosenbergii (MrL, Neu5,9Ac2-specific) and Arachis hypogaea (PNA, Gal-specific) showed low staining of prion deposits. Immunohistochemistry colocalization with prion antibody indicated that all lectins stained prion protein deposits. These results show that specific modifications in the glycosylation pattern are closely related to the hallmark lesions and might be an early event in neuronal degeneration in GSS disease.
机译：on病毒疾病是由an蛋白（PrP（Sc））的异常形式引起的。我们用凝集素鉴定了Gerstmann-Straussler-Scheinker（GSS）患者的糖基化引起的脑蛋白翻译后修饰。特定于粘蛋白O型糖基化结构（Galss1,3 GalNAcalpha1,0 Ser / Thr或GalNAcalpha1,0 Ser / Thr）的凝集素Amaranthus leucocarpus（ALL）和特定于Neu5Acalpha2,6 Gal /的黑胶凝集素（SNA） GalNAc，分别在所有病毒沉积物和PrP（Sc）沉积物的核心中显示阳性标记，表明O-糖基化和唾液酸化结构的特定分布。来自黑莓（Maackia amurensis）（MAA，Neu5Acalpha2,3），罗氏沼虾（MrL，Neu5,9Ac2特异性）和花生（PNA，Gal特异性）的凝集素对病毒沉积物的染色较低。免疫组织化学与病毒抗体的共定位表明，所有凝集素均会染色病毒蛋白质沉积物。这些结果表明，糖基化模式的特定修饰与标志性病变密切相关，可能是GSS疾病中神经元变性的早期事件。

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