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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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001-es BibID:	BIBFORM004728
Első szerző:	Hajdu Péter (biofizikus)
Cím:	Cholesterol modifies the gating of Kv1.3 in human T lymphocytes / Péter Hajdú, Zoltán Varga, Carlo Pieri, György Panyi, Rezső Gáspár
Dátum:	2003
ISSN:	0031-6768
Megjegyzések:	The Kv1.3 potassium channel that belongs to the Shaker family of voltage-gated K(+) channels plays a crucial role in the mitogenic response of T cells. Because it spans the cell membrane its function can be influenced by lipid-protein interactions. In order to study the effect of lipid-protein interactions on the functioning of Kv1.3 we manipulated the membrane cholesterol content in T cells mimicking various physiological conditions by means of the oligosaccharide methyl-beta-cyclodextrin (MbetaCD) and its cholesterol-saturated complex (MbetaCD/C). Fluorescence polarization anisotropy and peak current density were used to monitor the efficiency of cholesterol removal (MbetaCD) and loading (MbetaCD/C). Using whole-cell patch-clamp technique we determined the kinetic and steady-state parameters of activation and inactivation of the Kv1.3 currents under different treatment conditions. Upon elevation of cholesterol content by 1 or 1.5 mg/ml MbetaCD/C the rates of both activation and inactivation were slowed. Moreover, the increased cholesterol level in the membrane resulted in a biphasic activation curve. Cholesterol depletion with MbetaCD (0.95 and 1.425 mg/ml) caused no significant changes in the gating characteristics of Kv1.3. The equilibrium between the open and the closed states of the channels was affected by increased cholesterol content, but at the same time steady-state inactivation was unchanged. We argue that manipulation of membrane cholesterol changed both the kinetic properties of Kv1.3 and steady-state parameters of activation by modifying lipid-protein interactions
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban beta-Cyclodextrins Biophysics Cell Membrane Cells Cholesterol Cyclodextrins drug effects Electric Conductivity Fluorescence Fluorescence Polarization Human Humans Hungary Ion Channel Gating Kinetics Kv1.3 Potassium Channel Lymphocytes Membrane Microdomains Membrane Potentials metabolism pharmacology physiology Potassium Potassium Channels Potassium Channels,Voltage-Gated Research Support T-Lymphocytes
Megjelenés:	Pflügers Archiv. - 445 : 6 (2003), p. 674-682. -
További szerzők:	Varga Zoltán (1969-) (biofizikus, szakfordító) Pieri, Carlo Panyi György (1966-) (biofizikus) Gáspár Rezső (1944-) (biofizikus)
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001-es BibID:	BIBFORM004739
Első szerző:	Starkus, John G.
Cím:	Mechanisms of the inhibition of Shaker potassium channels by protons / John G. Starkus, Zoltán Varga, Roland Schönherr, Stefan H. Heinemann
Dátum:	2003
ISSN:	0031-6768
Megjegyzések:	Potassium channels are regulated by protons in various ways and, in most cases, acidification results in potassium current reduction. To elucidate the mechanisms of proton-channel interactions we investigated N-terminally truncated Shaker potassium channels (Kv1 channels) expressed in Xenopus oocytes, varying pH at the intracellular and the extracellular face of the membrane. Intracellular acidification resulted in rapid and reversible channel block. The block was half-maximal at pH 6.48, thus even physiological excursions of intracellular pH will have an impact on K+ current. The block displayed only very weak voltage dependence and C-type inactivation and activation were not affected. Extracellular acidification (up to pH 4) did not block the channel, indicating that protons are effectively excluded from the selectivity filter. Channel current, however, was reduced greatly due to marked acceleration of C-type inactivation at low pH. In contrast, inactivation was not affected in the T449V mutant channel, in which C-type inactivation is impaired. The pH effect on inactivation of the wild-type channel had an apparent pK of 4.7, suggesting that protonation of extracellular acidic residues in Kv channels makes them subject to pH regulation
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Animals Comparative Study drug effects Female Ion Channel Gating Oocytes pharmacology physiology Potassium Potassium Channel Blockers Potassium Channels Protons Research Shaker Superfamily of Potassium Channels Support Xenopus
Megjelenés:	Pflügers Archiv. - 447 : 1 (2003), p. 44-54. -
További szerzők:	Varga Zoltán (1969-) (biofizikus, szakfordító) Schönherr, Roland Heinemann, Stefan H.
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