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1.

001-es BibID:BIBFORM040112
Első szerző:Collet, Claude
Cím:Effects of extracellular ATP on freshly isolated mouse skeletal muscle cells during pre-natal and post-natal development / Collet Claude, Strube Caroline, Csernoch Laszlo, Mallouk Nora, Ojeda Carlos, Allard Bruno, Jacquemond Vincent
Dátum:2002
ISSN:0031-6768
Megjegyzések:Extracellular adenosine 5'-triphosphate (ATP) has profound effects on membrane conductance and on the intracellular free [Ca(2+)] ([Ca(2+)](i)) in cultured skeletal muscle cells. The aim of the present study was to examine the occurrence and to characterize the properties of such responses during mammalian muscle development in vivo. The effect of ATP (0.2 mM) was tested on membrane current and [Ca(2+)](i) in freshly isolated pre- and post-natal mouse skeletal muscle cells. Pre-natal cells were from 14- to 19-day-old fetuses. In pre- and early post-natal cells, very small elevations of [Ca(2+)](i) (<50 nM) following ATP application could be detected with the fluorescent indicator fura-2. A clear subsarcolemmal rise in [Ca(2+)] was however associated to the presence of ATP, as demonstrated by increased activity of plasma membrane Ca(2+)-activated K(+) channels in cells bathed in a depolarizing, high-calcium-containing solution. In cells voltage-clamped at -80 mV in external Tyrode, ATP induced an inward current associated with an increased membrane conductance. The mean maximal amplitude of the ATP-induced current was -0.84 +/- 0.07 A/F ( n=39). The response to ATP was still present after birth, although its amplitude tended to decrease with post-natal development and was completely absent in muscle cells from 3- to 6-month-old mice. The ATP-induced current could be abolished reversibly by suramin. Our results suggest that, over the range of developmental stages examined, skeletal muscle cells display an ionotropic purinergic signalling pathway with functional properties qualitatively consistent with what is observed in cultured myotubes.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Pflugers Archiv-European Journal Of Physiology. - 443 : 5-6 (2002), p. 771-778. -
További szerzők:Strube, Caroline Csernoch László (1961-) (élettanász) Mallouk, Nora Ojeda, Carlos Allard, Bruno Jacquemond, Vincent
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2.

001-es BibID:BIBFORM040114
Első szerző:Collet, Claude
Cím:Calcium Signaling in Isolated Skeletal Muscle Fibers Investigated Under "Silicone Voltage-Clamp" Conditions / Collet Claude, Pouvreau Sandrine, Csernoch Laszlo, Allard Bruno, Jacquemond Vincent
Dátum:2004
ISSN:1085-9195
Megjegyzések:In skeletal muscle, release of calcium from the sarcoplasmic reticulum (SR) represents the major source of cytoplasmic Ca2+ elevation. SR calcium release is under the strict command of the membrane potential, which drives the interaction between the voltage sensors in the t-tubule membrane and the calcium-release channels. Either detection or control of the membrane voltage is thus essential when studying intracellular calcium signaling in an intact muscle fiber preparation. The silicone-clamp technique used in combination with intracellular calcium measurements represents an efficient tool for such studies. This article reviews some properties of the plasma membrane and intracellular signals measured with this methodology in mouse skeletal muscle fibers. Focus is given to the potency of this approach to investigate both fundamental aspects of excitation-contraction coupling and potential alterations of intracellular calcium handling in some muscle diseases.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Cell Biochemistry And Biophysics. - 40 : 2 (2004), p. 225-236. -
További szerzők:Pouvreau, Sandrine Csernoch László (1961-) (élettanász) Allard, Bruno Jacquemond, Vincent
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3.

