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人髓鞘/少突胶质细胞糖蛋白:L2/HNK-1家族的新成员。

Human myelin/oligodendrocyte glycoprotein: a new member of the L2/HNK-1 family.

作者信息

Burger D, Steck A J, Bernard C C, Kerlero de Rosbo N

机构信息

Department of Neurology, Centre Hospitalier Universitaire Vaudois, Lausanne, Switzerland.

出版信息

J Neurochem. 1993 Nov;61(5):1822-7. doi: 10.1111/j.1471-4159.1993.tb09822.x.

Abstract

Myelin/oligodendrocyte glycoprotein (MOG) is a quantitatively minor component of CNS myelin. In this study, human MOG was found to express the L2/HNK-1 epitope on N-linked oligosaccharide structures. This carbohydrate epitope has been found previously in three other characterized human myelin glycoproteins: the myelin-associated glycoprotein, P0, and the oligodendrocyte-myelin glycoprotein. It seems, therefore, that the L2/HNK-1 epitope is expressed frequently in human myelin glycoproteins. Serial lectin affinity chromatography of 14C-glycopeptides indicated that MOG N-oligosaccharide structures are mainly of the complex type, accounting for 77.8% of total radioactivity. In contrast with myelin-associated glycoprotein and P0, which express the L2/HNK-1 epitope on fucosylated structures, in MOG the epitope was detected on all glycopeptide fractions obtained by serial lectin affinity chromatography, although a preferential expression of the L2/HNK-1 epitope was observed on fucosylated structures. Finally, the data indicated that, as for other human myelin glycoproteins, only a subpopulation of MOG molecules expresses the L2/HNK-1 epitope.

摘要

髓鞘/少突胶质细胞糖蛋白(MOG)是中枢神经系统髓鞘中含量较少的一种成分。在本研究中,发现人MOG在N-连接寡糖结构上表达L2/HNK-1表位。此前已在其他三种已鉴定的人髓鞘糖蛋白中发现了这种碳水化合物表位:髓鞘相关糖蛋白、P0和少突胶质细胞-髓鞘糖蛋白。因此,L2/HNK-1表位似乎在人髓鞘糖蛋白中频繁表达。对14C-糖肽进行系列凝集素亲和层析表明,MOG的N-寡糖结构主要为复合型,占总放射性的77.8%。与在岩藻糖基化结构上表达L2/HNK-1表位的髓鞘相关糖蛋白和P0不同,在MOG中,尽管在岩藻糖基化结构上观察到L2/HNK-1表位的优先表达,但在通过系列凝集素亲和层析获得的所有糖肽组分中均检测到该表位。最后,数据表明,与其他人类髓鞘糖蛋白一样,只有一部分MOG分子表达L2/HNK-1表位。

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