TY - JOUR AU - Blaskó, Andrea AU - Tóth, Béla Ernő TI - A COVID-19 betegség klinikai lefolyása a D-vitamin-ellátottság tükrében JF - ORVOSTOVÁBBKÉPZŐ SZEMLE J2 - ORVOSTOVÁBBKÉPZŐ SZLE VL - 28 PY - 2021 IS - 2 SP - 57 EP - 63 PG - 7 SN - 1218-2583 UR - https://m2.mtmt.hu/api/publication/31996560 ID - 31996560 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Tóth, Béla Ernő AU - Blaskó, Andrea TI - A D-vitamin feltételezett szerepe a COVID-19-pandémia és más vírusfertőzések megelőzésében és kimenetelében JF - HÁZIORVOS TOVÁBBKÉPZŐ SZEMLE J2 - HÁZIORVOS TOVÁBBKÉPZŐ SZEMLE VL - 25 PY - 2020 SP - 303 SN - 1219-8641 UR - https://m2.mtmt.hu/api/publication/31996592 ID - 31996592 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Fajka-Boja, Roberta AU - Suhajdáné Urbán, Veronika AU - Szebeni, Gábor AU - Czibula, Ágnes AU - Blaskó, Andrea AU - Kriston-Pál, Éva AU - Makra, Ildikó AU - Hornung, Ákos AU - Szabó, Enikő AU - Uher, Ferenc AU - Than, Nándor Gábor AU - Monostori, Éva TI - Galectin-1 is a local but not systemic immunomodulatory factor in mesenchymal stromal cells JF - CYTOTHERAPY J2 - CYTOTHERAPY VL - 18 PY - 2016 IS - 3 SP - 360 EP - 370 PG - 11 SN - 1465-3249 DO - 10.1016/j.jcyt.2015.12.004 UR - https://m2.mtmt.hu/api/publication/3024122 ID - 3024122 AB - BACKGROUND AIMS: Mesenchymal stromal cells (MSCs) have powerful immunosuppressive activity. This function of MSCs is attributed to plethora of the expressed immunosuppressive factors, such as galectin-1 (Gal-1), a pleiotropic lectin with robust anti-inflammatory effect. Nevertheless, whether Gal-1 renders or contributes to the immunosuppressive effect of MSCs has not been clearly established. Therefore, this question was the focus of a complex study. METHODS: MSCs were isolated from bone marrows of wild-type and Gal-1 knockout mice and their in vitro anti-proliferative and apoptosis-inducing effects on activated T cells were examined. The in vivo immunosuppressive activity was tested in murine models of type I diabetes and delayed-type hypersensitivity. RESULTS: Both Gal-1-expressing and -deficient MSCs inhibited T-cell proliferation. Inhibition of T-cell proliferation by MSCs was mediated by nitric oxide but not PD-L1 or Gal-1. In contrast, MSC-derived Gal-1 triggered apoptosis in activated T cells that were directly coupled to MSCs, representing a low proportion of the T-cell population. Furthermore, absence of Gal-1 in MSCs did not affect their in vivo immunosuppressive effect. CONCLUSIONS: These results serve as evidence that Gal-1 does not play a role in the systemic immunosuppressive effect of MSCs. However, a local contribution of Gal-1 to modulation of T-cell response by direct cell-to-cell interaction cannot be excluded. Notably, this study serves a good model to understand how the specificity of a pleiotropic protein depends on the type and localization of the producing effector cell and its target. LA - English DB - MTMT ER - TY - PAT AU - Szebeni, Gábor AU - Monostori, Éva AU - Uher, F AU - Fajka-Boja, R AU - Gercso, A AU - Martinek, Tamás AU - Tubak, Vilmos AU - Blaskó, Andrea AU - Kovacs, Solyom