Počet záznamů: 1  

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

  1. 1.
    0543839 - FGÚ 2022 RIV CH eng J - Článek v odborném periodiku
    Sedlář, Antonín - Trávníčková, Martina - Bojarová, Pavla - Vlachová, Miluše - Slámová, Kristýna - Křen, Vladimír - Bačáková, Lucie
    Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells.
    International Journal of Molecular Sciences. Roč. 22, č. 10 (2021), č. článku 5144. E-ISSN 1422-0067
    Grant CEP: GA MŠk(CZ) LM2018129; GA MŠk(CZ) EF18_046/0016045; GA ČR(CZ) GA18-01163S; GA MŠk(CZ) LTC18041; GA MŠk(CZ) LTC18038
    Institucionální podpora: RVO:67985823 ; RVO:61388971
    Klíčová slova: galectin * HUVEC * ADSC * integrin * carbohydrate
    Obor OECD: Biomaterials (as related to medical implants, devices, sensors); Biomaterials (as related to medical implants, devices, sensors) (MBU-M)
    Impakt faktor: 6.208, rok: 2021
    Způsob publikování: Open access
    https://www.mdpi.com/1422-0067/22/10/5144

    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.
    Trvalý link: http://hdl.handle.net/11104/0320954

     
     
Počet záznamů: 1