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First published online 15 September 2009
doi: 10.1242/jcs.045674

Journal of Cell Science 122, 3684-3693 (2009)
Published by The Company of Biologists 2009
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Research Article

Galectin-3 promotes lamellipodia formation in epithelial cells by interacting with complex N-glycans on {alpha}3β1 integrin

Chandrassegar Saravanan1,2, Fu-Tong Liu3, Ilene K. Gipson4 and Noorjahan Panjwani1,2,*

1 Program in Cell, Molecular and Developmental Biology, Sackler School of Graduate Biomedical Sciences, Tufts University School of Medicine, Boston, MA 02111, USA
2 Department of Ophthalmology and The New England Eye Center, Tufts University School of Medicine, Boston, MA 02111, USA
3 Department of Dermatology, School of Medicine, University of California Davis, Sacramento, CA 95817, USA
4 Schepens Eye Research Institute and Department of Ophthalmology, Harvard Medical School, Boston, MA 02116, USA

* Author for correspondence (Noorjahan.Panjwani{at}tufts.edu)

Accepted 10 August 2009

Recent studies have shown that galectin-3 (Gal-3; also known as LGALS3), a β-galactoside-binding lectin, promotes cell migration during re-epithelialization of corneal wounds. The goal of this study was to characterize the molecular mechanism by which Gal-3 stimulates cell migration. We demonstrate here that exogenous Gal-3, but not Gal-1 or Gal-8, promotes cell scattering and formation of lamellipodia in human corneal epithelial cells in a β-lactose-inhibitable manner. {alpha}3β1 integrin was identified as the major Gal-3-binding protein in corneal epithelial cells by affinity chromatography of cell lysates on a Gal-3-Sepharose column. Preincubation of cells with anti-{alpha}3 integrin function-blocking antibody significantly inhibited the induction of lamellipodia by Gal-3. Furthermore, exogenous Gal-3 activated both focal adhesion kinase, a key regulator of integrin-dependent intracellular signaling, and Rac1 GTPase, a member of the family of Rho GTPases, well known for its role in the reorganization of the actin cytoskeleton and formation of lamellipodial extensions. Experiments involving knockdown of β-1,6-N-acetylglucosaminytransferase V, an enzyme that synthesizes high-affinity glycan ligands for Gal-3, revealed that carbohydrate-mediated interaction between Gal-3 and complex N-glycans on {alpha}3β1 integrin plays a key role in Gal-3-induced lamellipodia formation. We propose that Gal-3 promotes epithelial cell migration by cross-linking MGAT5-modified complex N-glycans on {alpha}3β1 integrin and subsequently activating {alpha}3β1-integrin–Rac1 signaling to promote lamellipodia formation.

Key words: Galectin-3, {alpha}3β1 integrin, Lamellipodia, Cell migration, Epithelium


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