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1.

001-es BibID:BIBFORM079916
035-os BibID:(WoS)000468321900014 (Scopus)85060466641 (PubMed)30685438
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Expression of BK channels and Na+-K+ pumps in the apical membrane of lacrimal acinar cells suggests a new molecular mechanism for primary tear-secretion / János Almássy, Gyula Diszházi, Marianna Skaliczki, Ildikó Márton, Zsuzsanna Édua Magyar, Péter P. Nánási, David I. Yule
Dátum:2019
ISSN:1542-0124
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Acinar cell
BK channel
Fluid secretion
Lacrimal gland
Na(+)-K(+) ATP-ase
Tear
maxiK
Megjelenés:Ocular Surface. - 17 : 2 (2019), p. 272-277. -
További szerzők:Diszházi Gyula (1992-) (gyógyszerész) Skaliczki Marianna Márton Ildikó (1954-) (fogszakorvos) Magyar Zsuzsanna Édua (1993-) (molekuláris biológus) Nánási Péter Pál (1956-) (élettanász) Yule, David I.
Pályázati támogatás:NKFIH PD112199
egyéb
NKFIH K115397
egyéb
GINOP-2.3.2-15-2016-00040
GINOP
EFOP-3.6.2-16-2017-00006
EFOP
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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
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Intézményi repozitóriumban (DEA) tárolt változat
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3.

001-es BibID:BIBFORM049387
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Apical Ca2+-activated K+-channels in mouse parotid acinar cells / Janos Almassy, Ted Begenisich, David Yule
Dátum:2012
ISSN:0006-3495
Megjegyzések:Ca2+ activation of Cl-- and K+-channels are key events underlying stimulated fluid secretion from parotid salivary glands. Cl--channels are exclusively present on the apical plasma membrane (PM) while the localization of K+-channels has not been established. Mathematical models have suggested that localization of some K+-channels to the apical PM is optimum for fluid secretion. A combination of whole cell electrophysiology and temporally resolved digital imaging with local manipulation of intracellular [Ca2+] was used to investigate if Ca2+-activated K+-channels are present in the apical PM of parotid acinar cells. Initial experiments established Ca2+ buffering conditions that produced brief, localized increases in [Ca2+] following focal laser photolysis of caged-Ca2+. Conditions were employed to isolate K+ and Cl- conductances. Photolysis at the apical PM resulted in a robust increase in K+ and Cl- currents. A localized reduction in [Ca2+] at the apical PM following photolysis of Diazo-2, a caged-Ca2+ chelator, resulted in a decrease in both K+ and Cl- currents. The K+ currents evoked by apical photolysis were partially blocked by both paxilline and TRAM-34, specific blockers of BK and IK respectively and almost abolished by incubation with both antagonists. Apical TRAM-34 sensitive K+ currents were also observed in BK null parotid acini. In contrast, when the [Ca2+] was increased at the basal PM no increase in either K+ or Cl- currents was evoked. These data provide strong evidence that K+- and Cl--channels are similarly distributed in the apical PM. Furthermore, both IK and BK channels are present in this domain and that the density of these channels appears higher in the apical vs. basal PM. In total, this study provides support for a model in which fluid secretion is optimized following expression of K+-channels specifically in the apical PM.
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
calcium release
Megjelenés:Biophysical Journal. - 102 : 3 (2012), p. 650a-651a. -
További szerzők:Begenisich, Ted B. Yule, David I.
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4.

001-es BibID:BIBFORM049383
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Apical Ca2+ activated K+ channels in mouse lacrimal acinar cells / Janos Almassy, David I. Yule
Dátum:2013
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
Lacrimal Acinar Cell
Megjelenés:Biophysical Journal. - 104 : 2 (2013), p. 474a. -
További szerzők:Yule, David I.
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Intézményi repozitóriumban (DEA) tárolt változat
DOI
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5.

001-es BibID:BIBFORM049159
035-os BibID:PMID:22291145
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Apical Ca2+-activated potassium channels in mouse parotid acinar cells / Janos Almassy, Jong Hak Won, Ted B. Begenisich, David I. Yule
Dátum:2012
Megjegyzések:Ca2+ activation of Cl and K channels is a key event underlying stimulated fluid secretion from parotid salivary glands. Cl channels are exclusively present on the apical plasma membrane (PM), whereas the localization of K channels has not been established. Mathematical models have suggested that localization of some K channels to the apical PM is optimum for fluid secretion. A combination of whole cell electrophysiology and temporally resolved digital imaging with local manipulation of intracellular [Ca2+] was used to investigate if Ca2+-activated K channels are present in the apical PM of parotid acinar cells. Initial experiments established Ca2+-buffering conditions that produced brief, localized increases in [Ca2+] after focal laser photolysis of caged Ca2+. Conditions were used to isolate K+ and Cl? conductances. Photolysis at the apical PM resulted in a robust increase in K+ and Cl? currents. A localized reduction in [Ca2+] at the apical PM after photolysis of Diazo-2, a caged Ca2+ chelator, resulted in a decrease in both K+ and Cl? currents. The K+ currents evoked by apical photolysis were partially blocked by both paxilline and TRAM-34, specific blockers of large-conductance "maxi-K" (BK) and intermediate K (IK), respectively, and almost abolished by incubation with both antagonists. Apical TRAM-34?sensitive K+ currents were also observed in BK-null parotid acini. In contrast, when the [Ca2+] was increased at the basal or lateral PM, no increase in either K+ or Cl? currents was evoked. These data provide strong evidence that K and Cl channels are similarly distributed in the apical PM. Furthermore, both IK and BK channels are present in this domain, and the density of these channels appears higher in the apical versus basolateral PM. Collectively, this study provides support for a model in which fluid secretion is optimized after expression of K channels specifically in the apical PM.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
parotid cell
Megjelenés:Jopurnal of General Physiology. - 139 : 2 (2012), p. 121-133. -
További szerzők:Won, Jong Hak Begenisich, Ted B. Yule, David I.
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Intézményi repozitóriumban (DEA) tárolt változat
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6.

