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Glycobiology Advance Access published online on February 29, 2008
Glycobiology, doi:10.1093/glycob/cwn020
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© The Author 2008. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org
This is an Open Access article distributed under the terms of the Creative Commons Attribution Non-Commercial License (http://creativecommons.org/licenses/by-nc/2.0/uk/) which permits unrestricted non-commercial use, distribution, and reproduction in any medium, provided the original work is properly cited.

Communications

PSGL-1 from the Murine Leukocytic Cell Line WEHI-3 is Enriched for Core 2-Based O-glycans with Sialyl Lewis x Antigen

Ziad S. Kawar1,2, Thomas K. Johnson1,3, Suvi Natunen1,4, John B. Lowe5 and Richard D. Cummings1,3,6

1 Department of Biochemistry and Molecular Biology and Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104
5 Department of Pathology, Case Western Reserve University School of Medicine, Cleveland, OH 44106 (john.lowe{at}case.edu)

6 Address Correspondence to: Richard D. Cummings, Ph.D., Department of Biochemistry, Emory University School of Medicine, O. Wayne Rollins Research Center, 1510 Clifton Road, Suite 4001, Atlanta, GA 30322, Tel: 404-727-5962 (main office), Fax: 404-727-2738, email: rdcummi{at}emory.edu

Received on January 17, 2008; accepted on February 27, 2008

Leukocyte trafficking involves specific recognition between P-selectin and L-selectin and PSGL-1 containing core 2-based O-glycans expressing sialyl Lewis x antigen (SLex). However, the structural identity of the glycan component(s) displayed by murine neutrophil PSGL-1 that contribute to its P-selectin counter-receptor activity has been uncertain, since these cells express little if any SLex, 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 SLex antigen.

Key words: P-selectin / PSGL-1 / murine / O-glycan / Sialyl Lewis x

2 Current Address: Selexys Pharmaceuticals Corp., 800 Research Parkway Suite, 338 Oklahoma City, OK 73104; email: zskawar@hotmail.com

3 Current Address: Department of Biochemistry, Emory University School of Medicine, O. Wayne Rollins Research Center, 1510 Clifton Road, Suite 4001, Atlanta, GA 30322; email: tkjohns@emory.edu

4 Current Address: Cell Surface Analytics Laboratory, Research and Development, Finnish Red Cross Blood Service, Kivihaantie 7, 00310 Helsinki, Finland; email: suvi.natunen@bts.redcross.fi


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