F AU - Joó, Gabriella AU - Blazsó, Péter AU - Krenacs, L AU - Katona, R TI - Tumorellenes anyagok szállítása szolid tumorokba CY - Country:10001(1) PY - 2011 UR - https://m2.mtmt.hu/api/publication/3184448 ID - 3184448 LA - Hungarian DB - MTMT ER - TY - THES AU - Blaskó, Andrea TI - Szolubilis és sejteredetű galektin-1 által kiváltott T sejt apoptózis mechanizmusa; egy összehasonlító tanulmány a galektin-1 fiziológiás hatásának meghatározására PB - Szegedi Tudományegyetem (SZTE) PY - 2011 SP - 98 DO - 10.14232/phd.702 UR - https://m2.mtmt.hu/api/publication/2774048 ID - 2774048 LA - Hungarian DB - MTMT ER - TY - JOUR AU - Blaskó, Andrea AU - Fajka-Boja, Roberta AU - Ion, Gabriella AU - Monostori, Éva TI - How does it act when soluble? Critical evaluation of mechanism of galectin-1 induced T-cell apoptosis JF - ACTA BIOLOGICA HUNGARICA (1983-2018) J2 - ACTA BIOL HUNG VL - 62 PY - 2011 SP - 106 EP - 111 PG - 6 SN - 0236-5383 DO - 10.1556/ABiol.61.2011.1.11 UR - https://m2.mtmt.hu/api/publication/1921569 ID - 1921569 N1 - Megjegyzés-21919647 Chemicals/CAS: caspase 3, 169592-56-7; caspase 9, 180189-96-2; galectin 1, 258495-34-0; protein kinase ZAP 70, 148047-34-1 Megjegyzés-21955779 Chemicals/CAS: caspase 3, 169592-56-7; caspase 9, 180189-96-2; galectin 1, 258495-34-0; protein kinase ZAP 70, 148047-34-1; Caspases, 3.4.22.-; Galectin 1 Megjegyzés-22193508 DI: 10.1556/ABiol.61.2011.1.11 Megjegyzés-22175937 DI: 10.1556/ABiol.61.2011.1.11 LA - English DB - MTMT ER - TY - JOUR AU - Kovács, Ferenc AU - Blaskó, Andrea AU - Fajka-Boja, Roberta AU - Katona, Róbert László AU - Végh, Lea AU - Novák, Julianna AU - Szebeni, Gábor AU - Krenács, László AU - Uher, Ferenc AU - Tubak, Vilmos AU - Kiss, R AU - Monostori, Éva TI - Mechanism of tumor cell-induced T-cell apoptosis mediated by galectin-1 JF - IMMUNOLOGY LETTERS J2 - IMMUNOL LETT VL - 127 PY - 2010 IS - 2 SP - 108 EP - 118 PG - 11 SN - 0165-2478 DO - 10.1016/j.imlet.2009.10.003 UR - https://m2.mtmt.hu/api/publication/1303865 ID - 1303865 N1 - Megjegyzés-22175938 DI: 10.1016/j.imlet.2009.10.003 Megjegyzés-22193511 DI: 10.1016/j.imlet.2009.10.003 Megjegyzés-20893666 UR: http://www.scopus.com/inward/record.url?eid=2-s2.0-71649092570&partnerID=40&md5=5bd1ae42d9e527aefe59878f02f5d515 Megjegyzés-21955783 Chemicals/CAS: caspase, 186322-81-6; galectin 1, 258495-34-0; protein kinase Lck, 114051-78-4; protein kinase ZAP 70, 148047-34-1; Caspases, 3.4.22.-; Galectin 1; Lymphocyte Specific Protein Tyrosine Kinase p56(lck), 2.7.10.2; Neoplasm Proteins; RNA, Small Interfering; ZAP-70 Protein-Tyrosine Kinase, 2.7.10.2 Institute of Genetics, Biological Research Center, Hungarian Academy of Sciences, Temesvári krt. 62, H-6726 Szeged, Hungary Laboratory of Tumor Pathology and Molecular Diagnostics, Hungary Stem Cell Biology, National Blood Service, Hungary Institute of Biochemistry, Biological Research Center, Hungarian Academy of Sciences, Hungary Laboratory of Toxicology, Institute of Pharmacy, Université Libre de Bruxelles (ULB), Brussels, Belgium Cited By :53 Export Date: 10 February 2021 CODEN: IMLED Correspondence Address: Monostori, E.; Institute