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1.

001-es BibID:BIBFORM006028
Első szerző:Damjanovich Sándor (biofizikus)
Cím:Dynamic physical interactions of plasma membrane molecules generate cell surface patterns and regulate cell activation processes / Damjanovich S., Mátyus L., Balázs, M., Gáspár R., Krasznai Z., Pieri C., Szöllösi J., Trón L.
Dátum:1992
Megjegyzések:Molecular interaction and transmembrane signal transducing events generate a very dynamic and ever changing "pattern" in the plasma membranes. Lymphocytes, the key functional elements of the immune system, are eminently suited to be the primary targets to investigate these proximity, mobility, or other physical-chemical changes in their plasma membranes. Recently, a number of experiments suggested that processed peptides from antigens can bind specific components of MHC molecules (Elliott et al., 1991). This is certainly a way to alter their structure. Cell surface patterns of topological nature, assembly and disassembly of oligomeric receptor structure like the IL-2 receptor have been investigated by sophisticated biophysical techniques. The dynamic changes in the two-dimensional cell surface pattern and intramolecular conformational changes within this "larger" macro-pattern may have a strong regulatory role in signal transducing and intercellular recognition processes. Recent data on these problems are presented together with brief and critical discussions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Animal
Cell Membrane
Human
Hungary
immunology
Lymphocyte Transformation
Lymphocytes
Membrane Proteins
Peptides
Signal Transduction
Megjelenés:Immunobiology. - 185 : 2-4 (1992), p. 337-349. -
További szerzők:Mátyus László (1956-) (biofizikus) Balázs Margit (1952-) (sejtbiológus, molekuláris genetikus) Gáspár Rezső (1944-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) Pieri, Carlo Szöllősi János (1953-) (biofizikus) Trón Lajos (1941-) (biofizikus)
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2.

001-es BibID:BIBFORM004645
035-os BibID:(scopus)0033552675 (wos)000084290400003
Első szerző:Damjanovich Sándor (biofizikus)
Cím:Two-dimensional receptor patterns in the plasma membrane of cells : a critical evaluation of their identification, origin and information content / Damjanovich, S., Bene, L., Matko, J., Matyus, L., Krasznai, Z., Szabo, G., Pieri, C., Gaspar, R., Szollosi, J.
Dátum:1999
Megjegyzések:A concise review is presented on the nature, possible origin and functional significance of cell surface receptor patterns in the plasma membrane of lymphoid cells. A special emphasize has been laid on the available methodological approaches, their individual virtues and sources of errors. Fluorescence energy transfer is one of the oldest available means for studying non-randomized co-distribution patterns of cell surface receptors. A detailed and critical description is given on the generation of two-dimensional cell surface receptor patterns based on pair-wise energy transfer measurements. A second hierarchical-level of receptor clusters have been described by electron and scanning force microscopies after immuno-gold-labeling of distinct receptor kinds. The origin of these receptor islands at a nanometer scale and island groups at a higher hierarchical (mum) level, has been explained mostly by detergent insoluble glycolipid-enriched complexes known as rafts, or detergent insoluble glycolipids (DIGs). These rafts are the most-likely organizational forces behind at least some kind of receptor clustering [K. Simons et al., Nature 387 (1997) 569]. These models, which have great significance in trans-membrane signaling and intra-membrane and intracellular trafficking, are accentuating the necessity to revisit the Singer-Nicolson fluid mosaic membrane model and substitute the free protein diffusion with a restricted diffusion concept.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Biophysics
Cells
Diffusion
Energy Transfer
Fluorescence
Hungary
Microscopy
Megjelenés:Biophysical Chemistry. - 82 : 2-3 (1999), p. 99-108. -
További szerzők:Bene László (1963-) (biofizikus) Matkó János (1952-) (biológus) Mátyus László (1956-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) Szabó Gábor (1953-) (biofizikus) Pieri, Carlo Gáspár Rezső (1944-) (biofizikus) Szöllősi János (1953-) (biofizikus)
Internet cím:DOI
elektronikus változat
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3.

001-es BibID:BIBFORM015989
Első szerző:Gáspár Rezső (biofizikus)
Cím:Measurement and analysis of different aspects of potassium currents in human lymphocytes / R. Gáspár, Z. Varga, Gy. Panyi, Z. Krasznai, C. Pieri, S. Damjanovich
Dátum:1998
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
Megjelenés:Signal Transduction. Single cell techniques / eds. Bert van Duijn; Anneke Wiltink. - p. 214-235.
További szerzők:Varga Zoltán (1969-) (biofizikus, szakfordító) Panyi György (1966-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) Pieri, Carlo Damjanovich Sándor (1936-2017) (biofizikus)
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4.

