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Glycobiology Advance Access originally published online on June 26, 2009
Glycobiology 2009 19(12):1402-1407; doi:10.1093/glycob/cwp077
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© The Author 2009. Published by Oxford University Press. All rights reserved. For permissions, please e-mail: journals.permissions@oxfordjournals.org

Galectin-1 stimulates monocyte chemotaxis via the p44/42 MAP kinase pathway and a pertussis toxin-sensitive pathway

Reshad K J Malik, Rohit R Ghurye, Diana J Lawrence-Watt and Helen J S Stewart1

Brighton and Sussex Medical School, University of Sussex, Falmer, Brighton BN1 9PS, UK

1 To whom correspondence should be addressed: Tel: +44-1273-877886; Fax: +44-1273-877884; e-mail: H.J.S.Stewart{at}sussex.ac.uk

Received on September 19, 2008; revised on May 27, 2009; accepted on May 28, 2009

Galectin-1, the prototype of a family of β-galactoside-binding proteins, has been implicated in a wide variety of biological processes. Data presented herein show that galectin-1 stimulates monocyte migration in a dose-dependent manner but is not chemotactic for macrophages. Galectin-1-induced monocyte chemotaxis is blocked by lactose and inhibited by an anti-galectin-1 antibody but not by nonspecific antibodies. Furthermore, galectin-1-mediated monocyte migration was significantly inhibited by MEK inhibitors in a rapid, time-dependent manner suggesting that MAP kinase pathways are involved in galectin-1. Migration was also almost completely blocked by pertussis toxin implying G-protein involvement in the galectin-1-induced chemotaxis. These results demonstrate a role for galectin-1 in monocyte chemotaxis which differs from galectin-3 in that macrophages are nonresponsive. Furthermore, our observations suggest that galectin-1 may be involved in chemoattraction at sites of inflammation in vivo and may contribute to disease processes such as atherosclerosis.

Key words: chemotaxis / galectin-1 / monocytes / signal transduction


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