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O-glycans on human high endothelial CD34 putatively participating in L-selectin recognition

Leukocyte traffic into lymph nodes and sites of inflammation is guided by L-selectin. Experiments performed in vitro and with gene-deleted mice suggest that CD34 recognizes L-selectin if decorated by 6-sulfo sialyl Lewis x (sLex) saccharides and the MECA-79 epitope. However, very little is known abo...

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Published in:Blood 2002-04, Vol.99 (7), p.2609-2611
Main Authors: Satomaa, Tero, Renkonen, Ossi, Helin, Jari, Kirveskari, Juha, Mäkitie, Antti, Renkonen, Risto
Format: Article
Language:English
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Summary:Leukocyte traffic into lymph nodes and sites of inflammation is guided by L-selectin. Experiments performed in vitro and with gene-deleted mice suggest that CD34 recognizes L-selectin if decorated by 6-sulfo sialyl Lewis x (sLex) saccharides and the MECA-79 epitope. However, very little is known about glycosylation of human L-selectin ligands. We report here on matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF MS) profiles of N- and O-linked oligosaccharide fractions from human tonsillar endothelial CD34. All detected O-glycans were sialylated; some were also monosulfated or monosulfated and monofucosylated. If a given CD34-glycan may carry all requirements for L-selectin recognition, that is, both 6-sulfo-sLex and MECA-79 epitopes, only one O-glycan fraction, O-9, SA2Hex3HexNAc3- Fuc1(SO3)1, meets the criteria. A candidate structure is SAα2-3Galβ1-4(Fucα1-3)(6-sulfo)GlcNAcβ1-3Galβ1-3(SAα2-3Galβ1-4GlcNAcβ1-6)GalNAc. However, if sulfo sLex glycans are supplemented with separate sulfated, nonfucosylated O-glycans, saccharides in O-6, O-8, or O-9, putatively carrying MECA-79 epitopes, could form multiglycan binding epitopes for L-selectin.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood.V99.7.2609