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1.

001-es BibID:BIBFORM049403
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Investigation of ryanodine receptor using peptide toxins / J. Almassy, S. Sarkozi, I. Jona
Dátum:2010
ISSN:0231-424X 1588-2683
Megjegyzések:Action potential of the skeletal muscle surface membrane leads to Ca2+ release from the sarcoplasmic reticulum evoked by direct coupling between dihydropyridine receptor (DHPR) and Ca2+ release channel (RyR). The structural basis of the allosteric connection is the intracellular loop between the 2nd and 3rd transmembrane repeat of the DHPR ?1 subunit. We previously showed that a ?-scorpion toxin maurocalcine (MCa) that shares primary sequence homology with the amino acid residues of DHPR-loop peptide essential for RyR activation raises single RyR channel open probability and blocks RyR in long lasting subconductive states These long lasting subconductance events characterised by mean event duration, which is about 12 secs for the wild type toxin. Using peptide where one charged amino acid (at a time) were replased with a neutral one ? wew showed that the critical amino acid is the 24th. Furtehrmore the strength of the toxin effect is proportional witht the distance of the muatted and of the 24th AA. The aimed to of this study was to confirm the hypothesis that MCa shares common binding sites with the DHPR loop peptide on RyR, and to characterize the potential effects of other MCa-homologue toxins (such as charybdotoxin (ChTx) and iberiotoxin (IbTx)) on RyR gating. Using single channel electrophysiology we demonstrated a competitive interaction between the loop peptide ? Mca and MCa ? ChTx respectively. We also found that ChTx albeit increased RyR open probability, induced long channel closures in dose-, and membrane potential- and Ca2+-dependent manner, but not in a use dependent fashion, while IbTx in spite of the significant homology was ineffective.
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Acta Physiologica Hungarica. - 97 : 3 (2010), p. 89. -
További szerzők:Sárközi Sándor (1966-) (élettanász) Jóna István (1948-) (élettanász, fizikus)
Pályázati támogatás:81923
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2.

001-es BibID:BIBFORM049386
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Effect of scorpion toxins on the CRC/RyR function / Janos Almassy, Balazs Lukacs, Sandor Sarkozi, Istvan Jona
Dátum:2012
ISSN:0006-3495
Megjegyzések:It was shown previously that maurocalcin (MCa) induces long lasting subconductance states (LLSS) investigating the RyR function by single channel electrophysiology. These LLSSs are polarity and potential dependent and caused by the distinct positively charged surface formed by 5 amino acids corresponding to the peptide A binding site. We tested the effect of beta scorpion toxins - having a similar structure - on the RyR1 function. Charibdotoxin (CHTX) elicits close state at 20 nM in an all or none and voltage dependent manner because of smaller surface charge. Smaller size makes it easier to reach the most inner toxin binding site (out of the three) which causes the closure of the channel. MCa and CHTX share a common binding site which is identical to the peptide A binding site. Noxiustoxin has a similar effect at slightly higher toxin concentration. At nanomolar concentration Kaliotoxin evokes "flickering" of the channel in subconductance state which is occasionally interrupted by long lasting closed states, while locks the channel in closed state at micromolar concentration. Iberiotoxin induces a slight increase of the open probability accompanied by normal gating while Slotoxin has no effect. With the exception of MCa all toxins are effective only at one side, at the preferred side. Iberiotoxin and Slotoxin - ion spite of similar structure - have no large positive surfaces, they exhibit random surface charge distribution. A model has been proposed for the possible mode of action which accounts for the above effect of the tested toxins. Supported by Hungarian Research Found OTKA 81923.1563-PosB333
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Biophysical Journal. - 102 : 3 (2012), p. 306a-307a. -
További szerzők:Lukács Balázs (1978-) (élettanász) Sárközi Sándor (1966-) (élettanász) Jóna István (1948-) (élettanász, fizikus)
Pályázati támogatás:81923
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3.