001-es BibID:BIBFORM078604
035-os BibID:(WOS)000469204700012 (Scopus)85064219867
Első szerző:Kutchukian, Candice
Cím:Ca2+-induced sarcoplasmic reticulum Ca2+ release in myotubularin-deficient muscle fibers / Candice Kutchukian, Peter Szentesi, Bruno Allard, Anna Buj-Bello, Laszlo Csernoch, Vincent Jacquemond
Dátum:2019
ISSN:0143-4160
Megjegyzések:Skeletal muscle deficiency in the 3-phosphoinositide (PtdInsP) phosphatase myotubularin (MTM1) causes myotubular myopathy which is associated with severe depression of voltage-activated sarcoplasmic reticulum Ca2+ release through ryanodine receptors. In the present study we aimed at further understanding how Ca2+ release is altered in MTM1-deficient muscle fibers, at rest and during activation. While in wild-type muscle fibers, SR Ca2+ release exhibits fast stereotyped kinetics of activation and decay throughout the voltage range of activation, Ca2+ release in MTM1-deficient muscle fibers exhibits slow and unconventional kinetics at intermediate voltages, suggestive of partial loss of the normal control of ryanodine receptor Ca2+ channel activity. In addition, the diseased muscle fibers at rest exhibit spontaneous elementary Ca2+ release events at a frequency 30 times greater than that of control fibers. Eighty percent of the events have spatiotemporal properties of archetypal Ca2+ sparks while the rest take either the form of lower amplitude, longer duration Ca2+ release events or of a combination thereof. The events occur at preferred locations in the fibers, indicating spatially uneven distribution of the parameters determining spontaneous ryanodine receptor 1 opening. Spatially large Ca2+ release sources were obviously involved in some of these events, suggesting that opening of ryanodine receptors in one cluster can activate opening of ryanodine receptors in a neighboring one. Overall results demonstrate that opening of Ca2+-activated ryanodine receptors is promoted both at rest and during excitation-contraction coupling in MTM1-deficient muscle fibers. Because access to this activation mode is denied to ryanodine receptors in healthy skeletal muscle, this may play an important role in the associated disease situation.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
Skeletal muscle
Ryanodine receptor
Sarcoplasmic reticulum Ca2+ release
Myotubular myopathy
Megjelenés:Cell Calcium. - 80 (2019), p. 91-100. -
További szerzők:Szentesi Péter (1967-) (élettanász) Allard, Bruno Buj-Bello, Anna Csernoch László (1961-) (élettanász) Jacquemond, Vincent
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4.

001-es BibID:BIBFORM071966
Első szerző:Kutchukian, Candice
Cím:Impaired excitation-contraction coupling in muscle fibres from the dynamin2R465W mouse model of centronuclear myopathy / Candice Kutchukian, Peter Szentesi, Bruno Allard, Delphine Trochet, Maud Beuvin, Christine Berthier, Yves Tourneur, Pascale Guicheney, Laszlo Csernoch, Marc Bitoun, Vincent Jacquemond
Dátum:2017
ISSN:0022-3751
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Journal of Physiology-London 595 : 24 (2017), p. 7369-7382. -
További szerzők:Szentesi Péter (1967-) (élettanász) Allard, Bruno Trochet, Delphine Beuvin, Maud Berthier, Christine Tourneur, Yves Guicheney, Pascale Csernoch László (1961-) (élettanász) Bitoun, Marc Jacquemond, Vincent
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5.

001-es BibID:BIBFORM017071
Első szerző:Oláh Tamás (élettanász)
Cím:Overexpression of transient receptor potential canonical type 1 (TRPC1) alters both store operated calcium entry and depolarization-evoked calcium signals in C2C12 cells / Oláh Tamás, Fodor János, Ruzsnavszky Olga, Vincze János, Berbey Celine, Allard Bruno, Csernoch László
Dátum:2011
ISSN:0143-4160
Megjegyzések:When the intracellular calcium stores are depleted, a Ca2+ influx is activated to refill these stores. Thisstore-operated Ca2+ entry (SOCE) depends on the cooperation of several proteins as STIM1, Orai1, and,possibly, TRPC1. To elucidate this role of TRPC1 in skeletal muscle, TRPC1 was overexpressed in C2C12cells and SOCE was studied by measuring the changes in intracellular Ca2+ concentration ([Ca2+]i). TRPC1overexpression significantly increased both the amplitude and the maximal rate-of-rise of SOCE. WhenYM-58483, an inhibitor of TRPC1 was used, these differences were eliminated, moreover, SOCE wasslightly suppressed. A decrease in the expression of STIM1 together with the downregulation of SERCAwas confirmed by Western-blot. As a consequence, a reduction in maximal Ca2+ uptake rate and a higherresting [Ca2+]i following the Ca2+ transients evoked by 120mMKCl were detected. Morphological changesalso accompanied the overexpression of TRPC1. Differentiation of the myoblasts started later, and themyotubes were thinner in TRPC1-overexpressing cultures. For these changes the observed decrease inthe nuclear expression of NFAT1 could be responsible. Our results suggest that enhanced expression ofTRPC1 increases SOCE and has a negative effect on the STIM1-Orai1 system, indicating an interactionbetween these proteins.
Tárgyszavak:Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban
SOCE
TRPC1
STIM1
Calcium transient
Skeletal muscle
Megjelenés:Cell Calcium 49 : 6 (2011), p. 415-425. -
További szerzők:Fodor János (1973-) (élettanász, biotechnológus) Ruzsnavszky Olga (1983-) (élettanász) Vincze János (1988-) (orvos) Berbey, Celine Allard, Bruno Csernoch László (1961-) (élettanász)
Pályázati támogatás:NK 78398
OTKA
K 75604
OTKA
TÁMOP-4.2.2-08/1/2008-0019
TÁMOP
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6.

