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001-es BibID:BIBFORM077738
035-os BibID:(WoS)000469213300008 (Scopus)85066271383 (PubMed)30517027
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Brief structural insight into the allosteric gating mechanism of BK (Slo1) channel / János Almássy, Péter P. Nánási
Dátum:2019
ISSN:0008-4212
Megjegyzések:The big conductance Ca2+-dependent K+ channel, also known as BK, MaxiK, Slo1, or KCa1.1, is a ligand- and voltage-gated K+ channel. Although structure-function studies of the past decades, involving mutagenesis and electrophysiological measurements, revealed fine details of the mechanism of BK channel gating, the exact molecular details remained unknown until the quaternary structure of the protein has been solved at a resolution of 3.5 ?A using cryo-electron microscopy. In this short review, we are going to summarize these results and interpret the gating model of the BK channel in the light of the recent structural results.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
BK channel
Megjelenés:Canadian Journal Of Physiology And Pharmacology. - 97 : 6 (2019), p. 498-502. -
További szerzők:Nánási Péter Pál (1956-) (élettanász)
Pályázati támogatás:OTKA K115307
OTKA
GINOP-2.3.2-15-2016-00040
GINOP
EFOP-3.6.2-16-2017-00006
EFOP
Internet cím:DOI
Intézményi repozitóriumban (DEA) tárolt változat
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2.

001-es BibID:BIBFORM074550
035-os BibID:(WoS)000427631700003 (Scopus)85040654509 (PubMed)29344775
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:New saliva secretion model based on the expression of Na+-K+ pump and K+ channels in the apical membrane of parotid acinar cells / Almássy János, Siguenza Elias, Skaliczki Marianna, Matesz Klara, Sneyd James, Yule David I., Nánási Péter P.
Dátum:2018
ISSN:0031-6768
Megjegyzések:The plasma membrane of parotid acinar cells is functionally divided into apical and basolateral regions. According to the current model, fluid secretion is driven by transepithelial ion gradient, which facilitates water movement by osmosis into the acinar lumen from the interstitium. The osmotic gradient is created by the apical Cl? efflux and the subsequent paracellular Na+ transport. In this model, the Na+-K+ pump is located exclusively in the basolateral membrane and has essential role in salivary secretion, since the driving force for Cl? transport via basolateral Na+?K+?2Cl? cotransport is generated by the Na+-K+ pump. In addition, the continuous electrochemical gradient for Cl? flow during acinar cell stimulation is maintained by the basolateral K+ efflux. However, using a combination of single-cell electrophysiology and Ca2+-imaging, we demonstrate that photolysis of Ca2+ close to the apical membrane of parotid acinar cells triggered significant K+ current, indicating that a substantial amount of K+ is secreted into the lumen during stimulation. Nevertheless, the K+ content of the primary saliva is relatively low, suggesting that K+ might be reabsorbed through the apical membrane. Therefore, we investigated the localization of Na+-K+ pumps in acinar cells. We show that the pumps appear evenly distributed throughout the whole plasma membrane, including the apical pole of the cell. Based on these results, a new mathematical model of salivary fluid secretion is presented, where the pump reabsorbs K+ from and secretes Na+ to the lumen, which can partially supplement the paracellular Na+ pathway.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Parotid acinar cell
Saliva production
Fluid secretion model
Na+-K+ pump
BK channel
maxiK
Gardos channel
Megjelenés:Pflugers Archiv-European Journal Of Physiology. - 470 : 4 (2018), p. 613-621. -
További szerzők:Siguenza, Elias Skaliczki Marianna Matesz Klára (1949-) (anatómus, neurobiológus) Sneyd, James Yule, David I. Nánási Péter Pál (1956-) (élettanász)
Pályázati támogatás:GINOP-2.3.2-15-2016-00040
GINOP
EFOP-3.6.2-16-2017-00006
EFOP
Internet cím:Szerző által megadott URL
DOI
Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM082980
035-os BibID:(WoS)000511350000001 (Scopus)85079060274 (PubMed)31917868
Első szerző:Fanczal Júlia
Cím:TRPM2-mediated extracellular Ca2+ entry promotes acinar cell necrosis in biliary acute pancreatitis / Júlia Fanczal, Petra Pallagi, Marietta Görög, Gyula Diszházi, János Almássy, Tamara Madácsy, Árpád Varga, Péter Csernay-Biró, Xénia Katona, Emese Tóth, Réka Molnár, Zoltán Rakonczay, Péter Hegyi, József Maléth
Dátum:2020
ISSN:0022-3751 1469-7793
