TY - JOUR AU - Virág, László AU - Hegedűs, Csaba AU - Kovács, Katalin AU - Polgár, Zsuzsanna AU - Kókai, Endre AU - Sturniolo, Isotta AU - Demény, Máté Ágoston AU - Virág, Bernadett AU - Szabó, Éva TI - Automated high-throughput cell culture scratch assay identifies wound healing promoting and inhibiting compounds from a small compound library of redox active molecules JF - FREE RADICAL BIOLOGY AND MEDICINE J2 - FREE RADICAL BIO MED VL - 208 PY - 2023 SP - S144 EP - S144 PG - 1 SN - 0891-5849 DO - 10.1016/j.freeradbiomed.2023.10.328 UR - https://m2.mtmt.hu/api/publication/34729573 ID - 34729573 LA - English DB - MTMT ER - TY - JOUR AU - Ujlaki, Gyula AU - Kovács, Tünde AU - Vida, András AU - Kókai, Endre AU - Rauch, Boglárka AU - Schwarcz, Szandra AU - Mikó, Edit AU - Janka, Eszter AU - Sipos, Adrienn AU - Hegedűs, Csaba AU - Uray (Davis), Karen L. AU - Nagy, Péter AU - Bay, Péter TI - Identification of Bacterial Metabolites Modulating Breast Cancer Cell Proliferation and Epithelial-Mesenchymal Transition JF - MOLECULES J2 - MOLECULES VL - 28 PY - 2023 IS - 15 SN - 1420-3049 DO - 10.3390/molecules28155898 UR - https://m2.mtmt.hu/api/publication/34089348 ID - 34089348 AB - Breast cancer patients are characterized by the oncobiotic transformation of multiple microbiome communities, including the gut microbiome. Oncobiotic transformation of the gut microbiome impairs the production of antineoplastic bacterial metabolites. The goal of this study was to identify bacterial metabolites with antineoplastic properties. We constructed a 30-member bacterial metabolite library and screened the library compounds for effects on cell proliferation and epithelial-mesenchymal transition. The metabolites were applied to 4T1 murine breast cancer cells in concentrations corresponding to the reference serum concentrations. However, yric acid, glycolic acid, d-mannitol, 2,3-butanediol, and trans-ferulic acid exerted cytostatic effects, and 3-hydroxyphenylacetic acid, 4-hydroxybenzoic acid, and vanillic acid exerted hyperproliferative effects. Furthermore, 3-hydroxyphenylacetic acid, 4-hydroxybenzoic acid, 2,3-butanediol, and hydrocinnamic acid inhibited epithelial-to-mesenchymal (EMT) transition. We identified redox sets among the metabolites (d-mannitol—d-mannose, 1-butanol—butyric acid, ethylene glycol—glycolic acid—oxalic acid), wherein only one partner within the set (d-mannitol, butyric acid, glycolic acid) possessed bioactivity in our system, suggesting that changes to the local redox potential may affect the bacterial secretome. Of the nine bioactive metabolites, 2,3-butanediol was the only compound with both cytostatic and anti-EMT properties. LA - English DB - MTMT ER - TY - JOUR AU - Ráduly, Zsolt AU - Szabó, László AU - Dienes, Beatrix AU - Szentesi, Péter AU - Bana, Ágnes Viktória AU - Hajdú, Tibor AU - Kókai, Endre AU - Hegedűs, Csaba AU - Csernoch, László AU - Gönczi, Mónika TI - Migration of Myogenic Cells Is Highly Influenced by Cytoskeletal Septin7 JF - CELLS J2 - CELLS-BASEL VL - 12 PY - 2023 IS - 14 PG - 17 SN - 2073-4409 DO - 10.3390/cells12141825 UR - https://m2.mtmt.hu/api/publication/34082035 ID - 34082035 AB - Septin7 as a unique member of the GTP binding protein family, is widely expressed in the eukaryotic cells and considered to be essential in the formation of hetero-oligomeric septin complexes. As a cytoskeletal component, Septin7 is involved in many important cellular processes. However, its contribution in striated muscle physiology is poorly described. In skeletal muscle, a highly orchestrated process of migration is crucial in the development of functional fibers and in regeneration. Here, we describe the pronounced appearance of Septin7 filaments and a continuous change of Septin7 protein architecture during the migration of myogenic cells. In Septin7 knockdown C2C12 cultures, the basic parameters of migration are