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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 ASEP0543839
    Document TypeJ - Journal Article
    R&D Document TypeJournal Article
    Subsidiary JČlánek ve WOS
    TitleInteraction 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, ORCID
    Article number5144
    Source TitleInternational Journal of Molecular Sciences. - : MDPI
    Roč. 22, č. 10 (2021)
    Number of pages26 s.
    Languageeng - English
    CountryCH - Switzerland
    Keywordsgalectin ; HUVEC ; ADSC ; integrin ; carbohydrate
    Subject RIVEI - Biotechnology ; Bionics
    OECD categoryBiomaterials (as related to medical implants, devices, sensors)
    Subject RIV - cooperationInstitute of Microbiology - Biotechnology ; Bionics
    R&D ProjectsLM2018129 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 publishingOpen access
    Institutional supportFGU-C - RVO:67985823 ; MBU-M - RVO:61388971
    UT WOS000662006700001
    EID SCOPUS85105699642
    DOI10.3390/ijms22105144
    AnnotationGalectin-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.
    WorkplaceInstitute of Physiology
    ContactLucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400
    Year of Publishing2022
    Electronic addresshttps://www.mdpi.com/1422-0067/22/10/5144
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