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001-es BibID:	BIBFORM004121
Első szerző:	Csernoch László (élettanász)
Cím:	Voltage-activated elementary calcium release events in isolated mouse skeletal muscle fibers / Laszlo Csernoch, Sandrine Pouvreau, Michel Ronjat, Vincent Jacquemond
Dátum:	2008
Megjegyzések:	The elementary Ca(2+)-release events underlying voltage-activated myoplasmic Ca(2+) transients in mammalian muscle remain elusive. Here, we looked for such events in confocal line-scan (x,t) images of fluo-3 fluorescence taken from isolated adult mouse skeletal muscle fibers held under voltage-clamp conditions. In response to step depolarizations, spatially segregated fluorescence signals could be detected that were riding on a global increase in fluorescence. These discrete signals were separated using digital filtering in the spatial domain; mean values for their spatial half-width and amplitude were 1.99 +/- 0.09 microm and 0.16 +/- 0.005 DeltaF/F(0) (n = 151), respectively. Under control conditions, the duration of the events was limited by the pulse duration. In contrast, in the presence of maurocalcine, a scorpion toxin suspected to disrupt the process of repolarization-induced ryanodine receptor (RyR) closure, events uninterrupted by the end of the pulse were readily detected. Overall results establish these voltage-activated low-amplitude local Ca(2+) signals as inherent components of the physiological Ca(2+)-release process of mammalian muscle and suggest that they result from the opening of either one RyR or a coherently operating group of RyRs, under the control of the plasma membrane polarization.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	The Journal of Membrane Biology. - 226 : (1-3) (2008), p. 43-55. -
További szerzők:	Pouvreau, Sandrine Ronjat, Michel Jacquemond, Vincent
Internet cím:	elektronikus változat DOI
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001-es BibID:	BIBFORM004689
Első szerző:	Péter Mózes (orvos, neuroradiológus) ifj.
Cím:	Effects of toxins Pi2 and Pi3 on human T lymphocyte Kv1.3 channels : the role of Glu7 and Lys24 / Peter, M., Jr., Varga, Z., Hajdu, P., Gaspar, R., Damjanovich, S., Horjales, E., Possani, L. D., Panyi, G.
Dátum:	2001
Megjegyzések:	Pandinus imperator scorpion toxins Pi2 and Pi3 differ only by a single amino acid residue (neutral Pro7 in Pi2 vs. acidic Glu7 in Pi3). The binding kinetics of these toxins to human Kv1.3 showed that the decreased ON rate (k(ON) = 2.18 x 10(8) m(-1)sec(-1) for Pi2 and 1.28 x 10(7) m(-1)sec(-1) for Pi3) was almost entirely responsible for the increased dissociation constant (K(d)) of Pi3 (K(d) = 795 pm) as compared to Pi2 (K(d) = 44 pm). The ionic strength dependence of the association rates was exactly the same for the two toxins indicating that through-space electrostatic interactions can not account for the different ON rates. Results were further analyzed on the basis of the three-dimensional structural models of the toxins. A 3D structure of Pi3 was generated from the NMR spectroscopy coordinates of Pi2 by computer modeling. The Pi3 model resulted in a salt bridge between Glu7 and Lys24 in Pi3. Based on this finding our interpretation of the reduced ON rate of Pi3 is that the intramolecular salt bridge reduces the local positive electrostatic potential around Lys24 resulting in decreased short-range electrostatic interactions during the binding step. To support our finding, we constructed a 3D model of the Ser-10-Asp Charybdotoxin mutant displaying distinctly reduced affinity for Shaker channels. The mutant Charybdotoxin structure also displayed a salt bridge between residues Asp10 and Lys27 equivalent to the one between Glu7 and Lys24 in Pi3.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Amino Acid Sequence Animal Charybdotoxin chemistry drug effects genetics Glutamic Acid Human Hungary In Vitro Kinetics Lysine Membrane Potentials metabolism Models,Molecular Molecular Sequence Data pharmacology Point Mutation Potassium Potassium Channel Blockers Potassium Channels Protein Conformation Scorpion Venoms Sequence Homology,Amino Acid Support,Non-U.S.Gov't T-Lymphocytes Toxins
