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1.

001-es BibID:BIBFORM004855
Első szerző:Bagdány Miklós
Cím:Anuroctoxin, a new scorpion toxin of the alpha-KTx 6 subfamily, is highly selective for Kv1.3 over IKCa1 ion channels of human T lymphocytes / Bagdany, M., Batista, C. V. F., Valdez-Cruz, N. A., Somodi, S., Rodriguez de la Vega, R. C., Licea, A. F., Varga, Z., Gaspar, R., Possani, L. D., Panyi, G.
Dátum:2005
Megjegyzések:The physiological function of T lymphocytes can be modulated selectively by peptide toxins acting on Kv1.3 K(+) channels. Because Kv1.3-specific peptide toxins are considered to have a significant therapeutic potential in the treatment of autoimmune diseases, the discovery of new toxins is highly motivated. Through chromatographic procedures and electrophysiological assays, using patch-clamp methodology, the isolation of a novel peptide named anuroctoxin was accomplished using the venom of the Mexican scorpion Anuroctonus phaiodactylus. It has 35 amino acid residues with a molecular weight of 4082.8, tightly bound by four disulfide bridges whose complete covalent structure was determined. It has a pyroglutamic acid at the N-terminal region and an amidated C-terminal residue. Sequence comparison and phylogenetic clustering analysis classifies anuroctoxin into subfamily 6 of the alpha-KTx scorpion toxins (systematic name, alpha-KTx 6.12). Patch-clamp experiments show that anuroctoxin is a high-affinity blocker of Kv1.3 channels of human T lymphocytes with a K(d) of 0.73 nM, and it does not block the Ca(2+)-activated IKCa1 K(+) channels. These two channels play different but important roles in T-lymphocyte activation. Furthermore, the toxin practically does not inhibit Shaker IR, mKv1.1, and rKv2.1 channels, whereas the affinity of anuroctoxin for hKv1.2 is almost an order of magnitude smaller than for Kv1.3. The pharmacological profile and the selectivity of this new toxin for Kv1.3 over IKCa1 may provide an important tool for the modulation of the immune system, especially in cases in which selective inhibition of Kv1.3 is required.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
analysis
Animals
antagonists & inhibitors
Autoimmune Diseases
Biophysics
chemistry
drug effects
Human
Humans
Hungary
Immune System
Intermediate-Conductance Calcium-Activated Potassium Channels
Ion Channels
isolation & purification
Kv1.3 Potassium Channel
Lymphocytes
Models,Molecular
Molecular Weight
pharmacology
Phylogeny
Potassium
Potassium Channel Blockers
Potassium Channels
Potassium Channels,Calcium-Activated
Potassium Channels,Voltage-Gated
Research
Scorpion Venoms
Sequence Alignment
Support
T-Lymphocytes
Toxins
Toxins,Biological
Megjelenés:Molecular Pharmacology. - 67 : 4 (2005), p. 1034-1044. -
További szerzők:Batista, Cesar V. F. Valdez-Cruz, Norma A. Somodi Sándor (1977-) (belgyógyász) Rodriguez de la Vega, Ricardo C. Licea, Alexei F. Varga Zoltán (1969-) (biofizikus, szakfordító) Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
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elektronikus változat
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2.

001-es BibID:BIBFORM084527
035-os BibID:(WoS)000375141600351
Első szerző:Balajthy András (általános orvos)
Cím:7-Dehydrocholesterol Modifies the Operation of Kv1.3 Channels in T Cells Isolated from Smith-Lemli-Opitz Syndrome Patients / Balajthy Andras, Petho Zoltan, Somodi Sandor, Varga Zoltan, Peter Maria, Vígh Laszlo, Szabó Gabriella P., Paragh Gyorgy, Panyi Gyorgy, Hajdu Peter
Dátum:2016
ISSN:0006-3495
Tárgyszavak:Orvostudományok Klinikai orvostudományok idézhető absztrakt
folyóiratcikk
Megjelenés:Biophysical Journal. - 110 : 3 (2016), p. 278a-279a. -
További szerzők:Pethő Zoltán (1989-) (orvos) Somodi Sándor (1977-) (belgyógyász) Varga Zoltán (1969-) (biofizikus, szakfordító) Péter Mária Vígh László (orvos Szeged) P. Szabó Gabriella (1975-) (csecsemő- és gyermekgyógyász, klinikai genetikus) Paragh György (1953-) (belgyógyász) Panyi György (1966-) (biofizikus) Hajdu Péter (1975-) (biofizikus)
Internet cím:DOI
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3.

