J. Biochem, 2003, Vol. 134, No. 6 869-874
© 2003 Japanese Biochemical Society
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Galectin-1 Induces Cell Adhesion to the Extracellular Matrix and Apoptosis of Non-Adherent Human Colon Cancer Colo201 Cells
1 Department of Biotechnology, Kyoto Institute of Technology, Kyoto 606-8585; 2 Department of Public Health, Kansai Medical University, Moriguchi 570-8506; and 3 Department of Biotechnology, Kyoto Sangyo University, Kyoto 603-8555
To isolate cDNAs for molecules involved in cell adhesion to the extracellular matrix, expression cloning with non-adherent colon cancer Colo201 cells was carried out. Four positive clones were isolated and, when sequenced, one was found to be galectin-1, a ß-galactosidebinding protein. When cultured on fibronectin-, laminin-, and collagen-coated and non-coated dishes, the adherent galectin-1 cDNA-transfected Colo201 cells increased and spread somewhat. Immunofluorescence staining revealed that galectin-1 was expressed inside and outside of Colo201 cells. The adhesion was dependent on the carbohydrate-recognition domain of galectin-1 since lactose inhibited the adhesion and exogenously-added galectin-1 caused the adhesion. PD58059, an inhibitor of mitogen-activated protein kinase, or LY294002, a phosphoinositide 3-OH kinase inhibitor, decreased the adhesion. Furthermore, the expression of galectin-1 in Colo201 cells induced apoptotic cell death, while exogenously-added galectin-1 did not cause apoptosis. These results indicate that galectin-1 plays a role in both cellmatrix interactions and the inhibition of Colo201 cell proliferation, and suggest that galectin-1 expressed in cells could be associated with apoptosis.
* To whom correspondence should be addressed. Tel: +81-75-724-7789, Fax: +81-75-724-7760, E-mail: taketani{at}ipc.kit.ac.jp
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