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Titolo:
Glycosylation of a CNS-specific extracellular matrix glycoprotein, tenascin-R, is dominated by O-linked sialylated glycans and "brain-type" neutral N-glycans
Autore:
Zamze, S; Harvey, DJ; Pesheva, P; Mattu, TS; Schachner, M; Dwek, RA; Wing, DR;
Indirizzi:
Glycobiol Inst, Dept Biochem, Oxford OX1 3QU, England Glycobiol Inst Oxford England OX1 3QU t Biochem, Oxford OX1 3QU, England ETH Honggerberg, Dept Neurobiol, CH-8093 Zurich, Switzerland ETH Honggerberg Zurich Switzerland CH-8093 , CH-8093 Zurich, Switzerland
Titolo Testata:
GLYCOBIOLOGY
fascicolo: 8, volume: 9, anno: 1999,
pagine: 823 - 831
SICI:
0959-6658(199908)9:8<823:GOACEM>2.0.ZU;2-A
Fonte:
ISI
Lingua:
ENG
Soggetto:
MYELIN-ASSOCIATED GLYCOPROTEIN; CELL-ADHESION MOLECULE; CENTRAL-NERVOUS-SYSTEM; ACID-BINDING RECEPTOR; NEURITE OUTGROWTH; MESSENGER-RNA; ADULT-MOUSE; PROTEIN TENASCIN; SUGAR CHAINS; OPTIC-NERVE;
Keywords:
CNS; extracellular matrix; N- and O-glycans; sialylation; tenascin-R;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
62
Recensione:
Indirizzi per estratti:
Indirizzo: Wing, DR Glycobiol Inst, Dept Biochem, S Parks Rd, Oxford OX1 3QU, EnglandGlycobiol Inst S Parks Rd Oxford England OX1 3QU X1 3QU, England
Citazione:
S. Zamze et al., "Glycosylation of a CNS-specific extracellular matrix glycoprotein, tenascin-R, is dominated by O-linked sialylated glycans and "brain-type" neutral N-glycans", GLYCOBIOLOG, 9(8), 1999, pp. 823-831

Abstract

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 rolein 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-a 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 the3-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, NeuAc alpha 2-3Gal beta 1-3(NeuAc alpha 2-6)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.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 01/04/20 alle ore 19:19:14