Megjegyzések:Acute biliary pancreatitis poses a significant clinical challenge as currently no specific pharmaceutical treatment exists. Disturbed intracellular Ca2+ signalling caused by bile acids is a hallmark of the disease, which induces increased reactive oxygen species (ROS) production, mitochondrial damage, intra-acinar digestive enzyme activation and cell death. Because of this mechanism of action, prevention of toxic cellular Ca2+ overload is a promising therapeutic target. Transient Receptor Potential Melastatin 2 (TRPM2) is a non-selective cation channel that has recently emerged as an important contributor to oxidative-stress-induced cellular Ca2+ overload across different diseases. However, the expression and possible functions of TRPM2 in the exocrine pancreas remain unknown. Here we found that TRPM2 is expressed in the plasma membrane of mouse pancreatic acinar and ductal cells, which can be activated by increased oxidative stress induced by H2O2 treatment. TRPM2 activity was found to contribute to bile acid-induced extracellular Ca2+ influx in acinar cells, but did not have the same effect in ductal cells. The generation of intracellular ROS in response to bile acids was remarkably higher in pancreatic acinar cells compared to isolated ducts, which can explain the difference between acinar and ductal cells. This activity promoted acinar cell necrosis in vitroindependently from mitochondrial damage or mitochondrial fragmentation. In addition, bile-acid-induced experimental pancreatitis was less severe in TRPM2 knockout mice, whereas the lack of TRPM2 had no protective effect in cerulein induced acute pancreatitis. Our results suggest that the inhibition of TRPM2 may be a potential treatment option for biliary pancreatitis.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Ca2+ signalling
TRPM2 channel
acinar cell necrosis
acute pancreatitis
bile acid
epithelial ion transport
Megjelenés:Journal of Physiology. - 598 : 6 (2020), p. 1253-1270. -
További szerzők:Pallagi Petra Görög Marietta Diszházi Gyula (1992-) (gyógyszerész) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Madácsy Tamara Varga Árpád Csernay-Biró Péter Katona Xénia Tóth Emese Molnár Réka Rakonczay Zoltán Hegyi Péter Jenő (belgyógyász) Maléth József
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DOI
Intézményi repozitóriumban (DEA) tárolt változat
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4.

001-es BibID:BIBFORM076044
035-os BibID:(WoS)000436909600011 (Scopus)85054071643 (PubMed)29769426
Első szerző:Horváth Balázs (élettanász)
Cím:Effect of the intracellular calcium concentration chelator BAPTA acetoxy-methylester on action potential duration in canine ventricular myocytes / B. Horvath, N. Szentandrassy, R. Veress, D. Baranyai, K. Kistamas, J. Almassy, A. Toth, J. Magyar, T. Banyasz, P. P. Nanasi
Dátum:2018
Megjegyzések:Intracellular calcium concentration ([Ca2+]i) is often buffered by using the cell-permeant acetoxy-methylester form of the Ca2+ chelator BAPTA (BAPTA-AM) under experimental conditions. This study was designed to investigate the time-dependent actions of extracellularly applied BAPTA-AM on action potential duration (APD) in cardiac cells. Action potentials were recorded from enzymatically isolated canine ventricular myocytes with conventional sharp microelectrodes. The effect of BAPTA-AM on the rapid delayed rectifier K+ current (IKr) was studied using conventional voltage clamp and action potential voltage clamp techniques. APD was lengthened by 5 ?M BAPTA-AM - but not by BAPTA - and shortened by the Ca2+ ionophore A23187 in a time-dependent manner. The APD-lengthening effect of BAPTA-AM was strongly suppressed in the presence of nisoldipine, and enhanced in the presence of BAY K8644, suggesting that a shift in the [Ca2+]i-dependent inactivation of L-type Ca2+ current may be an important underlying mechanism. However, in the presence of the IKr-blocker dofetilide or E-4031 APD was shortened rather than lengthened by BAPTA-AM. Similarly, the APD-lengthening effect of 100 nM dofetilide was halved by the pretreatment with BAPTA-AM. In line with these results, IKr was significantly reduced by extracellularly applied BAPTA-AM under both conventional voltage clamp and action potential voltage clamp conditions. This inhibition of IKr was partially reversible and was not related to the Ca2+ chelator effect BAPTA-AM. The possible mechanisms involved in the APD-modifying effects of BAPTA-AM are discussed. It is concluded that BAPTA-AM has to be applied carefully to control [Ca2+]i in whole cell systems because of its direct inhibitory action on IKr.
