Human Myelin/Oligodendrocyte Glycoprotein: A New Member of the L2/HNK‐1 Family

Danielle Burger, Andreas J. Steck, Claude C.A. Bernard, Nicole Kerlero de Rosbo

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Abstract

Abstract— Myelin/oligodendrocyte glycoprotein (MOG) is a quantitatively minor component of CMS 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 my‐elin‐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‐asso‐ciated 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.

Original languageEnglish
Pages (from-to)1822-1827
Number of pages6
JournalJournal of Neurochemistry
Volume61
Issue number5
DOIs
Publication statusPublished - 1993
Externally publishedYes

Keywords

  • arbohydrate epitop
  • Myelin/oligodendrocyte glycoprotei
  • NK‐1 antibody
  • yelin glycoprotein

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