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Originally published In Press as doi:10.1074/jbc.M803634200 on September 19, 2008
J. Biol. Chem., Vol. 283, Issue 47, 32264-32272, November 21, 2008
Galectin-3 Regulates Integrin 2β1-mediated Adhesion to Collagen-I and -IV*
Jens Friedrichs ,
Aki Manninen ,
Daniel J. Muller , and
Jonne Helenius 1
From the
Biotechnology Center, University of Technology Dresden, 01307 Dresden Germany and the Biocenter Oulu, Oulu Centre for Cell-Matrix Research, Department of Medical Biochemistry and Molecular Biology, University of Oulu, 90220 Oulu, Finland
Galectins are a taxonomically widespread family of galactose-binding proteins of which galectin-3 is known to modulate cell adhesion. Using single cell force spectroscopy, the contribution of galectin-3 to the adhesion of Madin-Darby canine kidney (MDCK) cells to different extracellular matrix proteins was investigated. When adhering to collagen-I or –IV, some cells rapidly entered an enhanced adhesion state, marked by a significant increase in the force required for cell detachment. Galectin-3-depleted cells had an increased probability of entering the enhanced adhesion state. Adhesion enhancement was specific to integrin 2β1, as it was not observed when cells adhered to extracellular matrix substrates by other integrins. The adhesion phenotype of galectin-3-depleted cells was mimicked in a galactoside-deficient MDCK cell line and could be complemented by the addition of recombinant galectin-3. We propose that galectin-3 influences integrin 2β1-mediated adhesion complex formation by altering receptor clustering.
Received for publication, May 12, 2008
, and in revised form, August 15, 2008.
* This work was supported by the Volkswagenstiftung, the AO Research Fund, the Deutsche Forschungsgemeinschaft (DFG), the Sigrid Juselius Foundation, and the Academy of Finland. 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.
1 To whom correspondence should be addressed: Tatzberg 47/49, 01307 Dresden Germany. Tel.: 0049-351-463-40306; Fax: 0049-351-463-40342; E-mail: jonne.helenius{at}biotec.tu-dresden.de.

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Copyright © 2008 by the American Society for Biochemistry and Molecular Biology.
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