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Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells
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SYSNO ASEP 0543839 Document Type J - Journal Article R&D Document Type Journal Article Subsidiary J Článek ve WOS Title Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells Author(s) Sedlář, Antonín (FGU-C) ORCID
Trávníčková, Martina (FGU-C) RID, ORCID, SAI
Bojarová, Pavla (MBU-M) ORCID
Vlachová, Miluše (MBU-M) ORCID
Slámová, Kristýna (MBU-M) RID, ORCID
Křen, Vladimír (MBU-M) RID, ORCID
Bačáková, Lucie (FGU-C) RID, ORCIDArticle number 5144 Source Title International Journal of Molecular Sciences. - : MDPI - ISSN 1422-0067
Roč. 22, č. 10 (2021)Number of pages 26 s. Language eng - English Country CH - Switzerland Keywords galectin ; HUVEC ; ADSC ; integrin ; carbohydrate Subject RIV EI - Biotechnology ; Bionics OECD category Biomaterials (as related to medical implants, devices, sensors) Subject RIV - cooperation Institute of Microbiology - Biotechnology ; Bionics R&D Projects LM2018129 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) EF18_046/0016045 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) GA18-01163S GA ČR - Czech Science Foundation (CSF) LTC18041 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) LTC18038 GA MŠMT - Ministry of Education, Youth and Sports (MEYS) Method of publishing Open access Institutional support FGU-C - RVO:67985823 ; MBU-M - RVO:61388971 UT WOS 000662006700001 EID SCOPUS 85105699642 DOI https://doi.org/10.3390/ijms22105144 Annotation Galectin-3 (Gal-3) is a beta-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 beta-galactoside LacdiNAc (GalNAc beta 1,4GlcNAc), 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 beta 1 and alpha V integrins-namely alpha 5 beta 1, alpha V beta 3, and alpha V beta 1 integrins. Workplace Institute of Physiology Contact Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Year of Publishing 2022 Electronic address https://www.mdpi.com/1422-0067/22/10/5144
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