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J. Biol. Chem., Vol. 282, Issue 40, 29375-29383, October 5, 2007

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Contributions of Galectin-3 and -9 to Epithelial Cell Adhesion Analyzed by Single Cell Force Spectroscopy^*

Jens Friedrichs¹, Juha M. Torkko¹, Jonne Helenius, Terhi P. Teräväinen^¶, Joachim Füllekrug^||, Daniel J. Muller, Kai Simons, and Aki Manninen^¶2

From the Max Planck Institute of Molecular Cell Biology and Genetics, 01307 Dresden, Germany, the Biotechnology Center, Dresden University of Technology, 01307 Dresden, Germany, the ^||Department of Internal Medicine IV (Gastroenterology), University of Heidelberg, 69120 Heidelberg, Germany, and ^¶Biocenter Oulu, Department of Medical Biochemistry and Molecular Biology, University of Oulu, P.O. Box 5000, FIN-90014 Oulu, Finland

Galectins are widely expressed in epithelial tissues and have been implicated in a variety of cellular processes, including adhesion and polarization. Here we studied the contributions of galectins in cell adhesion and cyst formation of Madin-Darby canine kidney cells. Quantitative single cell force spectroscopy and standard adhesion assays were employed to study both early (<2 min) and long term (90 min) adhesion of cells to different extracellular matrix components. Inhibitors were used to examine the contribution of integrins and galectins in general and RNA interference to specifically address the role of two abundantly expressed galectins, galectin-3 and -9. We found that both galectin-3 and -9 were required for optimal long term cell adhesion to both collagen I and laminin-111. Early adhesion to laminin was found to be integrin-independent and was instead mediated by carbohydrate interactions and galectin-3 and -9. The opposite was observed for early adhesion to collagen. Although similar, the contributions of galectin-3 and -9 to adhesion appeared to be by distinct processes. These defects in adhesion of the two galectin knockdown cell lines may underlie the epithelial phenotypes observed in the cyst assays. Our findings emphasize the complex regulation of epithelial cell functions by galectins.

Received for publication, March 2, 2007 , and in revised form, July 9, 2007.

^* This work was supported by Deutsche Forschungsgemeinschaft Grant MU1791/3-2, European Commission Network Grant HPRN-CT-2002-00259, the Max-Planck-Society, and Academy of Finland Grant 114330. The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

The on-line version of this article (available at http://www.jbc.org) contains supplemental Table S1 and Figs. S1–S3.

¹ These two authors contributed equally to this work.

² To whom correspondence should be addressed: Biocenter Oulu, Dept. of Medical Biochemistry and Molecular Biology, University of Oulu, P.O. Box 5000, FIN-90014 Oulu, Finland. Tel.: 358-8-537-6081; Fax: 358-8-537-6115; E-mail: aki.manninen{at}oulu.fi.

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