Megjelenés:	The Journal of Membrane Biology. - 179 : 1 (2001), p. 13-25. -
További szerzők:	Varga Zoltán (1969-) (biofizikus, szakfordító) Hajdu Péter (1975-) (biofizikus) Gáspár Rezső (1944-) (biofizikus) Damjanovich Sándor (1936-2017) (biofizikus) Horjales, E. Possani, Lourival Domingos Panyi György (1966-) (biofizikus)
Internet cím:	DOI elektronikus változat
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001-es BibID:	BIBFORM002150
Első szerző:	Seres Ildikó (biokémikus)
Cím:	The Association between angiotensin II-induced free radical generation and membrane fluidity in neutrophils of patients with metabolic syndrome / Seres Ildikó, Fóris Gabriella, Varga Zsuzsa, Kosztáczky Béla, Kassai Andrea, Balogh Zoltán, Fülöp Péter, Paragh György
Dátum:	2006
Tárgyszavak:	Orvostudományok Klinikai orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	The Journal of Membrane Biology 214 : 2 (2006), p. 91-98. -
További szerzők:	Fóris Gabriella (1937-) (belgyógyász) Varga Zsuzsa (1951-) (biokémikus, nephrológus) Kosztáczky Béla (1967-) (orvos) Kassai Andrea Balogh Zoltán (1965-) (belgyógyász, gasztroenterológus, diabetológus) Fülöp Péter (1974-) (belgyógyász, endokrinológus, lipidológus) Paragh György (1953-) (belgyógyász)
Internet cím:	elektronikus változat DOI
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001-es BibID:	BIBFORM005105
Első szerző:	Szűcs Attila (fül-orr-gégész)
Cím:	Changes in purinoceptor distribution and intracellular calcium levels following noise exposure in the outer hair cells of the guinea pig / Szucs, A., Szappanos, H., Batta, T. J., Toth, A., Szigeti, G. P., Panyi, G., Csernoch, L., Sziklai, I.
Dátum:	2006
ISSN:	022-2631 (Print)
Megjegyzések:	Among the cells of the inner ear, the outer hair cells (OHCs) are the most important targets of noise-induced effects, being the most sensitive cell types. The aim of this study was to examine the effects of noise (50 Hz-20 kHz, 80 dB sound pressure level, 14 days) on intracellular calcium levels and on the expression pattern of purinoceptors in the membrane of the OHCs of the guinea pig and to measure the stiffness changes of the lateral membrane of these cells. In noise-exposed animals, the resting intracellular calcium concentration increased compared to nontreated animals and was slightly higher in the cells of the basal (219 +/- 29 nM: ) than in the apical (181 +/- 24 nM: ) turns of the cochlea. After application of 180 muM: adenosine triphosphate, the intracellular calcium level rose by 60 +/- 22 nM: in cells from the apical and by 44 +/- 10 nM: in cells from the basal turns, significantly less than in nontreated animals. Expression of the P(2X1), P(2X2), P(2X4), P(2X7), P(2Y1) and P(2Y4) receptor subtypes was suppressed, while expression of the P(2Y2) subtype did not decrease in either of the two preparations. In parallel with the increase in intracellular calcium concentration, the stiffness of the lateral wall of the OHCs was increased. Noise-induced changes in intracellular calcium homeostasis and subsequently in the calcium-dependent regulatory mechanisms may modify OHC lateral wall stiffness and may lead to reduction of the efficacy of the cochlear amplifier.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban Adenosine Adenosine Triphosphate adverse effects Animal Animals Calcium Cell Membrane Cells Cochlea Cytoplasm drug effects Female Guinea Pigs Hair Cells,Outer Hungary Male metabolism Noise pharmacology physiology Receptors,Purinergic Research Support
Megjelenés:	The Journal Membrane Biology. - 213 : 3 (2006), p. 135-141. -
További szerzők:	Szappanos Henrietta (1976-) (biológus, élettanász) Batta József Tamás (1970-) (fül-orr-gégész) Tóth Andrea (1973-) (fül-orr-gégész) Szigeti Gyula (1969-) (élettanász, elektrofiziológus) Panyi György (1966-) (biofizikus) Csernoch László (1961-) (élettanász) Sziklai István (1954-) (fül-orr-gégész)
Internet cím:	elektronikus változat DOI
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