of Genetics, Temesvári krt. 62, H-6726 Szeged, Hungary; email: monos@brc.hu AB - Galectin-1 (Gal-1) has been implicated in tumor progression partly via the induction of T-cell apoptosis. However the mechanism of Gal-1 induced T-cell death was mostly studied using recombinant, soluble Gal-1 producing controversial results. To explore the true mechanism of Gal-1 and hence tumor cell-induced T-cell death, we applied co-cultures of tumor cells and T-cells thus avoiding artificial circumstances generated using recombinant protein. T-cells died when co-cultured with Gal-1-expressing but survived with Gal-1 non-expressing tumor cells. Removing tumor cell surface Gal-1 or knocking down Gal-1 expression resulted in diminution of T-cell apoptosis. Gal-1 transgenic or soluble Gal-1 treated HeLa cells became cytotoxic. Stimulation of apoptosis required interaction between the tumor and T-cells, presence of p56lck and ZAP70, decrease of mitochondrial membrane potential and caspase activation. Hence tumor cell-derived Gal-1 might efficiently contribute to tumor self-defense. Moreover this system resolves the discrepancies obtained using recombinant Gal-1 in T-cell apoptosis studies. © 2009 Elsevier B.V. All rights reserved. LA - English DB - MTMT ER - TY - JOUR AU - Fajka-Boja, Roberta AU - Blaskó, Andrea AU - Kovács-Sólyom, F AU - Szebeni, Gábor AU - Tóth, Gábor AU - Monostori, Éva TI - Co-localization of galectin-1 with GM1 ganglioside in the course of its clathrin- and raft-dependent endocytosis JF - CELLULAR AND MOLECULAR LIFE SCIENCES J2 - CELL MOL LIFE SCI VL - 65 PY - 2008 IS - 16 SP - 2586 EP - 2593 PG - 8 SN - 1420-682X DO - 10.1007/s00018-008-8143-x UR - https://m2.mtmt.hu/api/publication/1303868 ID - 1303868 N1 - Megjegyzés-22175944 DI: 10.1007/s00018-008-8143-x Megjegyzés-22193519 DI: 10.1007/s00018-008-8143-x Megjegyzés-21955794 Chemicals/CAS: galectin 1, 258495-34-0; ganglioside GM1, 37758-47-7; leukosialin, 123897-54-1; Antigens, CD7; Clathrin; G(M1) Ganglioside, 37758-47-7; Galectin 1; Ligands AB - Mammalian galectin-1 (Gal-1), a β-galactoside-binding lectin has a prominent role in regulating cell adhesion, cell growth and immune responses. Downregulation of these biological functions may occur via internalization of Gal-1. In the present study we have investigated the mechanism and possible mediator(s) of Gal- 1 endocytosis. We show that internalization occurs at a temperature higher than 22°C in an energy dependent fashion. After one hour incubation Gal-1 localizes in the Golgi system within the cells, and then disappears without accumulation in degradation compartments, such as lysosomes. Based on their strong intracellular co-localization, two glycoconjugates, GM1 ganglioside and CD7 are implicated in the sorting of internalized Gal-1 into Golgi. Other known Gal-1 binding glycoproteins on T cells (CD2, CD3, CD43 and CD45) do not cointernalize with the lectin. Internalization of Gal-1 depends on its lectin activity and follows dual pathways involving clathrin-coated vesicles and raft-dependent endocytosis. © 2008 Birkhaueser. LA - English DB - MTMT ER -