001-es BibID:BIBFORM006034
Első szerző:Gáspár Rezső (biofizikus)
Cím:Bretylium-induced voltage-gated sodium current in human lymphocytes / Rezső Gáspár, Zoltán Krasznai, Teréz Márián, Lajos Trón, Rina Recchioni, Marco Falasca, Fausto Moroni, Carlo Pieri, Sándor Damjanovich
Dátum:1992
ISSN:0167-4889
Megjegyzések:Using the whole-cell variation of the patch-clamp technique it has been determined that 0.25-3 mM bretylium tosylate (BT) exerts a repolarizing effect on partially depolarized human lymphocytes. The repolarizing effect was ouabain (40 microM)-sensitive, and was inhibited by the removal of external Na+ or by the Na(+)-channel-blocker amiloride (10-44 microM), but K(+)-channel-blockers 4-aminopyridine (0.1-5 mM) and quinine (100 microM) had no effect. The drug induced a sodium dependent, amiloride-sensitive transient inward current reaching its maximum value approx. 20-30 s after the administration of BT and lasting for 6-10 min. This current was activated by depolarization within 25 ms at around -42 mV, its inactivation took about 2 s and its reversal potential was +24 +/- 5 mV. An increase in the intracellular sodium concentration (1.8-3.2 mM) has been observed upon the addition of BT by monitoring the SBFI fluorescence of the dye-loaded cells. It has been shown that whole-cell K+ currents are significantly decreased by BT. The existence of voltage and ligand (BT)-gated sodium channels has been postulated in human lymphocytes. These channels are thought to participate in the initiation of membrane repolarization in human lymphocytes, and thereby influence mitogenic or antigen-induced cell-activation processes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Bretylium
Ion channel
Patch-clamp
Human lymphocyte
Megjelenés:Biochimica et Biophysica Acta (BBA). Molecular Cell Research. - 1137 : 2 (1992), p. 143-147. -
További szerzők:Krasznai Zoltán (1950-) (biofizikus) Márián Teréz (1950-) (radiobiológus) Trón Lajos (1941-) (biofizikus) Recchioni, Rina Falasca, Marco Moroni, Fausto Pieri, Carlo Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Szerző által megadott URL
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5.

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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6.

001-es BibID:BIBFORM004927
Első szerző:Gáspár Rezső (biofizikus)
Cím:Tetrodotoxin-sensitive fast Na+ current in embryonic chicken osteoclasts / Rezső Gáspár, A. Freek Weidema, Zoltán Krasznai, Peter J. Nijweide, Dirk L. Ypey
Dátum:1995
ISSN:0031-6768
Megjegyzések:A voltage-dependent, fast, transient inward current was characterized in embryonic chicken osteoclasts using the permeabilized patch configuration of the patch-clamp technique. The current was activated by depolarizations to higher than -28 +/- 4 mV from a holding potential of -80 mV. It peaked within 1-1.5 ms, and inactivated within 3.3-6.9 ms. The 50% inactivation voltage was -59 +/- 6 mV with a steepness factor of 0.11 +/- 0.06. The current disappeared with the removal of extracellular Na+ and was reversibly blocked by tetrodotoxin (K0.5 < 15 nM) but not by verapamil (< or = 100 microM). We conclude that this new current in embryonic chicken osteoclasts is a sodium current known from excitable cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animal
Chick Embryo
Culture Media
drug effects
Hungary
In Vitro
metabolism
Osteoclasts
Patch-Clamp Techniques
pharmacology
Sodium
Sodium Channels
Support,Non-U.S.Gov't
Tetrodotoxin
Verapamil
Megjelenés:Pflügers Archiv. - 430 : 4 (1995), p. 596-598. -
További szerzők:Weidema, Adam Freek (biofizikus) Krasznai Zoltán (1950-) (biofizikus) Nijweide, Peter J. Ypey, Dirk L.
Internet cím:DOI
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7.