001-es BibID:BIBFORM064954
Első szerző:Balajthy András (általános orvos)
Cím:7DHC-induced changes of Kv1.3 operation contributes to modified T cell function in Smith-Lemli-Opitz syndrome / András Balajthy, Sándor Somodi, Zoltán Pethő, Mária Péter, Zoltán Varga, Gabriella P. Szabó, György Paragh, László Vígh, György Panyi, Péter Hajdu
Dátum:2016
ISSN:0031-6768
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Pflügers Archiv. - 468 : 8 (2016), p. 1403-1418. -
További szerzők:Somodi Sándor (1977-) (belgyógyász) Pethő Zoltán (1989-) (orvos) Péter Mária Varga Zoltán (1969-) (biofizikus, szakfordító) P. Szabó Gabriella (1975-) (csecsemő- és gyermekgyógyász, klinikai genetikus) Paragh György (1953-) (belgyógyász) Vígh László (orvos Szeged) Panyi György (1966-) (biofizikus) Hajdu Péter (1975-) (biofizikus)
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4.

001-es BibID:BIBFORM052924
Első szerző:Bartók Ádám (biotechnológus)
Cím:Margatoxin is a non-selective inhibitor of human Kv1.3 K+ channels / Adam Bartok, Agnes Toth, Sandor Somodi, Tibor G. Szanto, Peter Hajdu, Gyorgy Panyi, Zoltan Varga
Dátum:2014
ISSN:0041-0101
Megjegyzések:Margatoxin (MgTx), an alpha-KTx scorpion toxin, is considered a selective inhibitor of the Kv1.3 K+ channel. This peptide is widely used in ion channel research; however, a comprehensive study of its selectivity with electrophysiological methods has not been published yet. The lack of selectivity might lead to undesired side effects upon therapeutic application or may lead to incorrect conclusion regarding the role of a particular ion channel in a physiological or pathophysiological response either in vitro or in vivo. Using the patch-clamp technique we characterized the selectivity profile of MgTx using L929 cells expressing mKv1.1 channels, human peripheral lymphocytes expressing Kv1.3 channels and transiently transfected tsA201 cells expressing hKv1.1, hKv1.2, hKv1.3, hKv1.4-IR, hKv1.5, hKv1.6, hKv1.7, rKv2.1, Shaker-IR, hERG, hKCa1.1, hKCa3.1 and hNav1.5 channels. MgTx is indeed a high affinity inhibitor of Kv1.3 (Kd = 11.7 pM) but is not selective, it inhibits the Kv1.2 channel with similar affinity (Kd = 6.4 pM) and Kv1.1 in the nanomolar range (Kd = 4.2 nM). Based on our comprehensive data MgTX has to be considered a non-selective Kv1.3 inhibitor, and thus, experiments aiming at elucidating the significance of Kv1.3 in in vitro or in vivo physiological responses have to be carefully evaluated.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
ion channel
potassium channel
scorpion toxin
margatoxin
Megjelenés:Toxicon. - 87 (2014), p. 6-16. -
További szerzők:Tóth Ágnes (1983-) (biofizikus) Somodi Sándor (1977-) (belgyógyász) Szántó Gábor Tibor (1980-) (vegyész) Hajdu Péter (1975-) (biofizikus) Panyi György (1966-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító)
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
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5.

