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1.

001-es BibID:BIBFORM006036
Első szerző:Gáspár Rezső (biofizikus)
Cím:Effects of bretylium tosylate on voltage-gated potassium channels in human T lymphocytes / Gaspar, R., Panyi, G., Ypey, D. L., Krasznai, Z., Vereb, G., Pieri, C., Damjanovich, S.
Dátum:1994
Megjegyzések:Using the patch-clamp technique, we determined that bretylium tosylate, a quaternary ammonium compound possessing immunomodulating activity, decreased the whole-cell K+ current in human T lymphocytes, in a dose-dependent manner, in the 0.05-5 mM extracellular concentration range. Bretylium tosylate prolonged the recovery from inactivation and accelerated the inactivation and deactivation of the K+ current but did not influence the kinetics of activation or the voltage dependence of activation and steady state inactivation of the K+ conductance. The percentage of drug-induced block was independent of membrane potential. K+ channel block by bretylium tosylate was partially and slowly removable by washing with drug-free extracellular solution. Bovine serum albumin (10 mg/ml) in the bath lifted the drug-induced block almost instantaneously, although not completely. In control experiments bovine serum albumin increased the inactivation time constant of the K+ channels but left the peak K+ current amplitude unaffected. On the basis of the experimental evidence, a gating-dependent allosteric interaction is suggested for the mechanism of drug action. The effective dose range, time of exposure, and reversibility of bretylium tosylate-induced K+ channel block correlated well with the same parameters of the drug-induced inhibition of T lymphocyte activation. The reported effects of bretylium tosylate on T cell mitogenesis can be regarded partly as a consequence of its blocking effects on voltage-gated K+ channels.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Bretylium Tosylate
Cell Membrane
drug effects
Electrophysiology
Human
Hungary
In Vitro
Ion Channel Gating
Kinetics
Lymphocytes
pharmacology
physiology
Potassium
Potassium Channels
Support,Non-U.S.Gov't
T-Lymphocytes
Megjelenés:Molecular pharmacology. - 46 : 4 (1994), p. 762-766. -
További szerzők:Panyi György (1966-) (biofizikus) Ypey, Dirk L. Krasznai Zoltán (1950-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Pieri, Carlo Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:elektronikus változat
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2.

001-es BibID:BIBFORM006044
035-os BibID:(scopus)0027275867 (wos)A1993KT12800009
Első szerző:Matkó János (biológus)
Cím:Biphasic effect of extracellular ATP on the membrane potential of mouse thymocytes / Matko J., Nagy P., Panyi G., Vereb G. Jr., Bene L., Matyus L., Damjanovich S.
Dátum:1993
Megjegyzések:Extracellular ATP induced changes in the membrane potential of thymocytes from BALB/c mice were analyzed. At concentrations below 0.1 mM, ATP hyperpolarizes the cell membrane on the time scale of development of the Ca(2+)-signal. After a longer time hyperpolarization turns to depolarization. ATP concentrations higher than 0.5 mM caused rapid depolarization without previous hyperpolarization. Verapamil, quinine or the absence of extracellular Ca2+ blocked the hyperpolarization by ATP. In Na(+)-free medium the magnitude of depolarization decreased. Our data suggest a contribution of Ca(2+)-activated K+ channels to the hyperpolarizing effect of ATP at lower concentrations. The direction of membrane potential changes is determined presumably by a sensitive balance of ATP-receptor mediated Ca(2+)- and Na(+)-influx and the Ca(2+)-activated K(+)-channel activity.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Adenosine Triphosphate
Animal
Biophysics
Cell Membrane
cytology
drug effects
Hungary
Kinetics
Membrane Potentials
Mice
Mice,Inbred BALB C
pharmacology
physiology
Quinine
Support,Non-U.S.Gov't
Thymus Gland
Verapamil
Megjelenés:Biochemical and Biophysical Research Communications. - 191 : 2 (1993), p. 378-384. -
További szerzők:Nagy Péter (1971-) (biofizikus) Panyi György (1966-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Bene László (1963-) (biofizikus) Mátyus László (1956-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:elektronikus változat
DOI
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3.