001-es BibID:BIBFORM049381
Első szerző:Bárdi Miklós
Cím:The effect of phenol derivatives on the sr Ca2+-atpase / Bardi M., Sarkozi S., Jona I.
Dátum:2012
Megjegyzések:During the contraction of a skeletal muscle fiber an action potential running along the fiber surface membrane results in the conformational change of the dihydropyridine receptors which in turn causes the opening of the sarcoplasmic reticulum (SR) calcium channels (RyR1). Calcium ions - released from the SR through the channels ? increase the myoplasmic calcium concentration that finally evokes the contraction of the fibre. The decrease in the myoplasmic calcium concentration causing relaxation of the fiber is achieved by the action of the SR Ca2+-ATPase (SERCA).It's known from the literature and our earlier results that thymol and its structural analogues ? which are widely used in the food, cosmetic and pharmaceutical industry as preservatives ? have influence on the activity of the RyR1 and SERCA. Continuing our previous work our aim was to study the effect of further phenol derivatives on the SERCA.Light SR (LSR) vesicles were prepared from rabbit skeletal muscle (m. longissimus dorsi) containing the SR Ca2+-pump in their membrane. ATP dependent hydrolytic activity of LSR vesicles was measured using "coupled enzyme assay" at 37oC. Specific activity of SERCA was calculated after determination of the non-specific activity in the presence of 20 ?M cyclopiazonic acid which specifically blocks SERCA.Pump activities were plotted against the concentration values of different drugs, dots were fitted by Hill-equation revealing the following parametes:4-Chloro-meta-crezol IC50=167 ? 8 ?M, nHill ~3;5-Chloro-orho-crezol IC50=554 ? 45 ?M, nHill ~2,4-Chloro-ortho-crezol IC50=1370 ? 88 ?M, nHill ~8.Almost all the compounds investigated here inhibited the pump except cresol which didn't exert any effect in concentration range 0?3 mM. Other compounds inhibited SERCA activity, but affinity and the number of ligands differed from each other.Our results prove that phenol derivative structural analogues have an inhibitory effect on SERCA activity but this effect is significantly modified by the relative position of the different substituent groups and the presence of cloride is also required for inhibition. The alterations in the shape of the pi electron cloud caused by the different substituents can be also involved in the effect of these compounds.Supported by: OTKA 81923
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
calcium pump
Megjelenés:Acta Physiologica. - 205 : Suppl. 690 (2012), p. P1. -
További szerzők:Sárközi Sándor (1966-) (élettanász) Jóna István (1948-) (élettanász, fizikus)
Pályázati támogatás:81923
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4.

001-es BibID:BIBFORM050035
Első szerző:Csernoch László (élettanász)
Cím:Effects of tetracaine on sarcoplasmic calcium permeability and the ryanodine receptor calcium release channel in mammalian skeletal muscle / L. Csernoch, P. Szentesi, S. Sárközi, C. Szegedi, I. Jona, L. Kovács
Dátum:1999
ISSN:0142-4319
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:Journal of Muscle Research and Cell Motility. - 20 (1999), p. 89-90. -
További szerzők:Szentesi Péter (1967-) (élettanász) Sárközi Sándor (1966-) (élettanász) Szegedi Csaba Jóna István (1948-) (élettanász, fizikus) Kovács László (1939-) (élettanász)
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5.