Tárgyszavak:idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
calcium chelators
intracellular calcium concentration
action potential duration
cardiac ion currents
potassium ion
currents
ventricular myocytes
Megjelenés:Journal of Physiology and Pharmacology. - 69 : 1 (2018), p. 99-107. -
További szerzők:Szentandrássy Norbert (1976-) (élettanász) Veress Roland (1992-) (molekuláris biológus) Baranyai Dóra Kistamás Kornél (1986-) (biológus) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Tóth A. (farmakológus) Magyar János (1961-) (élettanász) Bányász Tamás (1960-) (élettanász) Nánási Péter Pál (1956-) (élettanász)
Pályázati támogatás:NKFIHK-115397
NKFIH
NKFIH-K109736
NKFIH
NKFIH-PD120794
NKFIH
OTKA ANN-113273
OTKA
GINOP-2.3.2-15-2016-00040
GINOP
EFOP-3.6.2-16-2017-00006
EFOP
UNKP-17-4-III-DE-201
UNKP
Internet cím:Intézményi repozitóriumban (DEA) tárolt változat
DOI
Borító:

5.

001-es BibID:BIBFORM049153
035-os BibID:PMID:23907822
Első szerző:Kemény Lajos V. (bőrgyógyász Szeged)
Cím:Na+/Ca2+ exchangers regulate the migration and proliferation of human gastric myofibroblasts / Lajos V. Kemény, Andrea Schnúr, Mátyás Czepán, Zoltán Rakonczay, Jr., Eleonóra Gál, János Lonovics, György Lázár, Zsolt Simonka, Viktória Venglovecz, József Maléth, Linda Judák, István B. Németh, Kornélia Szabó, János Almássy, László Virág, Andrea Geisz, László Tiszlavicz, David I. Yule, Tibor Wittmann, Andrea Varró, Péter Hegyi
Dátum:2013
Megjegyzések:Gastrointestinal myofibroblasts are contractile, electrically nonexcitable, transitional cells that play a role in extracellular matrix production, in ulcer healing, and in pathophysiological conditions they contribute to chronic inflammation and tumor development. Na+/Ca2+ exchangers (NCX) are known to have a crucial role in Ca2+ homeostasis of contractile cells, however, no information is available concerning the role of NCX in the proliferation and migration of gastrointestinal myofibroblasts. In this study, our aim was to investigate the role of NCX in the Ca2+ homeostasis, migration, and proliferation of human gastrointestinal myofibroblasts, focusing on human gastric myofibroblasts (HGMs). We used microfluorometric measurements to investigate the intracellular Ca2+ and Na+ concentrations, PCR analysis and immunostaining to show the presence of the NCX, patch clamp for measuring NCX activity, and proliferation and migration assays to investigate the functional role of the exchanger. We showed that 53.0±8.1% of the HGMs present Ca2+ oscillations, which depend on extracellular Ca2+ and Na+, and can be inhibited by NCX inhibitors. NCX1, NCX2, and NCX3 were expressed at both mRNA and protein levels in HGMs, and they contribute to the intracellular Ca2+ and Na+ homeostasis as well, regardless of the oscillatory activity. NCX inhibitors significantly blocked the basal and insulin-like growth factor II-stimulated migration and proliferation rates of HGMs. In conclusion, we showed that NCX plays a pivotal role in regulating the Ca2+ homeostasis, migration, and proliferation of HGMs. The inhibition of NCX activity may be a potential therapeutic target in hyperproliferative gastric diseases.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
calcium oscillation
sodium-calcium exchanger
human myofibroblast
Megjelenés:American journal of physiology. Gastrointestinal and liver physiology. - 305 : 8 (2013), p. G552-G563. -
További szerzők:Schnúr Andrea Czepán Mátyás Rakonczay Zoltán Jr. Gál Eleonóra Lonovics János (Szeged) Lázár György Simonka Zsolt Venglovecz Viktória Maléth József Judák Linda Németh István Balázs Szabó Kornélia Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Virág László (élettanász Szeged) Geisz Andrea Tiszlavicz László Yule, David I. Wittmann Tibor Varró Andrea Hegyi Péter Jenő (belgyógyász)
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6.

