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Colon Cancer Mucin: A New Ligand for the ß-Galactoside-binding Protein Galectin-3¹

Department of Medicine, Henry Ford Health Sciences Center, Detroit, Michigan 48202 [R. S. B., J. C. B.]; Department of Medicine, University of Michigan School of Medicine, Ann Arbor, Michigan 48109 [R. S. B.]; and Tumor Progression and Metastasis Program and Departments of Pathology and Radiation Oncology, Karmanos Cancer Foundation, Wayne State University School of Medicine, Detroit, Michigan 48201 [L. W., A. R.]

Galectin-3, an endogenous ß-galactoside-binding lectin, is present on colon cancer cells and may play a role in metastasis. Galectin-3 binds poly-N-acetyllactosamine structures on glycoproteins, but its natural ligands remain to be fully defined. Galectin-3 bound to purified native and desialylated colon cancer mucin in a concentration-dependent manner, which was completely inhibited by 0.1 M lactose, the competitive inhibitory sugar for this protein. Mucin purified from highly metastatic LS-Lim6 human colon cancer cells bound galectin-3 to 2-fold greater extent than mucin from low-metastatic parental cell line LS174T. Desialylation increased binding to mucin >4-fold. Mucin purified from LS-B colon cancer cells is fully glycosylated and bound >40-fold more galectin-3 than mucin purified from clonal cell line LS-C, which produces mucin lacking peripheral carbohydrate structures. Endogenous galectin-3 was detected by Western analysis in all cell lines, and its expression was related to mucin production and metastatic capacity. When serum from a patient with metastatic colorectal cancer was chromatographed on Superose 6, >70% of galectin-3 ligand was identified as circulating mucin. Colon cancer mucin is a newly identified ligand for galectin-3, and binding of galectin-3 to mucins depends on peripheral carbohydrate structures. Binding of this endogenous lectin to mucins may influence cellular interactions that play a role in colon cancer metastasis.

¹ This work was supported in part by the Research Service of the Henry Ford Health Sciences Center and Research Foundation (R. S. B.), National Cancer Institute Grants 1R01CA69480 (R. S. B.) and 2R01CA46120 (A. R.), and the Paul Zuckerman Support Foundation for Cancer Research (A. R.).

² To whom requests for reprints should be addressed, at Henry Ford Health Sciences Center, 2799 West Grand Boulevard, Detroit MI 48202, Fax: (313) 876-9487.

Received 6/12/96. Accepted 8/16/96.

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