| Literature DB >> 7693868 |
D Burger1, A J Steck, C C Bernard, N Kerlero de Rosbo.
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.Entities:
Mesh:
Substances:
Year: 1993 PMID: 7693868 DOI: 10.1111/j.1471-4159.1993.tb09822.x
Source DB: PubMed Journal: J Neurochem ISSN: 0022-3042 Impact factor: 5.372