001-es BibID:BIBFORM125608
035-os BibID:(Scopus)85210708535 (WoS)001364160000001
Első szerző:Medyouni, Ghofrane (biológus)
Cím:Inhibition of K+ Channels Affects the Target Cell Killing Potential of CAR T Cells / Medyouni Ghofrane, Vörös Orsolya, Jusztus Vivien, Panyi György, Vereb György, Szöőr Árpád, Hajdu Péter
Dátum:2024
ISSN:2072-6694
Megjegyzések:Ion channels of T cells (Kv1.3, KCa3.1, and CRAC) participate in the regulation of activation and effector functions via modulation of the Ca2+-dependent pathway. T cells expressing chimeric antigen receptors (CAR T cells) showed a remarkable role in anti-tumor therapy, especially in the treatment of chemotherapy-resistant liquid cancers. Nevertheless, many challenges remain to be overcome to improve the treatment for solid tumors. In this study, we assessed the expression and role of ion channels in CAR T cells. We found that HER2-specific CAR T cells had higher KCa3.1 conductance compared to the non-transduced (NT, control) cells, which was more prominent in the CD8+ population (CD4+ cell also showed elevation). Conversely, the Kv1.3 expression level was the same for all cell types (CD4+, CD8+, CAR, and NT). Single-cell Ca2+ imaging revealed that thapsigargin-induced SOCE via CRAC is suppressed in CD8+ CAR T cells, unlike for CD4+ and CD8+ NT cells. To dissect the functional role of Kv1.3 and KCa3.1, we used specific antagonists (Kv1.3: Vm24; KCa3.1: TRAM-34): the target cell elimination capacity of the CD8+ CAR T cells was improved either by blocking KCa3.1 or Kv1.3. These results imply that ion channels could be a target in CAR T cell immunotherapy elaboration.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
CAR T cells
ion channels
Kv1.3
KCa3.1
CRAC
cancer
immunotherapy
Megjelenés:Cancers. - 16 : 22 (2024), p. 1-12. -
További szerzők:Vörös Orsolya (1989-) (biotechnológus) Jusztus Vivien (1991-) (Molekuláris biológus) Panyi György (1966-) (biofizikus) Vereb György (1965-) (biofizikus, orvos) Szöőr Árpád (1984-) (orvos) Hajdu Péter (1975-) (biofizikus)
Pályázati támogatás:NKFIH K128525
Egyéb
FK132773
Egyéb
K143071
Egyéb
Stipendium Hungaricum Scholarship
Egyéb
University of Debrecen Program for Scientific Publication
Egyéb
János Bolyai Research Scholarship of the Hungarian Academy of Sciences
Egyéb
ÚNKP-20-5-DE-48
Egyéb
K143771
Egyéb
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM033278
035-os BibID:(Scopus)0029331068 (WoS)A1995TF18900001 (PMID)8588941
Első szerző:Vereb György (biofizikus, orvos)
Cím:Plasma-membrane-bound macromolecules are dynamically aggregated to form non-random codistribution patterns of selected functional elements. Do pattern recognition processes govern antigen presentation and intercellular interactions? / György Vereb, László Matyus, László Bene, György Panyi, Zsolt Bacsó, Margit Balázs, János Matkó, János Szöllősi, Rezső Gáspár, Sándor Damjanovich, Robert E. Dale, Carlo Pieri, Marcel Ameloot
Dátum:1995
Megjegyzések:Molecular recognition processes between cell surface elements are discussed with special reference to cell surface pattern formation of membrane-bound integral proteins. The existence, as detected by flow cytometric resonance energy transfer (Appendix), and significance of cell surface patterns involving the interleukin-2 receptor, the T-cell receptor-CD3 system, the intercellular adhesion molecule ICAM-1, and the major histocompatibility complex class I and class II molecules in the plasma membrane of lymphocytes are described. The modulation of antigen presentation by transmembrane potential changes is discussed, and a general role of transmembrane potential changes, and therefore of ion channel activities, adduced as one of the major regulatory mechanisms of cell-cell communication. A general role in the mediation and regulation of intercellular interactions is suggested for cell-surface macromolecular patterns. The dynamic pattern of protein and lipid molecules in the plasma membrane is generated by the genetic code, but has a remarkable flexibility and may be one of the major instruments of accommodation and recognition processes at the cellular level.
Tárgyszavak:Orvostudományok Egészségtudományok idegen nyelvű folyóiratközlemény külföldi lapban
cell surface
molecular pattern
energy transfer
fluorescence
flow cytometry
transmembrane potential
MHC
antigen presentation
intercellular communication
egyetemen (Magyarországon) készült közlemény
Megjelenés:Journal of Molecular Recognition. - 8 : 4 (1995), p. 237-246. -
További szerzők:Mátyus László (1956-) (biofizikus) Bene László (1963-) (biofizikus) Panyi György (1966-) (biofizikus) Bacsó Zsolt (1963-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Matkó János (1952-) (biológus) Szöllősi János (1953-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Dale, Robert E. Pieri, Carlo Ameloot, Marcel
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5.

001-es BibID:BIBFORM006057
Első szerző:Vereb György (biofizikus, orvos)
Cím:Effect of cyclosporin A on the membrane potential and Ca2+ level of human lymphoid cell lines and mouse thymocytes / György Vereb Jr., György Panyi, Margit Balázs, László Mátyus, János Matkó, Sándor Damjanovich
Dátum:1990
ISSN:0005-2728
Megjegyzések:The effect of the immunosuppressive cyclosporin A (CsA) on the cytosolic free Ca2+ concentration ([Ca2+]i) and membrane potential of human B and T lymphoblastoid cells and mouse thymocytes was studied in order to reveal some features of the early stage of drug-cell interaction. Cytosolic free Ca2+ concentration of the cells was measured by spectrofluorimetry using indo-1 and quin2 fluorescent calcium indicators. Membrane potential was monitored in a flow cytometer with oxonol dye. CsA applied at 2-20 micrograms/ml final concentrations caused a dose-dependent, rapid, transient rise of [Ca2+]i in all cell types. This effect could be blocked by chelating the extracellular Ca2+ with EGTA but was not sensitive to Ca2+ channel blockers verapamil and nifedipine or K+ channel blocker 4-aminopyridine. A possible explanation for the calcium mobilizing effect of CsA is an ionophore-like mode of action at the cell membrane level. Besides directly interfering with mitogenic signals, the elevation of [Ca2+]i could be responsible for an initial hyperpolarization observed in CsA-treated T lymphocytes. This hyperpolarization, however, was not detectable in B lymphoblastoid cells. A further difference between B and T cells was the diverse pattern of depolarization following CsA treatment. This variance in the behaviour of T and B lymphocytes and the diversity of membrane transport systems in its background could account for the different final outcome of the drug-cell interaction.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Cyclosporin A
Indo-1
Quin2
Membrane potential
Human lymphoid cell lines
Mouse thymocytes
Megjelenés:Biochimica et Biophysica Acta (BBA). Bioenergetics. - 1019 : 2 (1990), p. 159-165. -
További szerzők:Panyi György (1966-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Mátyus László (1956-) (biofizikus) Matkó János (1952-) (biológus) Damjanovich Sándor (1936-2017) (biofizikus)
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DOI
Intézményi repozitóriumban (DEA) tárolt változa
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