001-es BibID:BIBFORM049385
Első szerző:Csernoch László (élettanász)
Cím:Estimation of Pore Geometry of RyR1 using Lanthanide Ruler / Laszlo Csernoch, Janos Almassy, Sandor Sarkozi, Balazs Lukacs, Istvan Jona
Dátum:2012
ISSN:0006-3495
Megjegyzések:It was shown previously that the Ca analogue Gd inhibits RyR1 gating symmetrically with a Kd about 5.5 microM and Hill coefficient (nH) of 4 both on cis and trans side using single channel electrophysiology. We further tested the RyR1-lanthanide interaction using two lanthanides - having an ionic radii between Ca2+ and Gd3+ - by bilayer measurements and ryanodine binding experiments. Cis inhibition of RyR1 by Eu was characterized by a binding constant of Kd=167?5 nM and an nH of 2?0.1 while trans inhibition exhibits Kd=4.8?0.2 microM and nN of 5.2?1.2. The inhibition constants for Sm on the cis side are Kd=64.3?2.5 nM and nH=2.2?0.2 while on the trans side Kd=6.15?0.13 microM and nH=4.68?0.45. Inhibition by Eu and Sm are potential and polarity dependent in contrast to Gd due to the differences in ionic radii of these lanthanides. Increasing the ionic radius from 0.938 (Gd) to 0.964 (Sm) increased the binding affinity from 5.6 microM to 64.3 nM revealing that the size of Ca binding pocket is only slightly higher than the ionic radius of Sm. Ryanodine (Ry) binding experiments revealed that lanthanides bind - at least partially - to the regulatory Ca binding site because the dose response curve of 3H Ry binding starts with an increase of Ry binding, which amounts to about 40% for Eu and 70% for Sm of basic Ry binding. A model has been proposed for one possible spatial arrangement of lanthanide and calcium binding sites of the RyR1 pore based on the ionic radii of Ca and the tested lanthanides. Supported by OTKA 81923.1557-PosB327
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Biophysical Journal. - 102 : 3 Supplement (2012), p. 305a. -
További szerzők:Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Sárközi Sándor (1966-) (élettanász) Lukács Balázs (1978-) (élettanász) Jóna István (1948-) (élettanász, fizikus)
Pályázati támogatás:81923
OTKA
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6.

001-es BibID:BIBFORM042914
Első szerző:Csernoch László (élettanász)
Cím:Effects of tetracaine on sarcoplasmic calcium release in mammalian skeletal muscle fibres / László Csernoch, Péter Szentesi, Sándor Sárközi, Csaba Szegedi, István Jona, László Kovács
Dátum:1999
Megjegyzések:1. Single muscle fibres were dissociated enzymatically from the extensor digitorum communis muscle of rats. The fibres were mounted into a double Vaseline gap experimental chamber and the events in excitation-contraction coupling were studied under voltage clamp conditions in the presence and absence of the local anaesthetic tetracaine. 2. Changes in intracellular calcium concentration ([Ca2+]i) were monitored using the calcium sensitive dyes antipyrylazo III and fura-2 and the rate of calcium release (Rrel) from the sarcoplasmic reticulum (SR) was calculated. Tetracaine decreased the maximal attained [Ca2+]i and suppressed, in a dose-dependent manner, both the early peak and the steady level of Rrel in the voltage range examined. 3. The concentration dependence of the effects on the two kinetic components of Rrel were almost identical with a half-effective concentration (K50) of 70 and 71 microM and a Hill coefficient (nH) of 2.7 and 2.3 for the peak and the steady level, respectively. Furthermore, the drug did not alter the peak to steady level ratio up to a concentration (50 microM) that caused a 35 +/- 5 % reduction in calcium release. Higher concentrations did suppress the ratio but the degree of suppression was voltage independent. 4. Tetracaine (50 microM) neither influenced the total available intramembrane charge nor altered its membrane potential dependence. It shifted the transfer function, the normalized SR permeability versus normalized charge to the right, indicating that similar charge transfer caused a smaller increase in SR permeability. 5. To explore the site of action of tetracaine further the ryanodine receptor (RyR) calcium release channel of the SR was purified and reconstituted into planar lipid bilayers. The reconstituted channel had a conductance of 511 +/- 14 pS (n = 8) in symmetric 250 mM KCl that was not affected by tetracaine. Tetracaine decreased the open probability of the channel in a concentration-dependent manner with K50 = 68 microM and nH = 1.5. 6. These experiments show that tetracaine suppresses SR calcium release in enzymatic isolated mammalian skeletal muscle fibres. This effect is due, presumably, to the decreased open probability of the RyR in the presence of the drug. Since both the inactivating peak and the steady level of Rrel were equally affected by tetracaine, our observations suggest that there is a tight coupling between these kinetic components of SR calcium release in mammalian skeletal muscle.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal Of Physiology (London). - 515 : 3 (1999), p. 843-857. -
További szerzők:Szentesi Péter (1967-) (élettanász) Sárközi Sándor (1966-) (élettanász) Szegedi Csaba Jóna István (1948-) (élettanász, fizikus) Kovács László (1939-) (élettanász)
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7.

