Galectin-3 Stimulates Cell Proliferation |
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Authors: | Hidenori Inohara Shiro Akahani Avraham Raz |
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Affiliation: | Tumor Progression and Metastasis Program, Karmanos Cancer Institute, Departments of Pathology and Radiation Oncology, Wayne State University, School of Medicine, Detroit, Michigan, 48201 |
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Abstract: | Galectin-3, a β-galactoside-binding protein, has been shown to be involved in multiple biological processes through interaction with its complementary glycoconjugates. Here we provide the first evidence of galectin-3 as a mitogen. Incubation of quiescent cultures of normal human lung fibroblast IMR-90 cells with recombinant galectin-3 (rgalectin-3) stimulated DNA synthesis as well as cell proliferation in a dose-dependent manner. This mitogenic activity was dependent on the lectin property of galectin-3, as it could be significantly inhibited by lactose, a disaccharide competitive for carbohydrate-binding by galectin-3. Chemical cross-linking and affinity-purification experiments identified binding of rgalectin-3 to cell surface glycoproteins, which were not recognized by antibodies directed against lysosome-associated membrane proteins (LAMPs), putative cellular ligands for galectin-3. Moreover, pulse–chase analysis revealed no secretion of galectin-3 by IMR-90 cells. These results indicate that galectin-3 is a mitogen capable of stimulating fibroblast cell proliferation in a paracrine fashion through interaction with cell surface glycoconjugates different from LAMPs and suggest a possible involvement of galectin-3 in tissue remodeling. |
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Keywords: | galectin-3 proliferation fibroblast lamp ligand |
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