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Article

Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells

1
Laboratory of Biomaterials and Tissue Engineering, Institute of Physiology of the Czech Academy of Sciences, Vídeňská 1083, CZ 142 20 Prague 4, Czech Republic
2
Department of Physiology, Faculty of Science, Charles University, Viničná 7, CZ 128 44 Prague 2, Czech Republic
3
Laboratory of Biotransformation, Institute of Microbiology of the Czech Academy of Sciences, Vídeňská 1083, CZ 142 20 Prague 4, Czech Republic
4
Department of Health Care Disciplines and Population Protection, Faculty of Biomedical Engineering, Czech Technical University in Prague, Nám. Sítná, CZ 272 01 Kladno, Czech Republic
*
Authors to whom correspondence should be addressed.
Academic Editor: Sonia Melino
Int. J. Mol. Sci. 2021, 22(10), 5144; https://doi.org/10.3390/ijms22105144
Received: 23 February 2021 / Revised: 7 May 2021 / Accepted: 9 May 2021 / Published: 13 May 2021
(This article belongs to the Special Issue Glycoconjugates and Glycomimetics for Targeting Lectins)
Galectin-3 (Gal-3) is a β-galactoside-binding protein that influences various cell functions, including cell adhesion. We focused on the role of Gal-3 as an extracellular ligand mediating cell-matrix adhesion. We used human adipose tissue-derived stem cells and human umbilical vein endothelial cells that are promising for vascular tissue engineering. We found that these cells naturally contained Gal-3 on their surface and inside the cells. Moreover, they were able to associate with exogenous Gal-3 added to the culture medium. This association was reduced with a β-galactoside LacdiNAc (GalNAcβ1,4GlcNAc), a selective ligand of Gal-3, which binds to the carbohydrate recognition domain (CRD) in the Gal-3 molecule. This ligand was also able to detach Gal-3 newly associated with cells but not Gal-3 naturally present on cells. In addition, Gal-3 preadsorbed on plastic surfaces acted as an adhesion ligand for both cell types, and the cell adhesion was resistant to blocking with LacdiNAc. This result suggests that the adhesion was mediated by a binding site different from the CRD. The blocking of integrin adhesion receptors on cells with specific antibodies revealed that the cell adhesion to the preadsorbed Gal-3 was mediated, at least partially, by β1 and αV integrins—namely α5β1, αVβ3, and αVβ1 integrins. View Full-Text
Keywords: galectin; HUVEC; ADSC; integrin; carbohydrate galectin; HUVEC; ADSC; integrin; carbohydrate
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MDPI and ACS Style

Sedlář, A.; Trávníčková, M.; Bojarová, P.; Vlachová, M.; Slámová, K.; Křen, V.; Bačáková, L. Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells. Int. J. Mol. Sci. 2021, 22, 5144. https://doi.org/10.3390/ijms22105144

AMA Style

Sedlář A, Trávníčková M, Bojarová P, Vlachová M, Slámová K, Křen V, Bačáková L. Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells. International Journal of Molecular Sciences. 2021; 22(10):5144. https://doi.org/10.3390/ijms22105144

Chicago/Turabian Style

Sedlář, Antonín, Martina Trávníčková, Pavla Bojarová, Miluše Vlachová, Kristýna Slámová, Vladimír Křen, and Lucie Bačáková. 2021. "Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells" International Journal of Molecular Sciences 22, no. 10: 5144. https://doi.org/10.3390/ijms22105144

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