Core2 β-1,6-N-Acetylglucosaminyltransferase Enzyme Activity Is Critical for P-Selectin Glycoprotein Ligand-1 Binding to P-Selectin

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...

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Bibliographic Details
Published in:Blood 1996-11, Vol.88 (10), p.3872-3879
Main Authors: Kumar, Ravindra, Camphausen, Raymond T., Sullivan, Francis X., Cumming, Dale A.
Format: Article
Language:English
Subjects:
Analytical, structural and metabolic biochemistry
Animals
Biological and medical sciences
Carbohydrate Conformation
CHO Cells
Cricetinae
Cricetulus
E-Selectin - metabolism
Enzymes and enzyme inhibitors
Fucosyltransferases - metabolism
Fundamental and applied biological sciences. Psychology
Gangliosides - metabolism
Glycosylation
Humans
Ligands
Membrane Glycoproteins - chemistry
Membrane Glycoproteins - metabolism
N-Acetylglucosaminyltransferases - genetics
N-Acetylglucosaminyltransferases - physiology
Oligosaccharides - metabolism
P-Selectin - metabolism
Protein Binding
Protein Processing, Post-Translational
Recombinant Fusion Proteins - metabolism
Sialyl Lewis X Antigen
Transfection
Transferases
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Summary: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.
ISSN:0006-4971
1528-0020
DOI:10.1182/blood.V88.10.3872.bloodjournal88103872