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Human Myelin/Oligodendrocyte Glycoprotein: A New Member of the L2/HNK‐1 Family
Author(s) -
Burger Danielle,
Steck Andreas J.,
Bernard Claude C. A.,
Rosbo Nicole Kerlero
Publication year - 1993
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1111/j.1471-4159.1993.tb09822.x
Subject(s) - epitope , glycoprotein , myelin oligodendrocyte glycoprotein , myelin associated glycoprotein , myelin , lectin , oligosaccharide , glycopeptide , biochemistry , chemistry , microbiology and biotechnology , biology , antibody , immunology , central nervous system , neuroscience , antibiotics
— 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, P 0 , 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 14 C‐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 P 0 , 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.