PSGL-1 from the murine leukocytic cell line WEHI-3 is enriched for core 2-based O-glycans with sialyl Lewis x antigen
Open Access
- 29 February 2008
- journal article
- research article
- Published by Oxford University Press (OUP) in Glycobiology
- Vol. 18 (6) , 441-446
- https://doi.org/10.1093/glycob/cwn020
Abstract
Leukocyte trafficking involves specific recognition between P-selectin and L-selectin and PSGL-1 containing core 2-based O-glycans expressing sialyl Lewis x (SLex) 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 SLex 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 3H-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 SLex 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 SLex antigen.Keywords
This publication has 31 references indexed in Scilit:
- N-glycans of core2 β(1,6)-N-acetylglucosaminyltransferase-I (C2GnT-I) but not those of α(1,3)-fucosyltransferase-VII (FucT-VII) are required for the synthesis of functional P-selectin glycoprotein ligand-1 (PSGL-1): effects on P-, L- and E-selectin bindingBiochemical Journal, 2005
- Glycan-dependent leukocyte adhesion and recruitment in inflammationCurrent Opinion in Cell Biology, 2003
- Discordant expression of selectin ligands and sialyl Lewis x–related epitopes on murine myeloid cellsBlood, 2002
- Partial characterization of the N-linked oligosaccharide structures on P-selectin glycoprotein ligand-1 (PSGL-1)Cell Research, 2001
- P-selectin Glycoprotein Ligand-1 and E-selectin Ligand-1 Are Differentially Modified by Fucosyltransferases Fuc-TIV and Fuc-TVII in Mouse NeutrophilsJournal of Biological Chemistry, 2000
- The E-selectin Ligand-1 Is Selectively Activated in Chinese Hamster Ovary Cells by the α(1,3)-Fucosyltransferases IV and VIIJournal of Biological Chemistry, 1996
- The α(1,3)Fucosyltransferase Fuc-TVII Controls Leukocyte Trafficking through an Essential Role in L-, E-, and P-selectin Ligand BiosynthesisCell, 1996
- Structures of the O-Glycans on P-selectin Glycoprotein Ligand-1 from HL-60 CellsJournal of Biological Chemistry, 1996
- Species differences in the expression of carbohydrate differentiation antigens on mammalian blood cells revealed by immunofluorescence with monoclonal antibodiesBioscience Reports, 1984
- The SdaBlood Group Antigen in Tissues and Body FluidsVox Sanguinis, 1970