001-es BibID:BIBFORM004881
Első szerző:Olamendi-Portugal, Timoteo
Cím:Novel alpha-KTx peptides from the venom of the scorpion Centruroides elegans selectively blockade Kv1.3 over IKCa1 K+ channels of T cells / Olamendi-Portugal, T., Somodi, S., Fernandez, J. A., Zamudio, F. Z., Becerril, B., Varga, Z., Panyi, G., Gaspar, R., Possani, L. D.
Dátum:2005
ISSN:0041-0101
Megjegyzések:From the venom of the Mexican scorpion Centruroides elegans Thorell five peptides were isolated to homogeneity by chromatographic procedures and their full amino acid sequence was determined by automatic Edman degradation. They all belong to the Noxiustoxin subfamily of scorpion toxins and were given the systematic names alpha-KTx 2.8 to 2.12, with trivial names Ce1 to Ce5, respectively. They have 39 amino acid residues, except for Ce3 which has only 38, but all of them have three disulfide bridges, and have molecular weights of 4255, 4267, 4249, 4295 and 4255 atomic mass units, respectively for Ce1 to Ce5. The C-terminal residues of Ce2, Ce4 and Ce5 were found to be amidated. The electrophysiological assay (whole-cell patch-clamp) showed that out of the five peptides, Ce1 (alpha-KTx 2.8), Ce2 (alpha-KTX2.9) and Ce4 (alpha-KTx 2.11) were effective blockers of Kv1.3 channels of human T lymphocytes, whereas these peptides did not inhibit the Ca2+-activated K+ channels (IKCa1) of the same cells. The equilibrium dissociation constants of these peptides for Kv1.3 were 0.70, 0.25 and 0.98nM for Ce1, Ce2 and Ce4, respectively. Furthermore, toxins Ce1, Ce2 and Ce4 practically did not inhibit the related voltage gated Shaker K+ channels, and rKv2.1 channels of the Shab family. The high affinity blockage of Kv1.3 channels by these peptides and their selectivity for Kv1.3 over IKCa1 may have significance in the development of novel tools for suppressing the function of those T cell subsets whose proliferation critically depends on the activity of Kv1.3 channels.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Amino Acid Sequence
Animals
antagonists & inhibitors
Bayes Theorem
Cell Line
Cells
chemistry
Chromatography,High Pressure Liquid
Comparative Study
Electrophysiology
Enzyme-Linked Immunosorbent Assay
genetics
Human
Humans
Intermediate-Conductance Calcium-Activated Potassium Channels
Kv1.3 Potassium Channel
Lymphocytes
Mass Spectrometry
metabolism
Mexico
Models,Genetic
Molecular Sequence Data
Molecular Weight
Organophosphorus Compounds
Peptides
Phylogeny
Potassium
Potassium Channels
Research
Scorpion Venoms
Scorpions
Sequence Analysis,Protein
Support
T-Lymphocytes
toxicity
Toxins
Megjelenés:Toxicon. - 46 : 4 (2005), p. 418-429. -
További szerzők:Somodi Sándor (1977-) (belgyógyász) Fernandez, Juan Antonio Zamudio, Fernando Z. Becerril, Baltazar Varga Zoltán (1969-) (biofizikus, szakfordító) Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Possani, Lourival Domingos
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DOI
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6.

001-es BibID:BIBFORM004715
Első szerző:Panyi György (biofizikus)
Cím:Pharmacological effects of melatonin on ion channels / Panyi, G., Somodi, S., Varga, Z., Hajdu, P., Pieri, C., Pandi-Perumal, S. R., Damjanovich, S., Gaspar, R., Hardar, C., Singaravel, M., Maitra, S. K.
Dátum:2002
Tárgyszavak:Orvostudományok Elméleti orvostudományok könyvfejezet
Ion Channels
Melatonin
Megjelenés:Treatise on Pineal Gland and Melatonin. - p. 489-506.
További szerzők:Somodi Sándor (1977-) (belgyógyász) Varga Zoltán (1969-) (biofizikus, szakfordító) Hajdu Péter (1975-) (biofizikus) Pieri, Carlo Pandi-Perumal, Seithikurippu R. Damjanovich Sándor (1936-2017) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Hardar, C. Singaravel, M. Maitra, S. K.
Borító:

7.

