Počet záznamů: 1
Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells
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SYSNO ASEP 0543839 Druh ASEP J - Článek v odborném periodiku Zařazení RIV J - Článek v odborném periodiku Poddruh J Článek ve WOS Název Interaction between Galectin-3 and Integrins Mediates Cell-Matrix Adhesion in Endothelial Cells and Mesenchymal Stem Cells Tvůrce(i) 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, ORCIDČíslo článku 5144 Zdroj.dok. International Journal of Molecular Sciences. - : MDPI
Roč. 22, č. 10 (2021)Poč.str. 26 s. Jazyk dok. eng - angličtina Země vyd. CH - Švýcarsko Klíč. slova galectin ; HUVEC ; ADSC ; integrin ; carbohydrate Vědní obor RIV EI - Biotechnologie a bionika Obor OECD Biomaterials (as related to medical implants, devices, sensors) Vědní obor RIV – spolupráce Mikrobiologický ústav - Biotechnologie a bionika CEP LM2018129 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy EF18_046/0016045 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy GA18-01163S GA ČR - Grantová agentura ČR LTC18041 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy LTC18038 GA MŠMT - Ministerstvo školství, mládeže a tělovýchovy Způsob publikování Open access Institucionální podpora FGU-C - RVO:67985823 ; MBU-M - RVO:61388971 UT WOS 000662006700001 EID SCOPUS 85105699642 DOI 10.3390/ijms22105144 Anotace 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. Pracoviště Fyziologický ústav Kontakt Lucie Trajhanová, lucie.trajhanova@fgu.cas.cz, Tel.: 241 062 400 Rok sběru 2022 Elektronická adresa https://www.mdpi.com/1422-0067/22/10/5144
Počet záznamů: 1