001-es BibID:BIBFORM046298
Első szerző:Goda Katalin (biofizikus)
Cím:Reversal of Multidrug Resistance by Valinomycin is Overcome by CCCP / Goda K., Krasznai Z., Gaspar R., Lankelma J., Westerhoff H. V., Damjanovich S., Szabo G.
Dátum:1996
ISSN:0006-291X
Megjegyzések:Reversal of P-glycoprotein-mediated multidrug resistance by valinomycin is overcome by the proton ionophore, CCCP. This effect, a complete suppression of the 5- to 10-fold valinomycin-induced reversal ("re-reversal"), exhibits a sharp extracellular potassium concentration ([K+(0)]) dependence. It is observed at [K+(0)] > 2-4 mM and not at [K+(0)] greater than or equal to 2 mM, in the case of the fluorescent substrates rhodamine 123 and daunorubicin. The fact that "re-reversal" is detected only for the combination of CCCP with valinomycin raises the possibility that a direct interaction between these ionophores may explain the phenomenon. We show spectroscopic evidence of such an interaction, with a [K+(0)]-dependence similar to that of the "re-reversal." These data suggest that the reversal of P-glycoprotein activity by valinomycin can be compromised by anionic compounds such as CCCP due to complex formation. More generally, molecular interactions involving P-glycoprotein substrates or reversing agents may significantly affect drug accumulation in multidrug resistant cells.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical And Biophysical Research Communications. - 219 : 2 (1996), p. 306-310. -
További szerzők:Krasznai Zoltán (1950-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Lankelma, Jan Westerhoff, Hans V. Damjanovich Sándor (1936-2017) (biofizikus) Szabó Gábor (1953-) (biofizikus)
Pályázati támogatás:T14655
OTKA
17592
OTKA
Internet cím:Szerző által megadott URL
DOI
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8.

001-es BibID:BIBFORM040003
Első szerző:Krasznai Zoltán (biofizikus)
Cím:A slow outward current and a hypoosmolality induced anion conductance in embryonic chicken osteoclasts / Krasznai, Z., Weidema, F., Ypey, D. L., Damjanovich, S., Gaspar, R., Marian, T.
Dátum:2001
ISSN:0236-5383
Megjegyzések:In this paper we report on a hypoosmolality induced current, I(osmo), in embryonic chicken osteoclasts, which could only be studied when blocking a simultaneously active, unidentified slow outward current, I(slo). I(slo) was observed in all of the examined cells when both the intracellular and extracellular solutions contained sodium as the major cation and no potassium. The current was outwardly rectifying and activated at membrane potentials more positive than -44 +/- 12 mV (n = 31). The time to half activation of the current was also voltage dependent and was 350 ms at Vm = +80 mV, and 78 ms at Vm = +120 mV. The current did not inactivate during periods up to 5 s. Extracellular 4-AP (5 mM), TEA (5 mM) and Ba2+ (1 mM), blockers of K+ conductances in chicken osteoclasts, did not influence I(slo). However, I(slo) was inhibited by 50 microM extracellular verapamil, which allowed us to study I(osmo) in isolation. Exposure of the osteoclasts to hypotonic solution resulted in the development of a depolarization activated I(osmo). It developed after a 1-min delay and reached its maximum within 10 minutes. Half-maximal activation occurred after 4.4 +/- 0.9 min (n = 9). The current activated within a few ms upon depolarization and did not inactivate during at least 5 sec. I(osmo) reversed around the calculated Nernst potential for Cl- (E(Cl) = +7.3 mV and V(rev) = +5.4 +/- 3.6 mV, n = 9). The underlying conductance, G(osmo) exhibited moderate outward rectification around 0 mV in symmetrical Cl- solutions. Ion substitution experiments showed that G(osmo) is an anion conductance with P(Cl) approximately = P(F) > P(gluc) >> P(Na). I(osmo) was blocked by 0.5 mM SITS but 50 microM verapamil, 5 mM TEA, 5 mM 4-AP, 1 mM Ba2+, 50 microM cytochalasin D and 0.5 mM alendronate did not have any effect on the current. Cl- currents have been implicated in charge neutralization during osteoclastic acid secretion for bone resorption. The present results imply that osmolality may be a factor controlling this charge neutralization.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény hazai lapban
Animal
Anions
Calcium
Calcium Channel Blockers
Chick Embryo
Cytochalasin D
drug effects
Hungary
Ion Transport
Membrane Potentials
metabolism
Osmolar Concentration
Osteoclasts
pharmacology
physiology
Potassium
Sodium
Support,Non-U.S.Gov't
Verapamil
Megjelenés:Acta Biologica Hungarica. - 52 : 1 (2001), p. 47-61. -
További szerzők:Weidema, F. Ypey, Dirk L. Gáspár Rezső (1944-) (biofizikus) Márián Teréz (1950-) (radiobiológus) Damjanovich Sándor (1936-2017) (biofizikus)
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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9.

001-es BibID:BIBFORM004731
Első szerző:Krasznai Zoltán (biofizikus)
Cím:Role of ion channels and membrane potential in the initiation of carp sperm motility / Krasznai, Z., Morisawa, M., Morisawa, S., Krasznai, Z. T., Tron, L., Gaspar, R., Marian, T.
Dátum:2003
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Ion Channels
Sperm Motility
Megjelenés:Aquatic living resources [electronic resource]. - 16 : 5 (2003), p. 445-449. -
További szerzők:Morisawa, Masaaki Morisawa, Sachiko Krasznai Zoárd Tibor (1973-) (szülész-nőgyógyász, gyermeknőgyógyász) Trón Lajos (1941-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Márián Teréz (1950-) (radiobiológus)
Internet cím:DOI
elektronikus változat
Borító:

10.

