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Glycobiology Advance Access published online on July 16, 2008
Glycobiology, doi:10.1093/glycob/cwn066
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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.

Galectin-1 Signaling in Leukocytes Requires Expression of Complex-type N-glycans

Sougata Karmakar1,4, Sean R. Stowell2,3, Richard D. Cummings2,3 and Rodger P. McEver1,2

1 Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation
2 Department of Biochemistry and Molecular Biology, Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104

Address correspondence to: Rodger P. McEver, M.D., Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation, 825 N.E. 13th Street, Oklahoma City, OK 73104, Phone: 405-271-6480, FAX: 405-271-3137, E-mail: rodger-mcever{at}omrf.org

Received on March 3, 2008; accepted on July 8, 2008

Galectin-1 (dGal-1) is a homodimeric lectin with multiple proposed functions. Although dGal-1 binds to diverse glycans, it is unclear whether dGal-1 preferentially binds to specific subsets of glycans on cell surfaces to transmit signals. To explore this question, we selectively inhibited major glycan biosynthetic pathways in human HL60, Molt-4, and Jurkat cells. Inhibition of N-glycan processing blocked surface binding of dGal-1 and prevented dGal-1-induced Ca2+ mobilization and phosphatidylserine exposure. By contrast, inhibition of O-glycan or glycosphingolipid biosynthesis did not affect dGal-1 binding or dGal-1-induced Ca2+ mobilization and phosphatidylserine exposure. These results demonstrate that dGal-1 preferentially binds to and signals through glycoproteins containing complex-type N-glycans in at least some leukocyte subsets.

Key words: galectin / leukocytes / signaling / N-glycans / inflammation

3 Current address: Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322

4 Current address: Department of Medicine, University of Massachusetts Medical School, Worcester, MA 01605


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