001-es BibID:BIBFORM094525
035-os BibID:(WoS)000651650200001 (Scopus)85106224539 (PubMed)34008188
Első szerző:Matta Csaba (molekuláris biológus, genetikus, angol szakfordító)
Cím:Transcriptome-based screening of ion channels and transporters in a migratory chondroprogenitor cell line isolated from late-stage osteoarthritic cartilage / Csaba Matta, Rebecca Lewis, Christopher Fellows, Gyula Diszhazi, Janos Almassy, Nicolai Miosge, James Dixon, Marcos C. Uribe, Sean May, Szilard Poliska, Richard Barrett-Jolley, Janos Fodor, Peter Szentesi, Tibor Hajdú, Aniko Keller-Pinter, Erin Henslee, Fatima H. Labeed, Michael P. Hughes, Ali Mobasheri1
Dátum:2021
ISSN:0021-9541 1097-4652
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Megjelenés:Journal of Cellular Physiology. - 236 : 11 (2021), p. 7421-7439. -
További szerzők:Lewis, Rebecca Fellows, Christopher R. Diszházi Gyula (1992-) (gyógyszerész) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító) Miosge, Nicolai Dixon, James E. Uribe, Marcos C. May, Sean Póliska Szilárd (1978-) (biológus) Barrett-Jolley, Richard Fodor János (1973-) (élettanász, biotechnológus) Szentesi Péter (1967-) (élettanász) Hajdú Tibor (1988-) (általános orvos) Keller-Pintér Anikó Henslee, Erin Labeed, Fatima H. Hughes, Michael P. Mobasheri, Ali
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Intézményi repozitóriumban (DEA) tárolt változat
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7.

001-es BibID:BIBFORM077837
035-os BibID:(PMID)29792814 (WoS)000438114100006 (Scopus)85049826983
Első szerző:Nánási Péter Pál ifj. (sejtbiológus)
Cím:Perspectives of a myosin motor activator agent with increased selectivity / Péter Nánási Jr., István Komáromi, János Almássy
Dátum:2018
ISSN:0008-4212
Megjegyzések:Clinical treatment of heart failure is still not fully solved. A novel class of agents, the myosin motor activators, acts directly on cardiac myosin resulting in an increased force generation and prolongation of contraction. Omecamtiv mecarbil, the lead molecule of this group, is now in human 3 phase displaying promising clinical performance. However, omecamtiv mecarbil is not selective to myosin, since it readily binds to and activates cardiac ryanodine receptors (RyR-2), an effect that may cause complications is case of overdose. In this study, in silico analysis was performed to investigate the docking of omecamtiv mecarbil and other structural analogues to cardiac myosin heavy chain and RyR-2 in order to select the structure which has a higher selectivity to myosin over RyR-2. In silico docking studies revealed that omecamtiv mecarbil has comparable affinity to myosin and RyR-2: the respective K values are 0.60 and 0.87 ?M. Another compound CK-1032100 has much lower affinity to RyR-2 than omecamtiv mecarbil, while it still has a moderate affinity to myosin. It was concluded that further research starting from the chemical structure of CK-1032100 may result a better myosin activator burdened probably less by the RyR-2 binding side effect. It also is possible, however, that the selectivity of omecamtiv mecarbil to myosin over RyR-2 cannot be substantially improved, because similar moieties seem to be responsible for the high affinity to both myosin and RyR-2.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Inotropic agents
Myosin activators
Omecamtiv mecarbil
Ryanodine receptor
Cytosolic Ca 2+
Megjelenés:Canadian Journal of Physiology and Pharmacology. - 96 : 7 (2018), p. 676-680. -
További szerzők:Komáromi István (1957-) (vegyész, molekuláris biológus, biokémikus) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító)
Pályázati támogatás:NKFIH PD112199
Egyéb
Internet cím:Szerző által megadott URL
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Intézményi repozitóriumban (DEA) tárolt változat
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