significantly different, and the intracellular calcium concentration change in migrating cells are lower compared to that of scrambled cultures. Using a plant cytokinin, forchlorfenuron, to dampen septin dynamics, the altered behavior of the migrating cells is described, where Septin7-depleted cells are more resistant to the treatment. These results indicate the functional relevance of Septin7 in the migration of myoblasts, implying its contribution to muscle myogenesis and regeneration. LA - English DB - MTMT ER - TY - JOUR AU - Skopál, Adrienn AU - Ujlaki, Gyula AU - Gerencsér, Attila Tibor AU - Bankó, Csaba AU - Bacsó, Zsolt AU - Ciruela, Francisco AU - Virág, László AU - Haskó, György AU - Kókai, Endre TI - Adenosine A2A Receptor Activation Regulates Niemann–Pick C1 Expression and Localization in Macrophages JF - CURRENT ISSUES IN MOLECULAR BIOLOGY J2 - CURR ISSUES MOL BIOL VL - 45 PY - 2023 IS - 6 SP - 4948 EP - 4969 PG - 22 SN - 1467-3037 DO - 10.3390/cimb45060315 UR - https://m2.mtmt.hu/api/publication/34020857 ID - 34020857 N1 - Funding Agency and Grant Number: National Research Development and Innovation Office [OTKA MB08A 84685, GINOP-2.3.2-15-2016-00020 TUMORDNS, R01GM066189]; National Research, Development and Innovation Office [K147482, GINOP-2.3.2-15-2016-00048-STAYALIVE]; National Institutes of Health [R01DK113790, R01HL158519]; [OTKA K132193] Funding text: EK received funding from National Research Development and Innovation Office OTKA MB08A 84685; LV received funding from the National Research, Development and Innovation Office grants GINOP-2.3.2-15-2016-00020 TUMORDNS, GINOP-2.3.2-15-2016-00048-STAYALIVE and National Research Development and Innovation Office OTKA K132193, K147482. GH received funding from National Institutes of Health grants R01GM066189, R01DK113790 and R01HL158519. AB - Adenosine plays an important role in modulating immune cell function, particularly T cells and myeloid cells, such as macrophages and dendritic cells. Cell surface adenosine A2A receptors (A2AR) regulate the production of pro-inflammatory cytokines and chemokines, as well as the proliferation, differentiation, and migration of immune cells. In the present study, we expanded the A2AR interactome and provided evidence for the interaction between the receptor and the Niemann–Pick type C intracellular cholesterol transporter 1 (NPC1) protein. The NPC1 protein was identified to interact with the C-terminal tail of A2AR in RAW 264.7 and IPMФ cells by two independent and parallel proteomic approaches. The interaction between the NPC1 protein and the full-length A2AR was further validated in HEK-293 cells that permanently express the receptor and RAW264.7 cells that endogenously express A2AR. A2AR activation reduces the expression of NPC1 mRNA and protein density in LPS-activated mouse IPMФ cells. Additionally, stimulation of A2AR negatively regulates the cell surface expression of NPC1 in LPS-stimulated macrophages. Furthermore, stimulation of A2AR also altered the density of lysosome-associated membrane protein 2 (LAMP2) and early endosome antigen 1 (EEA1), two endosomal markers associated with the NPC1 protein. Collectively, these results suggested a putative A2AR-mediated regulation of NPC1 protein function in macrophages, potentially relevant for the Niemann–Pick type C disease when mutations in NPC1 protein result in the accumulation of cholesterol and other lipids in lysosomes. LA - English DB - MTMT ER - TY - BOOK AU - Gerencsér, A AU - Tóth, PÁ AU - Vígh, D AU - Kókai, Endre AU - Virág, László TI - Optimization of tumor cell killing by chimeric antigen receptor expressing macrophages PY - 2023 UR - https://m2.mtmt.hu/api/publication/33806508 ID - 33806508 LA - English DB - MTMT ER - TY - JOUR AU - Skopál, Adrienn AU - Kéki, T AU - Tóth, PÁ AU - Csóka, B AU - Koscsó, B AU - Német, ZH AU - Antonioli, L AU - Ivessa, A AU - Ciruela, F