001-es BibID:BIBFORM049069
Első szerző:Estève, Eric
Cím:Critical Amino Acid Residues Determine the Binding Affinity and the Ca2+ Release Efficacy of Maurocalcine in Skeletal Muscle Cells / Eric Estève, Sophia Smida-Rezgui, Sandor Sarkozi, Csaba Szegedi, Imed Regaya, Lili Chen, Xavier Altafaj, Hervé Rochat, Paul Allen, Isaac N. Pessah, Isabelle Marty, Jean-Marc Sabatier, Istvan Jona, Michel De Waard, Michel Ronjat
Dátum:2003
ISSN:0021-9258 1083-351X
Megjegyzések:Maurocalcine (MCa) is a 33 amino acid residue peptide toxin isolated from the scorpion Scorpio maurus palmatus. MCa and mutated analogues were chemically synthesized, and their interaction with the skeletal muscle ryanodine receptor (RyR1) was studied on purified RyR1, sarcoplasmic reticulum (SR) vesicles, and cultured myotubes. MCa strongly potentiates [3H]ryanodine binding on SR vesicles (7-fold at pCa 5) with an apparent EC50 of 12 nm. MCa decreases the sensitivity of [3H]ryanodine binding to inhibitory high Ca2+ concentrations and increases it to the stimulatory low Ca2+ concentrations. In the presence of MCa, purified RyR1 channels show long-lasting openings characterized by a conductance equivalent to 60% of the full conductance. This effect correlates with a global increase in Ca2+ efflux as demonstrated by MCa effects on Ca2+ release from SR vesicles. In addition, we show for the first time that external application of MCa to cultured myotubes produces a cytosolic Ca2+ increase due to Ca2+ release from 4-chloro-m-cresol-sensitive intracellular stores. Using various MCa mutants, we identified a critical role of Arg24 for MCa binding onto RyR1. All of the other MCa mutants are still able to modify [3H]ryanodine binding although with a decreased EC50 and a lower stimulation efficacy. All of the active mutants produce both the appearance of a subconductance state and Ca2+ release from SR vesicles. Overall, these data identify some amino acid residues of MCa that support the effect of this toxin on ryanodine binding, RyR1 biophysical properties, and Ca2+ release from SR.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Biological Chemistry. - 278 : 39 (2003), p. 37822-37831. -
További szerzők:Smida-Resgui, Sophia Sárközi Sándor (1966-) (élettanász) Szegedi Csaba Regaya, Imed Chen, Li-Li Altafaj, Xavier Rochat, Hervé Allen, Paul Pessah, Isaac N. Marty, Isabelle Sabatier, Jean Marc Jóna István (1948-) (élettanász, fizikus) De Waard, Michel Ronjat, Michel
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8.

001-es BibID:BIBFORM062650
Első szerző:Jóna István (élettanász, fizikus)
Cím:Effect of magnesium and ATP on the calcium release channel : ryanodine receptor of the rat / I. Jóna, S. Sárközi, C. Szegedi, P. Szentesi, L. Kovács
Dátum:1999
ISSN:0142-4319
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:Journal of Muscle Research and Cell Motility. - 20 (1999), p. 830. -
További szerzők:Sárközi Sándor (1966-) (élettanász) Szegedi Csaba Szentesi Péter (1967-) (élettanász) Kovács László (1939-) (élettanász)
Pályázati támogatás:OTKA 22313
OTKA
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9.

001-es BibID:BIBFORM039994
Első szerző:Jóna István (élettanász, fizikus)
Cím:Altered inhibition of the rat skeletal ryanodine receptor/calcium release channel by magnesium in the presence of ATP / I. Jóna, C. Szegedi, S. Sárközi, P. Szentesi, L. Csernoch, L. Kovács
Dátum:2001
ISSN:0031-6768
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Pflugers Archiv. - 441 : 6 (2001), p. 729-738. -
További szerzők:Szegedi Csaba Sárközi Sándor (1966-) (élettanász) Szentesi Péter (1967-) (élettanász) Csernoch László (1961-) (élettanász) Kovács László (1939-) (élettanász)
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10.