001-es BibID:BIBFORM039513
Első szerző:Márián Teréz (radiobiológus)
Cím:A1 and A2 adenosine receptor activation inversely modulates potassium currents and membrane potential in DDT1 MF-2 smooth muscle cells / Marian, T., Rubovszky, B., Szentmiklosi, A. J., Tron, L., Balkay, L., Boros, I., Gaspar, R., Szekely, A., Krasznai, Z.
Dátum:2002
ISSN:0021-5198
Megjegyzések:Adenosine receptors are widely distributed in mammalian tissues and have been possibly involved through transmembrane potential changes in cell function regulation. The effect of A1 and A2A adenosine receptor ligands on transmembrane potential measured with flow cytometry and potassium conductance measured by the patch-clamp technique was investigated in DDT1 MF-2 smooth muscle cells. The A1 adenosine-receptor agonist CPA (50 nM) and the A2A adenosine-receptor agonist CGS 21680 (50 nM) elicited a rapid and maintained increase and decrease in the potassium conductance, respectively, and a concomitant hyperpolarization and depolarization of the membrane, respectively. These effects were eliminated by subtype-selective adenosine receptor antagonists (DPCPX, CSC, ZM 241385, all 1 microM). The ligand induced membrane potential changes were reversible. Based on these detected membrane potential changes along with the published voltage dependence of the adenylyl cyclase, the regulation of cAMP production by A1- and A2A-receptor activation is suggested to be mediated through the induced early hyperpolarization and depolarization. The interaction between the effects of these receptor subtypes allows for a complex regulation mechanism.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:The Japanese Journal of Pharmacology. - 89 : 4 (2002), p. 366-372. -
További szerzők:Rubovszky Bálint (1975-) (élettanász) Szentmiklósi József András (1948-) (farmakológus, klinikai laboratóriumi szakorvos) Trón Lajos (1941-) (biofizikus) Balkay László (1963-) (biofizikus) Boros István Gáspár Rezső (1944-) (biofizikus) Székely Andrea Krasznai Zoltán (1950-) (biofizikus)
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DOI
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11.

001-es BibID:BIBFORM046300
Első szerző:Panyi György (biofizikus)
Cím:Immunosuppressors inhibit voltage-gated potassium channels in human peripheral blood lymphocytes / Panyi G., Gaspar R., Krasznai Z., ter Horst J. J., Ameloot M., Aszalos A., Steels P., Damjanovich S.
Dátum:1996
ISSN:0006-291X
Megjegyzések:The effects of immunosuppressive agents on the potassium current of human peripheral blood lymphocytes have been studied using the whole-cell patch-clamp technique. Cyclosporin A (10 micrograms/ml), rapamycin (10 micrograms/ml) and FK-506 (2.5 micrograms/ml) reduced the peak K+ current by approximately 40, 30 and 40% of the control, respectively, without any change in the reversal potential of the current. The current inhibition was similar at all membrane potentials studied and was accompanied with an increase in the rate of K+ current inactivation. Membrane potential measurements in current-clamp showed a marked depolarization of the membrane (>10 mV) upon the addition of either immunosuppressor to the cells. Our findings revealed that the voltage-dependent potassium current in human peripheral blood lymphocytes is inhibited by Cyclosporin A and other immunosuppressors, resulting in a depolarized membrane potential.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biochemical and Biophysical Research Communications. - 221 : 2 (1996), p. 254-258. -
További szerzők:Gáspár Rezső (1944-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) ter Horst, Jan J. Ameloot, Marcel Aszalos Adorján Steels, Paul Damjanovich Sándor (1936-2017) (biofizikus)
Pályázati támogatás:1459
OTKA
1492
OTKA
6221
OTKA
E12533
OTKA
T14655
OTKA
F13335
OTKA
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
Borító:

12.

001-es BibID:BIBFORM004688
Első szerző:Panyi György (biofizikus)
Cím:Electrophysiology of human lymphocytes / Panyi, G., Gaspar, R., Krasznai, Z., Matyus, L., Van Duijn, B.
Dátum:2001
ISSN:90-8-2521-9-0
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
Electrophysiology
Human
Megjelenés:Molecular and Cell Biology: from plant to human. - p. 162-183.
További szerzők:Gáspár Rezső (1944-) (biofizikus) Krasznai Zoltán (1950-) (biofizikus) Mátyus László (1956-) (biofizikus) Duijn, B., Van
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