001-es BibID:BIBFORM062512
Első szerző:Pethő Zoltán (orvos)
Cím:The anti-proliferative effect of cation channel blockers in T lymphocytes depends on the strength of mitogenic stimulation / Zoltan Petho, Andras Balajthy, Adam Bartok, Krisztian Bene, Sandor Somodi, Orsolya Szilagyi, Eva Rajnavolgyi, Gyorgy Panyi, Zoltan Varga
Dátum:2016
ISSN:0165-2478
Megjegyzések:Ion channels are crucially important for the activation and proliferation of T lymphocytes, and thus, for the function of the immune system. Previous studies on the effects of channel blockers on T cell proliferation reported variable effectiveness due to differing experimental systems. Therefore our aim was to investigate how the strength of the mitogenic stimulation influences the efficiency of cation channel blockers in inhibiting activation, cytokine secretion and proliferation of T cells under standardized conditions. Human peripheral blood lymphocytes were activated via monoclonal antibodies targeting the TCR-CD3 complex and the co-stimulator CD28. We applied the blockers of Kv1.3 (Anuroctoxin), KCa3.1 (TRAM-34) and CRAC (2-Apb) channels of T cells either alone or in combination with rapamycin, the inhibitor of the mammalian target of rapamycin (mTOR). Five days after the stimulation ELISA and flow cytometric measurements were performed to determine IL-10 and IFN-? secretion, cellular viability and proliferation. Our results showed that ion channel blockers and rapamycin inhibit IL-10 and IFN-? secretion and cell division in a dose-dependent manner. Simultaneous application of the blockers for each channel along with rapamycin was the most effective, indicating synergy among the various activation pathways. Upon increasing the extent of mitogenic stimulation the anti-proliferative effect of the ion channel blockers diminished. This phenomenon may be important in understanding the fine-tuning of T cell activation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Immune regulation
Rapamycin
ion channel
Cytokine secretion
T cells
Megjelenés:Immunology Letters 171 (2016), p. 60-69. -
További szerzők:Balajthy András (1988-) (általános orvos) Bartók Ádám (1984-) (biotechnológus) Bene Krisztián (1986-) (Biológus) Somodi Sándor (1977-) (belgyógyász) Szilágyi Orsolya (1985-) (molekuláris biológus, biokémikus) Rajnavölgyi Éva (1950-) (immunológus) Panyi György (1966-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító)
Pályázati támogatás:KTIA NAP 13-2-2015-0009
Egyéb
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DOI
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8.

001-es BibID:BIBFORM004885
Első szerző:Somodi Sándor (belgyógyász)
Cím:The role of His399 in the pH-dependent modulation of Kv1.3 inactivation / Somodi, S., Varga, Z., Levy, D. I., Gaspar, R., Panyi, G.
Dátum:2005
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:Biophysical Journal. - 88 : 1 (2005), p. 278A. -
További szerzők:Varga Zoltán (1969-) (biofizikus, szakfordító) Levy, Daniel I. Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus)
Borító:

9.

001-es BibID:BIBFORM004738
Első szerző:Somodi Sándor (belgyógyász)
Cím:C-type inactivation of Kv1.3 channels : combined effects of extracellular pH,K+ concentration and ionic strength / Somodi, S., Hajdu, P., Varga, Z., Gaspar, R., Panyi, G.
Dátum:2003
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:Biophysical Journal. - 84 : 2 Part 2 (2003), p. B240. -
További szerzők:Hajdu Péter (1975-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító) Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus)
Borító:

10.

