TY - JOUR AU - Vishwakarma, Gayatri AU - Andrási, Melinda AU - Szabó, Dávid Ruben AU - Hajdu, Péter Béla AU - Petrilla, Vladimir AU - Petrillová, Monika AU - Legath, Jaroslav AU - Gáspár, Attila TI - Analysis of intact venom proteins with capillary zone electrophoresis - mass spectrometry JF - MICROCHEMICAL JOURNAL J2 - MICROCHEM J VL - 200 PY - 2024 PG - 8 SN - 0026-265X DO - 10.1016/j.microc.2024.110290 UR - https://m2.mtmt.hu/api/publication/34774200 ID - 34774200 N1 - Department of Inorganic and Analytical Chemistry, University of Debrecen, Egyetem ter 1., Debrecen, 4032, Hungary Department of Dental Biochemistry and Department of Biophysics and Cell Biology, University of Debrecen, Egyetem tér 1., Debrecen, 4032, Hungary Department of Biology and Physiology, University of Veterinary Medicine and Pharmacy, Košice, Slovakia Zoological Department, Zoological Garden Košice, Košice-Kavečany, Slovakia Department of General Competencies, University of Veterinary Medicine and Pharmacy, Košice, Slovakia Department of Pharmacology and Toxicology, University of Veterinary Medicine and Pharmacy, Košice, Slovakia Department of Biotechnology and Bioinformatics, Faculty of Chemistry, Rzeszow University of Technology, Rzeszow, Poland Export Date: 6 April 2024 CODEN: MICJA Correspondence Address: Gaspar, A.; Department of Inorganic and Analytical Chemistry, Egyetem ter 1., Hungary; email: gaspar@science.unideb.hu Funding details: Ministerstvo školstva, vedy, výskumu a športu Slovenskej republiky Funding details: Nemzeti Kutatási Fejlesztési és Innovációs Hivatal, NKFIH, K142134, K128525, 2022_526066, APVV - 22-0101 Funding text 1: The authors acknowledge the financial support provided for this project by the National Research, Development and Innovation Office, Hungary (K142134 (AG), K128525 (HP)), Stipendium Hungaricum (#2022_526066) and by the project APVV-22-0101 (Slovak Research and Development Agency Departmental Organization of the Ministry of Education, Science, Research and Sports of the Slovak Republic). LA - English DB - MTMT ER - TY - JOUR AU - Jusztus, Vivien AU - Medyouni, Ghofrane AU - Bagosi, Adrienn AU - Lampé, Rudolf AU - Panyi, György AU - Matolay, Orsolya AU - Maka, Eszter AU - Krasznai, Zoárd Tibor AU - Vörös, Orsolya AU - Hajdu, Péter Béla TI - Activity of Potassium Channels in CD8+ T Lymphocytes: Diagnostic and Prognostic Biomarker in Ovarian Cancer? JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 25 PY - 2024 IS - 4 SP - 1949 SN - 1661-6596 DO - 10.3390/ijms25041949 UR - https://m2.mtmt.hu/api/publication/34565926 ID - 34565926 AB - CD8+ T cells play a role in the suppression of tumor growth and immunotherapy. Ion channels control the Ca2+-dependent function of CD8+ lymphocytes such as cytokine/granzyme production and tumor killing. Kv1.3 and KCa3.1 K+ channels stabilize the negative membrane potential of T cells to maintain Ca2+ influx through CRAC channels. We assessed the expression of Kv1.3, KCa3.1 and CRAC in CD8+ cells from ovarian cancer (OC) patients (n = 7). We found that the expression level of Kv1.3 was higher in patients with malignant tumors than in control or benign tumor groups while the KCa3.1 activity was lower in the malignant tumor group as compared to the others. We demonstrated that the Ca2+ response in malignant tumor patients is higher compared to control groups. We propose that altered Kv1.3 and KCa3.1 expression in CD8+ cells in OC could be a reporter and may serve as a biomarker in diagnostics and that increased Ca2+ response through CRAC may contribute to the impaired CD8+ function. LA - English DB - MTMT ER - TY - JOUR AU - Colomer-Molera, Magalí AU - Sastre, Daniel AU - Sole Codina, Laura AU - Vallejo-Gracia, Albert AU - Navarro Perez, Maria AU - Capera-Aragones, Jesusa AU - Estadella, Irene AU - Cassinelli, Silvia AU - Panyi, György AU - Hajdu, Péter Béla AU - Tamkun, Michael M. AU - Felipe, Antonio TI - Kv1.3-dependent immune system activation is regulated by KCNE4 JF - BIOPHYSICAL JOURNAL J2 - BIOPHYS J VL - 122 PY - 2023 IS - 3 SP - 14a SN - 0006-3495 DO - 10.1016/j.bpj.2022.11.302 UR - https://m2.mtmt.hu/api/publication/33674239 ID - 33674239 LA - English DB - MTMT ER - TY - JOUR AU - Wai, Dorothy C. C. AU - Naseem, Muhammad Umair AU - Mocsár, Gábor AU - Babu Reddiar, Sanjeevini AU - Pan, Yijun AU - Csóti, Ágota AU - Hajdu, Péter Béla AU - Nowell, Cameron AU - Nicolazzo, Joseph A. AU - Panyi, György AU - Norton, Raymond S. TI - A Fluorescent Peptide Toxin for Selective Visualization of the Voltage-Gated Potassium Channel K V 1.3 JF - BIOCONJUGATE CHEMISTRY J2 - BIOCONJUGATE CHEM VL - 33 PY - 2022 IS - 11 SP - 2197 EP - 2212 PG - 16 SN - 1043-1802 DO - 10.1021/acs.bioconjchem.2c00436 UR - https://m2.mtmt.hu/api/publication/33266468 ID - 33266468 LA - English DB - MTMT ER - TY - JOUR AU - Hajdu, Péter Béla AU - Wulff, Heike AU - Niemeyer, Barbara A. AU - Szabo, Ildiko TI - Editorial: Ion Channels and Transporters in Ca2+-Dependent Functions of Lymphocytes JF - FRONTIERS IN PHYSIOLOGY J2 - FRONT PHYSIOL VL - 13 PY - 2022 PG - 3 SN - 1664-042X DO - 10.3389/fphys.2022.962110 UR - https://m2.mtmt.hu/api/publication/33103847 ID - 33103847 LA - English DB - MTMT ER - TY - JOUR AU - Sebestyén, Veronika AU - Nagy, Éva AU - Mocsár, Gábor AU - Volkó, Julianna AU - Szilágyi, Orsolya AU - Kenesei, Ádám AU - Panyi, György AU - Tóth, Katalin AU - Hajdu, Péter Béla AU - Vámosi, György TI - Role of C-Terminal Domain and Membrane Potential in the Mobility of Kv1.3 Channels in Immune Synapse Forming T Cells JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 23 PY - 2022 IS - 6 PG - 15 SN - 1661-6596 DO - 10.3390/ijms23063313 UR - https://m2.mtmt.hu/api/publication/32776876 ID - 32776876 AB - Voltage-gated Kv1.3 potassium channels are essential for maintaining negative membrane potential during T-cell activation. They interact with membrane-associated guanylate kinases (MAGUK-s) via their C-terminus and with TCR/CD3, leading to enrichment at the immunological synapse (IS). Molecular interactions and mobility may impact each other and the function of these proteins. We aimed to identify molecular determinants of Kv1.3 mobility, applying fluorescence correlation spectroscopy on human Jurkat T-cells expressing WT, C-terminally truncated (Delta C), and non-conducting mutants of mGFP-Kv1.3. Delta C cannot interact with MAGUK-s and is not enriched at the IS, whereas cells expressing the non-conducting mutant are depolarized. Here, we found that in standalone cells, mobility of Delta C increased relative to the WT, likely due to abrogation of interactions, whereas mobility of the non-conducting mutant decreased, similar to our previous observations on other membrane proteins in depolarized cells. At the IS formed with Raji B-cells, mobility of WT and non-conducting channels, unlike Delta C, was lower than outside the IS. The Kv1.3 variants possessing an intact C-terminus had lower mobility in standalone cells than in IS-engaged cells. This may be related to the observed segregation of F-actin into a ring-like structure at the periphery of the IS, leaving much of the cell almost void of F-actin. Upon depolarizing treatment, mobility of WT and Delta C channels decreased both in standalone and IS-engaged cells, contrary to non-conducting channels, which themselves caused depolarization. Our results support that Kv1.3 is enriched at the IS via its C-terminal region regardless of conductivity, and that depolarization decreases channel mobility. LA - English DB - MTMT ER - TY - JOUR AU - Vörös, Orsolya AU - Panyi, György AU - Hajdu, Péter Béla TI - Immune Synapse Residency of Orai1 Alters Ca2+ Response of T Cells JF - INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES J2 - INT J MOL SCI VL - 22 PY - 2021 IS - 21 SN - 1661-6596 DO - 10.3390/ijms222111514 UR - https://m2.mtmt.hu/api/publication/32487569 ID - 32487569 LA - English DB - MTMT ER - TY - JOUR AU - Vallejo-Gracia, Albert AU - Sastre, Daniel AU - Colomer-Molera, Magali AU - Sole, Laura AU - Navarro-Perez, Maria AU - Capera, Jesusa AU - Roig, Sara R. AU - Pedros-Gamez, Oriol AU - Estadella, Irene AU - Szilágyi, Orsolya AU - Panyi, György AU - Hajdu, Péter Béla AU - Felipe, Antonio TI - KCNE4-dependent functional consequences of Kv1.3-related leukocyte physiology JF - SCIENTIFIC REPORTS J2 - SCI REP VL - 11 PY - 2021 IS - 1 PG - 14 SN - 2045-2322 DO - 10.1038/s41598-021-94015-9 UR - https://m2.mtmt.hu/api/publication/32348330 ID - 32348330 AB - The voltage-dependent potassium channel Kv1.3 plays essential roles in the immune system, participating in leukocyte activation, proliferation and apoptosis. The regulatory subunit KCNE4 acts as an ancillary peptide of Kv1.3, modulates K+ currents and controls channel abundance at the cell surface. KCNE4-dependent regulation of the oligomeric complex fine-tunes the physiological role of Kv1.3. Thus, KCNE4 is crucial for Ca2+-dependent Kv1.3-related leukocyte functions. To better understand the role of KCNE4 in the regulation of the immune system, we manipulated its expression in various leukocyte cell lines. Jurkat T lymphocytes exhibit low KCNE4 levels, whereas CY15 dendritic cells, a model of professional antigen-presenting cells, robustly express KCNE4. When the cellular KCNE4 abundance was increased in T cells, the interaction between KCNE4 and Kv1.3 affected important T cell physiological features, such as channel rearrangement in the immunological synapse, cell growth, apoptosis and activation, as indicated by decreased IL-2 production. Conversely, ablation of KCNE4 in dendritic cells augmented proliferation. Furthermore, the LPS-dependent activation of CY15 cells, which induced Kv1.3 but not KCNE4, increased the Kv1.3-KCNE4 ratio and increased the expression of free Kv1.3 without KCNE4 interaction. Our results demonstrate that KCNE4 is a pivotal regulator of the Kv1.3 channelosome, which fine-tunes immune system physiology by modulating Kv1.3-associated leukocyte functions. LA - English DB - MTMT ER - TY - JOUR AU - Tajti, Gábor AU - Szántó, Gábor Tibor AU - Csóti, Ágota AU - Racz, G. AU - Evaristo, C. AU - Hajdu, Péter Béla AU - Panyi, György TI - Immunomagnetic separation is a suitable method for electrophysiology and ion channel pharmacology studies on T cells JF - CHANNELS J2 - CHANNELS VL - 15 PY - 2021 IS - 1 SP - 53 EP - 66 PG - 14 SN - 1933-6950 DO - 10.1080/19336950.2020.1859753 UR - https://m2.mtmt.hu/api/publication/31813030 ID - 31813030 N1 - Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, Debrecen, Hungary RD Reagents Chemical Biology, Miltenyi Biotec B.V. Co. KG, Bergisch Gladbach, Germany Department of Biophysics and Cell Biology, Faculty of Dentistry, University of Debrecen, Debrecen, Hungary Export Date: 15 January 2021 Correspondence Address: Panyi, G.; Department of Biophysics and Cell Biology, Faculty of Medicine, University of Debrecen, 1 Egyetem Ter, Life Science Bldg. 2.305, Hungary; email: panyi@med.unideb.hu AB - Ion channels play pivotal role in the physiological and pathological function of immune cells. As immune cells represent a functionally diverse population, subtype-specific functional studies, such as single-cell electrophysiology require proper subset identification and separation. Magnetic-activated cell sorting (MACS) techniques provide an alternative to fluorescence-activated cell sorting (FACS), however, the