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001-es BibID:	BIBFORM004333
Első szerző:	Choi, Sung Hee
Cím:	Characterization of the interaction of phorbol esters with the C1 domain of MRCK (myotonic dystrophy kinase-related Cdc42 binding kinase) alpha/beta / Choi S. H., Czifra G., Kedei N., Lewin N. E., Lázár J., Pu Y., Marquez V. E., Blumberg P. M.
Dátum:	2008
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	The Journal of Biological Chemistry 283 : 16 (2008), p. 10543-10549. -
További szerzők:	Czifra Gabriella (1975-) (élettanász) Kedei Noémi Lewin, Nancy E. Lázár József Pu, Yongmei Marquez, Victor E. Blumberg, Peter M.
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001-es BibID:	BIBFORM095956
035-os BibID:	(Scopus)85113278549 (cikkazonosító)101015 (WOS)000706408900003 (PubMed)34329682
Első szerző:	Diszházi Gyula (gyógyszerész)
Cím:	TRPM4 links calcium signaling to membrane potential in pancreatic acinar cells / Gyula Diszházi, Zsuzsanna É. Magyar, Erika Lisztes, Edit Tóth-Molnár, Péter P. Nánási, Rudi Vennekens, Balázs I. Tóth, János Almássy
Dátum:	2021
ISSN:	0021-9258 1083-351X
Megjegyzések:	TRPM4 is a Ca2+-activated nonselective cation channel that mediates membrane depolarization. Although, a current with the hallmarks of a TRPM4-mediated current has been previously reported in pancreatic acinar cells (PAC), the role of TRPM4 in the regulation of acinar cell function has not yet been explored. In the present study, we identify this TRPM4 current and describe its role in context of Ca2+ signaling of PACs using pharmacological tools and TRPM4-deficient mice. We found a significant Ca2+-activated cation current in PACs that was sensitive to the TRPM4 inhibitors 9-phenanthrol and CBA (4-Chloro-2-[[2-(2-chlorophenoxy)acetyl]amino]benzoic acid). We demonstrated that the CBA-sensitive current was responsible for a Ca2+-dependent depolarization of PACs from a resting membrane potential of -44.4 ? 2.9 to -27.7 ? 3 mV. Furthermore, we showed that Ca2+ influx was higher in the TRPM4 KO- and CBA-treated PACs than in control cells. As hormone induced repetitive Ca2+ transients partially rely on Ca2+ influx in PACs, the role of TRPM4 was also assessed on Ca2+ oscillations elicited by physiologically relevant concentrations of the cholecystokinin analogue cerulein. These data show that the amplitude of Ca2+ signals were significantly higher in TRPM4 KO than in control PACs. Our results suggest that PACs are depolarized by TRPM4 currents to an extent that results in a significant reduction of the inward driving force for Ca2+. In conclusion, TRPM4 links intracellular Ca2+ signaling to membrane potential as a negative feedback regulator of Ca2+ entry in PACs.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban folyóiratcikk pancreatic acinar cells calcium signaling ion channels
Megjelenés:	Journal of Biological Chemistry. - 297 : 3 (2021), p. 101015. -
További szerzők:	Magyar Zsuzsanna Édua (1993-) (molekuláris biológus) Lisztes Erika (1986-) (élettanász) Tóth-Molnár Edit Nánási Péter Pál (1956-) (élettanász) Vennekens, Rudi Tóth István Balázs (1978-) (élettanász) Almássy János (1981-) (élettanász, biológus, angol-magyar szakfordító)
Pályázati támogatás:	FK_135130 OTKA FK_134725 OTKA GINOP-2.3.2-15-2016-00040 GINOP
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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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001-es BibID:	BIBFORM009182
Első szerző:	Oddoux, Sarah
Cím:	Triadin deletion induces impaired skeletal muscle function / Oddoux, S., Brocard, J., Schweitzer, A., Szentesi, P., Giannesini, B., Brocard, J., Faure, J., Pernet-Gallay, K., Bendahan, D., Lunardi, J., Csernoch, L., Marty, I.
Dátum:	2009
ISSN:	1083-351X
Megjegyzések:	Triadin is a multiple proteins family, some isoforms being involved in muscle excitation-contraction coupling, and some having still unknown functions. In order to obtain clues on triadin functions, we engineered a triadin knock out mouse line, and characterized the physiological effect of triadin ablation on skeletal muscle function. These mice presented a reduced muscle strength, which seemed not to alter their survival, and which has been characterized in the present work. We first checked in these mice the expression level of the different proteins involved in calcium homeostasis, and observed in fast muscles an increase in expression of dihydropyridine receptor, with a large reduction in calsequestrin expression. Electron microscopy analysis of KO muscles morphology demonstrated the presence of triads in abnormal orientation, and a reduction in the sarcoplasmic reticulum terminal cisternae volume. Using calcium imaging on cultured myotubes, we observed a reduction in the total amount of calcium stored in the sarcoplasmic reticulum. Physiological studies have been performed to evaluate the influence of triadin deletion on skeletal muscle function. Muscle strength has been measured both on whole animal, using hang test or electrical stimulation combined with NMR analysis and strength measurement, or on isolated muscle using electrical stimulation. All the results obtained demonstrate an important reduction in muscle strength, indicating that triadin plays an essential role in skeletal muscle function and in skeletal muscle structure. These results indicate that triadin alteration lead to the development of a myopathy, which could be studied using this new animal model.
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:	Journal of Biological Chemistry. - 284 : 50 (2009), p. 34918-34929. -
További szerzők:	Brocard, Julie Schweitzer, Annie Szentesi Péter (1967-) (élettanász) Giannesini, Benoit Brocard, Jacques Faure, Julien Pernet-Gallay, Karine Bendahan, David Lunardi, Joel Csernoch László (1961-) (élettanász) Marty, Isabelle
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