دورية
Core2 β-1,6-N-Acetylglucosaminyltransferase Enzyme Activity Is Critical for P-Selectin Glycoprotein Ligand-1 Binding to P-Selectin
| العنوان: | Core2 β-1,6-N-Acetylglucosaminyltransferase Enzyme Activity Is Critical for P-Selectin Glycoprotein Ligand-1 Binding to P-Selectin |
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| المؤلفون: | Kumar, Ravindra, Camphausen, Raymond T., Sullivan, Francis X., Cumming, Dale A. |
| المصدر: | Blood; November 1996, Vol. 88 Issue: 10 p3872-3879, 8p |
| مستخلص: | P-selectin glycoprotein ligand-1 (PSGL-1) is a high-affinity counterreceptor for P-selectin on myeloid cells and activated T-cells. In addition, PSGL-1 can serve, both in vitro and in vivo, as an E-selectin ligand. Appropriate glycosylation of PSGL-1 is crucial for binding to P-selectin. Functional PSGL-1 is known to bear sialyl lewis X (SLex) or a closely related oligosaccharide. In this study, we show that Chinese hamster ovary (CHO) cells expressing PSGL-1 and fucosyltrans-ferase show a dramatic increase in binding to P-selectin when transfected with “core2” transferase, the enzyme that initiates branching of O-linked glycans. Moreover, only PSGL-1 from core2 transfectant CHO cells can be affinity-captured with P-selectin, suggesting that branched O-linked glycans are required for high-affinity binding to P-selectin. Analysis of PSGL-1 -derived O-linked oligosaccharides produced in core2 transfected cells shows the presence of more elaborated glycans. Interestingly, transfection of core2 in these cells does not alter binding to E-selectin. |
| قاعدة البيانات: | Supplemental Index |
Full Text Finder | تدمد: | 00064971 15280020 |
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| DOI: | 10.1182/blood.V88.10.3872.bloodjournal88103872 |