Glycobiology, Vol 9, 823-831, Copyright © 1999 by Oxford University Press
S Zamze, DJ Harvey, P Pesheva, TS Mattu, M Schachner, RA Dwek and DR Wing
As a member of the tenascin family of extracellular matrix glycoproteins,
tenascin-R is located exclusively in the CNS. It is believed to play a role
in myelination and axonal stabilization and, through repulsive properties,
may contribute to the lack of regeneration of CNS axons following damage.
The contrary functions of the tenascins have been localized to the
different structural domains of the protein. However, little is known
concerning the influence of the carbohydrate conjugated to the many
potential sites for N - and O - glycosylation (10-20% by weight). As a
first analytical requirement, we show that >80% of the N -glycans in
tenascin-R are neutral and dominated by complex biantennary structures.
These display the "brain- type" characteristics of outer-arm- and
core-fucosylation, a bisecting N -acetylglucosamine and, significantly, an
abundance of antennae truncation. In some structures, truncation resulted
in only a single mannose residue remaining on the 3-arm, a particularly
unusual consequence of the N -glycan processing pathway. In contrast to
brain tissue, hybrid and oligomannosidic N -glycans were either absent or
in low abundance. A high relative abundance of O -linked sialylated glycans
was found. This was associated with a significant potential for O -linked
glycosylation sites and multivalent display of the sialic acid residues.
These O -glycans were dominated by the disialylated structure,
NeuAcalpha2-3Galbeta1-3(NeuAcalpha2-6)GalNAc. The possibility that these O
-glycans enable tenascin-R to interact in the CNS either with the myelin
associated glycoprotein or with sialoadhesin on activated microglia is
discussed.
ORIGINAL ARTICLES
Glycosylation of a CNS-specific extracellular matrix glycoprotein, tenascin-R, is dominated by O-linked sialylated glycans and "brain- type" neutral N-glycans
Glycobiology Institute, Department of Biochemistry, South Parks Road, Oxford OX1 3QU, UK.
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