001-es BibID:BIBFORM049379
Első szerző:Lukács Balázs (élettanász)
Cím:Effect of maurocalcine on the skeletal type ryanodine receptor / Lukacs B., Sarkozi S., Almassy J., Jona I.
Dátum:2012
Megjegyzések:Maurocalcine (MCa) is a 33 amino acid long scorpion toxin which shows high homology with dihydropyridine receptor constituent peptide-A (pepA). The latter is believed to directly interact with ryanodine receptor (RyR1) and plays important role in the electromechanical coupling. The position and the positive charge of given amino acids residues of MCa are determinative in this interaction.We studied the effect of pepA and potassium ion on the MCa evoked Long Lasting Subconductance State (LLSS) type RyR1 operation assuming that both of them may have access to MCa binding sites of the channel. To investigate the binding of these peptides to RyR1, we used heavy sarcoplasmic reticulum vesicles (HSR) and CHAPS solubilized ryanodine receptor complex of rabbit skeletal muscle. Gating of RyR1 was monitored on channels incorporated into a planar lipid bilayer under voltage clamp conditions. Ca2+-release measurements were performed on HSR, where changes in extravesicular Ca2+ concentration were followed as changes in the absorption of APIII Ca2+-sensitive dye (?=710 nm).In single channel experiments LLSS type RyR1 gating was evoked applying of 5 and 10 nM MCa in the cytoplasmic side of the channel. The length and frequency of the characteristic subconductance states gradually ceased by consecutively added K+. The half effective concentration of K+ was higher at 10 nM MCa concentration which refers to a possible competition between MCa and potassium ion in biding to the same site on RyR1. A similar competitive-like effect of pepA was observed, when in the presence of 26 ?M pepA, much higher concentration of MCa was able to evoke LLSSs. In Ca2+ release measurements 5 nM MCa induced Ca2+-release at 100 mM K+, but release was completely eliminated at 250 mM K+. High concentration of K+inhibited only the MCa induced Ca2+-release but had no effect on the 4-CMC induced Ca2+-release suggesting specific effect of K+ on MCa-RyR1 interaction. Suppression of release in the presence of 250 mM K+ was inhibited by addition of higher concentration of MCa suggesting charge driven interaction between MCa and RyR1.Our data put forward a possible mode of MCa action with 3 binding sites at the cytosolic side on RyR1. The first binding site located on the surface of the channel, and is responsible for the Po increase at low MCa concentration. The second binding site in the pore of the channel induces potential- and voltage dependent LLSS-s at higher toxin concentration. Occupy of third one which located presumably in the pore, close to the selectivity filter results in closed states of RyR1.Supported by: OTKA 81923
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Acta Physiologica. - 205 : Suppl. 690 (2012), 26. p. -
További szerzők:Sárközi Sándor (1966-) (élettanász) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Jóna István (1948-) (élettanász, fizikus)
Pályázati támogatás:81923
OTKA
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11.

001-es BibID:BIBFORM004115
Első szerző:Lukács Balázs (élettanász)
Cím:Charged surface area of maurocalcine determines its interaction with the skeletal ryanodine receptor / Balazs Lukacs, Monika Sztretye, Janos Almassy, Sandor Sarkozi, Beatrix Dienes, Kamel Mabrouk, Cecilia Simut, Laszlo Szabo, Peter Szentesi, Michel De Waard, Michel Ronjat, Istvan Jona, Laszlo Csernoch
Dátum:2008
Megjegyzések:The 33 amino acid scorpion toxin maurocalcine (MCa) has been shown to modify the gating of the skeletal-type ryanodine receptor (RyR1). Here we explored the effects of MCa and its mutants ([Ala(8)]MCa, [Ala(19)]MCa, [Ala(20)]MCa, [Ala(22)]MCa, [Ala(23)]MCa, and [Ala(24)]MCa) on RyR1 incorporated into artificial lipid bilayers and on elementary calcium release events (ECRE) in rat and frog skeletal muscle fibers. The peptides induced long-lasting subconductance states (LLSS) on RyR1 that lasted for several seconds. However, their average length and frequency were decreased if the mutation was placed farther away in the 3D structure from the critical (24)Arg residue. The effect was strongly dependent on the direction of the current through the channel. If the direction was similar to that followed by calcium during release, the peptides were 8- to 10-fold less effective. In fibers long-lasting calcium release events were observed after the addition of the peptides. The average length of these events correlated well with the duration of LLSS. These data suggest that the effect of the peptide is governed by the large charged surface formed by residues Lys(20), Lys(22), Arg(23), Arg(24), and Lys(8). Our observations also indicate that the results from bilayer experiments mimic the in situ effects of MCa on RyR1.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biophysical Journal. - 95 : 7 (2008), p. 3497-3509. -
További szerzők:Sztretye Mónika (1981-) (élettanász, elektrofiziológus) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Sárközi Sándor (1966-) (élettanász) Dienes Beatrix (1972-) (élettanász, molekuláris biológus) Mabrouk, Kamel Simut, Cecilia Szabó László (Románia) Szentesi Péter (1967-) (élettanász) De Waard, Michel Ronjat, Michel Jóna István (1948-) (élettanász, fizikus) Csernoch László (1961-) (élettanász)
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12.

