Glycobiology Advance Access originally published online on July 16, 2008
Glycobiology 2008 18(10):770-778; doi:10.1093/glycob/cwn066
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Galectin-1 signaling in leukocytes requires expression of complex-type N-glycans
4 Cardiovascular Biology Research Program, Oklahoma Medical Research Foundation
5 Department of Biochemistry and Molecular Biology, Oklahoma Center for Medical Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma City, OK 73104, USA
1 To whom correspondence should be addressed: Tel: +1-405-271-6480; Fax: +1-405-271-3137; e-mail: rodger-mcever{at}omrf.org
Received on March 3, 2008; revised on June 26, 2008; accepted on July 8, 2008
Dimeric 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 / inflammation / leukocytes / N-glycans / signaling
2 Present address: Department of Medicine, University of Massachusetts Medical School, Worcester, MA 01605, USA.
3 Present address: Department of Biochemistry, Emory University School of Medicine, Atlanta, GA 30322, USA.