potential impact of MACS-related beads on the biophysical and pharmacological properties of the ion channels were not studied yet. We studied the aforementioned properties of the voltage-gated Kv1.3 K+ channel in activated CD4+ T-cells as well as the membrane capacitance using whole-cell patch-clamp following immunomagnetic positive separation, using the REAlease® kit. This kit allows three experimental configurations: bead-bound configuration, bead-free configuration following the removal of magnetic beads, and the label-free configuration following removal of CD4 recognizing antibody fragments. As controls, we used FACS separation as well as immunomagnetic negative selection. The membrane capacitance and of the biophysical parameters of Kv1.3 gating, voltage-dependence of steady-state activation and inactivation kinetics of the current were not affected by the presence of MACS-related compounds on the cell surface. We found subtle differences in the activation kinetics of the Kv1.3 current that could not be explained by the presence of MACS-related compounds. Neither the equilibrium block of Kv1.3 by TEA+ or charybdotoxin (ChTx) nor the kinetics of ChTx block are affected by the presence of the magnetics beads on the cell surface. Based on our results MACS is a suitable method to separate cells for studying ion channels in non-excitable cells, such as T-lymphocytes. © 2020 The Author(s). Published by Informa UK Limited, trading as Taylor & Francis Group. LA - English DB - MTMT ER - TY - CHAP AU - Szántó, Gábor Tibor AU - Mészáros, Beáta AU - Hajdu, Péter Béla AU - Tajti, Gábor AU - Panyi, György ED - Rakonczay, Zoltán ED - Kiss, Lóránd TI - KCa1.1 and Kv10.1 K+ channels are functionally expressed in chorion-derived mesenchymal stem cells T2 - Proceedings of the EFOP-3.6.2-16-2017-00006 (LIVE LONGER) project PB - University of Szeged CY - Szeged SN - 9789633067642 PY - 2020 SP - ISBN:9789633067642 UR - https://m2.mtmt.hu/api/publication/31672852 ID - 31672852 AB - Introduction: Multipotent mesenchymal stem cells (MSCs) can be found in nearly all tissues, including the placenta. Therapeutic application of placenta-derived MSCs is very promising, as this tissue type is more readily available then other sources of MSCs. The ion channel repertoire of chorion-derived MSCs (cMSC) are far less understood compared to their bone marrow-derived MSC counterparts. The mRNA expression of ion channels has already been examined in our group (Mészáros et al), so our aim in this study was to determine ion channels that are functionally expressed in cMSCs. Methods: Ionic current measurements were carried out using the patch-clamp technique in whole-cell configuration. For pharmacological investigations a gravity-controlled perfusion system was used. Results: A TTX sensitive sodium current was measured in cMSCs. This Na+ current was insensitive to the Nav1.7-specific inhibitor, ProTx-II. The outward K+ current was produced by multiple ion channels. The expression of Kv10.1 and KCa1.1 channels were confirmed based on either their characteristic biophysical properties or pharmacological features (i.e using the Kv10.1 inhibitor astemizole, or the subunit independent KCa1.1 blocker paxilline). Moreover, the expression of KCa1.1 associated β-subunits (β1, β3b and β3d) were identified on cMSCs using -subunit dependent inhibitor (iberiotoxin) and activators (arachidonic and lithocholic acid). Conclusions: Our results strongly suggest that Na+ and K+ channels are functionally expressed in cMSCs, similar to their bone marrow-derived MSC counterparts. Pharmacological targeting of these channels may serve as a tool to alter cMSC functions. Acknowledgements: This work was supported by EFOP 3.6.2-16-2017-00006 (LIVE LONGER). LA - English DB - MTMT ER -