001-es BibID:BIBFORM004844
Első szerző:Somodi Sándor (belgyógyász)
Cím:pH-dependent modulation of Kv1.3 inactivation : role of His399 / Somodi, S., Varga, Z., Hajdu, P., Starkus, J. G., Levy, D. I., Gaspar, R., Panyi, G.
Dátum:2004
Megjegyzések:The Kv1.3 K(+) channel lacks N-type inactivation, but during prolonged depolarized periods it inactivates via the slow (P/C type) mechanism. It bears a titratable histidine residue in position 399 (equivalent of Shaker 449), a site known to influence the rate of slow inactivation. As opposed to several other voltage-gated K(+) channels, slow inactivation of Kv1.3 is slowed when extracellular pH (pH(o)) is lowered under physiological conditions. Our findings are as follows. First, when His399 was mutated to a lysine, arginine, leucine, valine or tyrosine, extracellular acidification (pH 5.5) accelerated inactivation reminiscent of other Kv channels. Second, inactivation of the wild-type channel was accelerated by low pH(o) when the ionic strength of the external solution was raised. Inactivation of the H399K mutant was also accelerated by high ionic strength at pH 7.35 but not the inactivation of H399L. Third, after the external application of blocking barium ions, recovery of the wild-type current during washout was slower in low pH(o). Fourth, the dissociation rate of Ba(2+) was pH insensitive for both H399K and H399L. Furthermore, Ba(2+) dissociation rates were equal for H399K and the wild type at pH 5.5 and were equal for H399L and the wild type at pH 7.35. These observations support a model in which the electric field of the protonated histidines creates a potential barrier for potassium ions just outside the external mouth of the pore that hinders their exit from the binding site controlling inactivation. In Kv1.3, this effect overrides the generally observed speeding of slow inactivation when pH(o) is reduced.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Animals
Barium
Biophysics
chemistry
Extracellular Fluid
genetics
Histidine
Human
Humans
Hungary
Hydrogen-Ion Concentration
Ion Channel Gating
Kv1.3 Potassium Channel
Lysine
Membrane Potentials
metabolism
Models,Biological
Mutation
Patch-Clamp Techniques
physiology
Potassium
Potassium Channels
Potassium Channels,Voltage-Gated
Research
Support
Megjelenés:American Journal of Physiology. Cell Physiology. - 287 : 4 (2004), p. C1067-C1076. -
További szerzők:Varga Zoltán (1969-) (biofizikus, szakfordító) Hajdu Péter (1975-) (biofizikus) Starkus, John G. Levy, Daniel I. Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus)
Internet cím:DOI
elektronikus változat
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11.

001-es BibID:BIBFORM005515
Első szerző:Somodi Sándor (belgyógyász)
Cím:Effects of changes in extracellular pH and potassium concentration on Kv1.3 inactivation / Somodi S., Hajdu P., Gáspár R., Panyi G., Varga Z.
Dátum:2008
Megjegyzések:The Kv1.3 channel inactivates via the P/C-type mechanism, which is influenced by a histidine residue in the pore region (H399, equivalent of Shaker 449). Previously we showed that the electric field of the protonated histidines at low extracellular pH (pH(e)) creates a potential barrier for K(+) ions just outside the pore that hinders their exit from the binding site controlling inactivation (control site) thereby slowing inactivation kinetics. Here we examined the effects of extracellular potassium [K(+)](e) and pH(e) on the rate of inactivation of Kv1.3 using whole-cell patch-clamp. We found that in 150 mM [K(+)](e )inactivation was accelerated upon switching to pH(e) 5.5 as opposed to the slowing at 5 mM [K(+)](e). The transition from slowing to acceleration occurred at 40 mM [K(+)](e), whereas this "turning point" was at 20 mM [K(+)](e) for inward currents. The rate of entry of Ba(2+) ions from the extracellular space to the control site was significantly slowed by low pH(e) in wild-type hKv1.3, but it was insensitive to pH(e) in H399K and H399L mutants. Based on these observations we expanded our model and propose that the potential barrier created by the protonated histidines impedes the passage of K(+) ions between the extracellular medium and the control site in both directions and the effect on inactivation rate (acceleration or slowing) depends on the relative contribution of filling from the extracellular and intracellular sides.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:European Biophysics Journal. - 37 : 7 (2008), p. 1145-1156. -
További szerzők:Hajdu Péter (1975-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Panyi György (1966-) (biofizikus) Varga Zoltán (1969-) (biofizikus, szakfordító)
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