AU - Virág, László AU - Haskó, György AU - Kókai, Endre TI - Cathepsin D interacts with adenosine A2A receptors in mouse macrophages to modulate cell surface localization and inflammatory signalling JF - JOURNAL OF BIOLOGICAL CHEMISTRY J2 - J BIOL CHEM VL - 298 PY - 2022 IS - 5 PG - 18 SN - 0021-9258 DO - 10.1016/j.jbc.2022.101888 UR - https://m2.mtmt.hu/api/publication/32799560 ID - 32799560 N1 - Funding Agency and Grant Number: OTKA [MB08A 84685]; National Research, Development and Innovation Office [GINOP-2.3.2-15-2016-00020-TUMORDNS, GINOP-2.3.2-152016-00048-STAYALIVE, OTKA-K132193]; National Institutes of Health [R01GM066189, R01DK113790, R01HL158519, 1 R35 GM145245]; MCIN/AEI "ERDF. A way of making Europe" [PID2020-118511RB-I00] Funding text: E. K. received funding from OTKA (grant no.: MB08A 84685). L. V. received funding from the National Research, Development and Innovation Office grants (GINOP-2.3.2-15-2016-00020-TUMORDNS, GINOP-2.3.2-152016-00048-STAYALIVE, and OTKA-K132193). G. H. received funding from the National Institutes of Health grants R01GM066189, R01DK113790, R01HL158519, and 1 R35 GM145245. Also supported by project PID2020-118511RB-I00 founded by MCIN/AEI/10.13039/501100011033 "ERDF. A way of making Europe" to F. C. The content is solely the responsibility of the authors and does not necessarily represent the official views of the National Institutes of Health. LA - English DB - MTMT ER - TY - JOUR AU - Mészáros, Beáta AU - Papp, Ferenc AU - Mocsár, Gábor AU - Kókai, Endre AU - Kovács, Katalin AU - Tajti, Gábor AU - Panyi, György TI - The voltage-gated proton channel hHv1 is functionally expressed in human chorion-derived mesenchymal stem cells JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 10 PY - 2020 IS - 1 SN - 2045-2322 DO - 10.1038/s41598-020-63517-3 UR - https://m2.mtmt.hu/api/publication/31334758 ID - 31334758 LA - English DB - MTMT ER - TY - CONF AU - Katona, Éva AU - Juhász, Tamás AU - Hajdú, Tibor AU - Nagy, Gábor AU - Kókai, Endre AU - Trencsényi, György AU - Gergely, Pál AU - Zákány, Róza TI - PP2A szerepe a SOX9/CREB trnszkriciós faktorok és a RHAMM/CD44 interakciók szabályzásában humán melanoma sejtvonalakban T2 - 48. Membrán-Transzport Konferencia PY - 2018 SP - 32 UR - https://m2.mtmt.hu/api/publication/30477500 ID - 30477500 N1 - Import hibák 2019-02-27 11:02 A besorolást az importban szereplő adat alapján nem lehetett meghatározni a következő elemhez: absztrakt LA - Hungarian DB - MTMT ER - TY - JOUR AU - Hegedüs, Éva AU - Kókai, Endre AU - Nánási, Péter Pál AU - Imre, László AU - Halász, László AU - Jossé, R AU - Antunovics, Zsuzsa AU - Webb, MR AU - Hage, AE AU - Pommier, Y AU - Székvölgyi, Lóránt AU - Dombrádi, Viktor Béla AU - Szabó, Gábor TI - Endogenous single-strand DNA breaks at RNA polymerase II promoters in Saccharomyces cerevisiae JF - NUCLEIC ACIDS RESEARCH J2 - NUCLEIC ACIDS RES VL - 46 PY - 2018 IS - 20 SP - 10649 EP - 10668 PG - 20 SN - 0305-1048 DO - 10.1093/nar/gky743 UR - https://m2.mtmt.hu/api/publication/3406102 ID - 3406102 LA - English DB - MTMT ER - TY - JOUR AU - Csóka, B AU - Törő, G AU - Vindeirinho, J AU - Varga, Zoltán AU - Koscsó, B AU - Németh, ZH AU - Kókai, Endre AU - Antonioli, L AU - Suleiman, M AU - Marchetti, P AU - Cseri, Karolina AU - Deák, Ádám AU - Virág, László AU - Pacher, Pál AU - Bay, Péter AU - Haskó, György TI - A2A adenosine receptors control pancreatic dysfunction in high-fat-diet induced obesity JF - FASEB JOURNAL J2 - FASEB J VL - 31 PY - 2017 IS - 11 SP - 4985 EP - 4997 PG - 13 SN - 0892-6638 DO - 10.1096/fj.201700398R UR - https://m2.mtmt.hu/api/publication/3247963 ID - 3247963 N1 - Department of Surgery, Center for Immunity and Inflammation, Rutgers New Jersey Medical School, 185 South Orange Ave., University Heights, Newark, NJ 07103, United States National Institute on Alcohol Abuse and Alcoholism, National Institutes of