期刊
GLYCOBIOLOGY
卷 18, 期 6, 页码 441-446出版社
OXFORD UNIV PRESS INC
DOI: 10.1093/glycob/cwn020
关键词
Lewis x; murine; O-glycan; P-selectin; PSGL-1
资金
- NCI NIH HHS [P01 CA071932, P01 CA071932-11A2] Funding Source: Medline
- NIAID NIH HHS [AI48075, R01 AI048075] Funding Source: Medline
- NIGMS NIH HHS [U54 GM062116, GM62116] Funding Source: Medline
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 H-3-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.
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