001-es BibID:BIBFORM049157
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Studying the Activation of Epithelial Ion Channels Using Global Whole-field Photolysis / Janos Almassy, David I. Yule
Dátum:2013
Megjegyzések:The production of saliva by parotid acinar cells is stimulated by Ca2+ activation of Cl? and K+ channelslocated in the apical plasma membrane of these polarized cells. Here we provide a detailed description of a flash photolysis experiment designed to give a global and relatively uniform photorelease of inositol 1,4,5-trisphosphate (InsP3) or Ca2+ from caged precursors (NPE-InsP3 or NP-EGTA) combined with the simultaneous measurement of whole-cell Ca2+-activated currents. The photolysis light source can be either an ultraviolet (UV) flash lamp or alternatively the output from a 375-nm diodelaser, which is defocused to illuminate the entire field.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
whole field photolysis
Megjelenés:Cold Spring Harbor Protocols 1 (2013), p. 1-7. -
További szerzők:Yule, David I.
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Intézményi repozitóriumban (DEA) tárolt változat
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7.

001-es BibID:BIBFORM049158
035-os BibID:PMID:23282631
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Photolysis of Caged Compounds : studying Ca2+ Signaling and Activation of Ca2+-dependent Ion Channels / Janos Almassy, David I. Yule
Dátum:2013
Megjegyzések:wide variety of signaling molecules have been chemically modified by conjugation to a photolabile chromophore to render the substance temporarily biologically inert. Subsequent exposure to ultraviolet (UV) light can release the active moiety from the "caged" precursor in an experimentally controlled manner. This allows the concentration of active molecule to be precisely manipulated in both time and space. These techniques are particularly useful in experimental protocols designed to investigate the mechanisms underlying Ca2+ signaling and the activation of Ca2+-dependent effectors.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
whole field photolysis
caged compounds
Megjelenés:Cold Spring Harbor Protocols 1 (2013), p. 1-5. -
További szerzők:Yule, David I.
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8.

001-es BibID:BIBFORM049156
035-os BibID:PMID:23282644
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Investigating ion channel distribution using a combination of spatially limited photolysis, Ca2+ imaging, and patch clamp recording / Janos Almassy, David I. Yule
Dátum:2013
Megjegyzések:The production of saliva by parotid acinar cells is stimulated by Ca2+ activation of Cl? and K+ channels located in the apical plasma membrane of these polarized cells. Here, we utilize a combination of spatially limited flash photolysis, Ca2+ imaging, and electrophysiological recording to investigate the distinct distribution of Ca2+-dependent ion channels in the plasma membrane (PM) of enzymatically isolated murine parotid acinar cells. In these experiments, the aim of photolysis is to selectively target and modify the activity of ion channels, thereby revealing membrane-domain-specific differences in distribution. Specifically, the relative distribution of channels to either apical or basal PM can be investigated. Since there is substantial evidence that Ca2+-dependent Cl? channels are exclusively localized to the apical membrane of acinar cells, this provides an important electrophysiologicalverification that a particular membrane has been specifically targeted.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
human myofibroblast
photolysis
patch clamp
Megjelenés:Cold Spring Harbor Protocols 1 (2013), p. 1-6. -
További szerzők:Yule, David I.
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9.

001-es BibID:BIBFORM049155
Első szerző:Almássy János (élettanász, biológus, angol-magyar szakfordító)
Cím:Analyzing Ca2+ Dynamics in Intact Epithelial Cells Using Spatially Limited Flash Photolysis / Janos Almassy, David I. Yule
Dátum:2013
Megjegyzések:The production of saliva by parotid acinar cells is stimulated by Ca(2+) activation of Cl(-) and K(+) channels located in the apical plasma membrane of these polarized cells. Here we describe a paradigm for the focal photorelease of either Ca(2+) or an inositol 1,4,5 trisphosphate (InsP(3)) analog. The protocol is designed to be useful for investigating subcellular Ca(2+) dynamics in polarized cells with minimal experimental intervention. Parotid acinar cells are loaded with cell-permeable versions of the caged precursors (NP-EGTA-AM or Ci-InsP(3)/PM). Photolysis is accomplished using a spatially limited, focused diode laser, but the experiment can be readily modified to whole-field photolysis using a xenon flash lamp.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
human myofibroblast
photolysis
Megjelenés:Cold Spring Harbor Protocols 1 (2013), p. 1-4. -
További szerzők:Yule, David I.
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10.

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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