Health, Bethesda, MD, United States Department of Microbiology and Immunology, Pennsylvania State University College of Medicine, Hershey, PA, United States Department of Surgery, Morristown Memorial Medical Center, Morristown, NJ, United States Department of Medical Chemistry, Faculty of Medicine, University of Debrecen, Debrecen, Hungary Department of Operative Techniques, Surgical Research of the Institute of Surgery, University of Debrecen, Debrecen, Hungary Department of Clinical and Experimental Medicine, University of Pisa, Pisa, Italy Cell Biology and Signalling Research Group of the Hungarian Academy of Sciences, Debrecen, Hungary Cited By :24 Export Date: 9 June 2023 CODEN: FAJOE Correspondence Address: Csóka, B.; Department of Surgery, 185 South Orange Ave., United States; email: csokaba@njms.rutgers.edu Chemicals/CAS: Antigens, Differentiation; Dietary Fats; Receptor, Adenosine A2A Funding details: TéT_09-2010-0023 Funding details: GINOP-2.3.2-15-2016-00020, GINOP-2.3.2-15-2016-00048, K112336 Funding details: National Institutes of Health, NIH Funding details: National Institute on Alcohol Abuse and Alcoholism, NIAAA, ZIAAA000375 Funding details: National Institute of General Medical Sciences, NIGMS, R01GM066189 Funding details: National Institute of Diabetes and Digestive and Kidney Diseases, NIDDK, R01DK113790 Funding details: Medical Research and Materiel Command, MRMC, 09065004 Funding details: Hungarian Scientific Research Fund, OTKA, CK 78275, PD83473 Funding details: Nemzeti Kutatási, Fejlesztési és Innovációs Hivatal, GINOP-2.3.2-15-2016-00020 TUMORDNS, GINOP-2.3.2-15-2016-00048-STAYALIVE, OTKA K112336 Funding text 1: The authors thank Dr. Katalin Erdelyi (University of Debrecen) for technical assistance. This work was supported by U.S. National Institutes of Health (NIH) National Institute of General Medical Sciences Grant R01GM66189 (to G.H.), NIH National Institute of Diabetes and Digestive and Kidney Diseases Grant R01DK113790, U.S. Army Medical Research and Materiel Command Grant 09065004 (to G.H.), Hungarian Scientific Research Fund (OTKA) Grants CK 78275 (to G.H.) and PD83473 (to P.B.), the Intramural Research Program of the NIH National Institute on Alcohol Abuse and Alcoholism (to P.P.), a Bolyai fellowship (to P.B.), the Hungarian National Innovation Office (Baross Program Seahorse Grants TéT_09- 2010-0023), TA MOP-4.2.2. A-11/1/KONV-2012-0025, TAMOP- 4.2.1./B-09/KONV-2010-0007, TA MOP-4.2.2/B-10/1-2010-0024), and the Medical and Health Science Center (Mecenatura Mec-8/2011). L.V. is supported by National Research, Development and Innovation Office Grants GINOP-2.3.2-15-2016- 00020 TUMORDNS, GINOP-2.3.2-15-2016-00048-STAYALIVE, and OTKA K112336. The authors declare no conflicts of Interest. Funding text 2: The authors thank Dr. Katalin Erdelyi (University of Debrecen) for technical assistance. This work was supported by U.S. National Institutes of Health (NIH) National Institute of General Medical Sciences Grant R01GM66189 (to G.H.), NIH National Institute of Diabetes and Digestive and Kidney Diseases Grant R01DK113790, U.S. Army Medical Research and Materiel Command Grant 09065004 (to G.H.), Hungarian Scientific Research Fund (OTKA) Grants CK 78275 (to G.H.) and PD83473 (to P.B.), the Intramural Research Program of the NIH National Institute on Alcohol Abuse and Alcoholism (to P.P.), a Bolyai fellowship (to P.B.), the Hungarian National Innovation Office (Baross Program Seahorse Grants TéT_09-2010-0023), TÁMOP-4.2.2. A-11/1/KONV-2012-0025, TÁMOP-4.2.1./B-09/KONV-2010-0007, TÁMOP-4.2.2/B-10/1-2010-0024), and the Medical and Health Science Center (Mecenatura Mec-8/2011). L.V. is supported by National Research, Development and Innovation Office Grants GINOP-2.3.2-15-2016-00020 TUMORDNS, GINOP-2.3.2-15-2016-00048-STAYALIVE, and OTKA K112336. The authors declare no conflicts of Interest. LA - English DB - MTMT ER -