期刊
BLOOD
卷 114, 期 3, 页码 733-741出版社
AMER SOC HEMATOLOGY
DOI: 10.1182/blood-2009-03-210237
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资金
- Academy of Finland [107203, 118469]
- National Institutes of Health [HL085607]
- Magnus Ehrnrooth Foundation
- Helsinki University Central Hospital Research Funds, Helsinki, Finland
- Academy of Finland (AKA) [118469, 107203, 107203, 118469] Funding Source: Academy of Finland (AKA)
Endothelial sialomucin CD34 functions as an L-selectin ligand mediating lymphocyte extravasation only when properly glycosylated to express a sulfated carbohydrate epitope, 6-sulfo sialyl Lewis x (6-sulfo SLe(x)). It is thought that multivalent 6-sulfo SLex expression promotes high-affinity binding to L-selectin by enhancing avidity. However, the reported low amount of 6-sulfo SLex in total human CD34 is inconsistent with this model and prompted us to re-evaluate CD34 glycosylation. We separated CD34 into 2 glycoforms, the L-selectin-binding and nonbinding glycoforms, L-B-CD34 and L-NBCD34, respectively, and analyzed released O- and N-glycans from both forms. L-BCD34 is relatively minor compared with L-NB-CD34 and represented less than 10% of total tonsillar CD34. MECA-79, a mAb to sulfated core-1 O-glycans, bound exclusively to L-B-CD34 and this form contained all sulfated and fucosylated Oglycans. 6-Sulfo SLe(x) epitopes occur on core-2 and extended core-1 O-glycans with approximately 20% of total L-B-CD34 O-glycans expressing 6-sulfo SLe(x). Nglycans containing potential 6-sulfo SLex epitopes were also present in L-B-CD34, but their removal did not abolish binding to L-selectin. Thus, a minor glycoform of CD34 carries relatively abundant 6-sulfo SLex epitopes on O-glycans that are important for its recognition by L-selectin. (Blood. 2009;114:733-741)
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