PSGL-1 from the murine leukocytic cell line WEHI-3 is enriched for core 2-based O-glycans with sialyl Lewis x antigen
| Autor: | Ziad S. Kawar, Richard D. Cummings, John B. Lowe, Thomas K Johnson, Suvi Natunen |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2008 |
| Předmět: |
Glycan
Glycosylation Neutrophils Lewis X Antigen Biology Biochemistry Fucose Article Cell Line chemistry.chemical_compound Mice Antigen Cell Movement Animals L-Selectin chemistry.chemical_classification Membrane Glycoproteins integumentary system Molecular biology carbohydrates (lipids) P-Selectin Sialyl-Lewis X chemistry Cell culture biology.protein Glycoprotein Protein Modification Translational |
| Popis: | Leukocyte trafficking involves specific recognition between P-selectin and L-selectin and PSGL-1 containing core 2-based O-glycans expressing sialyl Lewis x (SLe(x)) antigen. However, the structural identity of the glycan component(s) displayed by murine neutrophil PSGL-1 that contributes to its P-selectin counter-receptor activity has been uncertain, since these cells express little if any SLe(x) antigen, and because there have been no direct studies to examine murine PSGL-1 glycosylation. To address this uncertainty, we studied PSGL-1 glycosylation in the murine cell line WEHI-3 using metabolic-radiolabeling with (3)H-monosaccharide precursors to detect low-abundance O-glycan structures. We report that PSGL-1 from WEHI-3 cells expresses a di-sialylated core 2 O-glycan containing the SLe(x) antigen. This fucosylated O-glycan is scarce on PSGL-1 and essentially undetectable in total leukocyte glycoproteins from WEHI-3 cells. These results demonstrate that WEHI-3 cells selectively fucosylate PSGL-1 to generate functionally important core 2-based O-glycans containing the SLe(x) antigen. |
| Databáze: | OpenAIRE |
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