001-es BibID:BIBFORM030264
035-os BibID:WOS:000086138300017
Első szerző:Nánási Péter Pál (élettanász)
Cím:Biphasic effect of bimoclomol on calcium handling in mammalian ventricular myocardium / Péter P. Nánási, Sándor Sárközi, Gyula Szigeti, István Jóna, Csaba Szegedi, Ágnes Szabó, Tamás Bányász, János Magyar, Péter Szigligeti, Ágnes Körtvély, László Csernoch, László Kovács, Andrea Jednákovits
Dátum:2000
ISSN:0007-1188
Megjegyzések:1 Concentration-dependent effects of bimoclomol, the novel heat shock protein coinducer, on intracellular calcium transients and contractility were studied in Langendorff-perfused guinea-pig hearts loaded with the fluorescent calcium indicator dye Fura-2. Bimoclomol had a biphasic effect on contractility: both peak left ventricular pressure and the rate of force development significantly increased at a concentration of 10 nM or higher. The maximal effect was observed between 0.1 and 1 mu M, and the positive inotropic action disappeared by further increasing the concentration of bimoclomol. The drug increased systolic calcium concentration with a similar concentration-dependence. In contrast, diastolic calcium concentration increased monotonically in the presence of bimoclomol. Thus low concentrations of the drug (10-100 nM) increased, whereas high concentrations (10 mu M) decreased the amplitude of intracellular calcium transients. 2 Effects of bimoclomol on action potential configuration was studied in isolated canine ventricular myocytes. Action potential duration was increased at low (10 nM), unaffected at intermediate (0.1-1 mu M) and decreased at high (10-100 mu M) concentrations of the drug. 3 In single canine sarcoplasmic calcium release channels (ryanodine receptor), incorporated into artificial lipid bilayer, bimoclomol significantly increased the open probability of the channel in the concentration range of 1-10 mu M. The increased open probability was associated with increased mean open time. The effect of bimoclomol was again biphasic: the open probability decreased below the control level in the presence of 1 mM bimoclomol. 4 Bimoclomol (10 mu M-1 mM) had no significant effect on the rate of calcium uptake into sarcoplasmic reticulum vesicles of the dog, indicating that in vivo calcium reuptake might not substantially be affected by the drug. 5 In conclusion, the positive inotropic action of bimoclomol is likely due to the activation of the sarcoplasmic reticulum calcium release channel in mammalian ventricular myocardium.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
egyetemen (Magyarországon) készült közlemény
Megjelenés:British Journal of Pharmacology. - 129 : 7 (2000), p. 1405-1412. -
További szerzők:Sárközi Sándor (1966-) (élettanász) Szigeti Gyula (1969-) (élettanász, elektrofiziológus) Jóna István (1948-) (élettanász, fizikus) Szegedi Csaba Szabó Ágnes Bányász Tamás (1960-) (élettanász) Magyar János (1961-) (élettanász) Szigligeti Péter Körtvély Ágnes Csernoch László (1961-) (élettanász) Kovács László (1939-) (élettanász) Jednákovits Andrea
Internet cím:DOI
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