001-es BibID:BIBFORM017084
Első szerző:Oláh Tamás (élettanász)
Cím:The Alterations of Store-Operated Calcium Entry in TRPC1-Overexpressing C2C12 Myotubes / Tamás Oláh, János Fodor, Olga Ruzsnavszky, Celine Berbey, Bruno Allard, László Csernoch
Dátum:2010
ISSN:0006-3495
Megjegyzések:When the endoplasmic reticulum (ER) calcium store is depleted, a Ca2+ influx is activated from the extracellular milieu to refill the intracellular stores. This well-regulated Ca2+ uptake mechanism, called store-operated Ca2+ entry (SOCE), depends on the cooperation of several proteins as STIM1, Orai1 and TRPC1. The role of STIM1 as the calcium sensor of the ER and Orai1 as the Ca2+ influx channel is well-known from the recent publications, but the function of TRPC1 as a store-operated channel remains elusive.Here TRPC1 was overexpressed by liposome-mediated transfection in C2C12 mouse skeletal muscle cell line. Overexpression was confirmed at mRNA level by RT-PCR and at protein level by immunostaining and Western-blot. The SOCE mechanism was studied by measuring the changes in [Ca2+]i evoked by the re-addition of 1.8 mM [Ca2+]e following the SERCA-inhibition by thapsigargin. As a result of TRPC1 overexpression, the amplitude and the maximum of the derivative of SOCE was significantly increased. When YM-58483, the antagonist of TRPC1 was used, these differences were eliminated, moreover in TRPC1-overexpressing myotubes the SOCE was slightly but not significantly lower, suggesting the downregulation of the STIM1-Orai1 system. This decrease in the expression level of STIM1 was confirmed by Western-blot together with the downregulation of SERCA. As a consequence a reduction in maximal Ca2+ uptake, and a higher resting [Ca2+]i following the transients evoked by 120 mM KCl were detected. Morphological changes caused by the overexpression of TRPC1 were also observed. The differentiation of the myoblasts started later, and the myotubes were thinner in TRPC1-overexpressing cultures.Our results suggest that enhancing the expression level of TRPC1 increases SOCE and has a negative feedback effect on the STIM1-Orai1 system, suggesting a cooperation between these proteins.
Tárgyszavak:Természettudományok Biológiai tudományok idézhető absztrakt
Megjelenés:Biophysical Journal. - 98 : 3 Suppl. 1 (2010), p. 152a-153a. -
További szerzők:Fodor János (1973-) (élettanász, biotechnológus) Ruzsnavszky Olga (1983-) (élettanász) Berbey, Celine Allard, Bruno Csernoch László (1961-) (élettanász)
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7.

001-es BibID:BIBFORM050282
Első szerző:Pouvreau, Sandrine
Cím:Nitric oxide and peptide modulation of excitation-contraction coupling in isolated mammalian skeletal muscle fibres / S. Pouvreau, L. Csernoch, B. Allard, M. Ronjat, V. Jacquemond
Dátum:2006
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:Journal of Muscle Research and Cell Motility. - 27 (2006), p. 513. -
További szerzők:Csernoch László (1961-) (élettanász) Allard, Bruno Ronjat, Michel Jacquemond, Vincent
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8.

001-es BibID:BIBFORM049814
Első szerző:Pouvreau, Sandrine
Cím:Transient loss of voltage control of Ca2+ release in the presence of Maurocalcine in mouse skeletal muscle / S. Pouvreau, L. Csernoch, B. Allard, J. M. Sabatier, M. de Waard, M. Ronjat, V. Jacquemond
Dátum:2006
Tárgyszavak:Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:Biophysical Journal. - 90 (2006), p. 1280a. -
További szerzők:Csernoch László (1961-) (élettanász) Allard, Bruno Sabatier, Jean Marc DeWaard, M. Ronjat, Michel Jacquemond, Vincent
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9.

001-es BibID:BIBFORM020027
Első szerző:Pouvreau, Sandrine
Cím:Transient loss of voltage control of Ca2+ release in the presence of maurocalcine in skeletal muscle / Sandrine Pouvreau, Laszlo Csernoch, Bruno Allard, Jean Marc Sabatier, Michel De Waard, Michel Ronjat, Vincent Jacquemond
Dátum:2006
ISSN:0006-3495
Megjegyzések:In skeletal muscle, sarcoplasmic reticulum (SR) calcium release is controlled by the plasma membrane voltage through interactions between the voltage-sensing dihydropyridine receptor (DHPr) and the ryanodine receptor (RYr) calcium release channel. Maurocalcine (MCa), a scorpion toxin peptide presenting some homology with a segment of a cytoplasmic loop of the DHPr, has been previously shown to strongly affect the activity of the isolated RYr. We injected MCa into mouse skeletal muscle fibers and measured intracellular calcium under voltage-clamp conditions. Voltage-activated calcium transients exhibited similar properties in control and in MCa-injected fibers during the depolarizing pulses, and the voltage dependence of calcium release was similar under the two conditions. However, MCa was responsible for a pronounced sustained phase of Ca2+ elevation that proceeded for seconds following membrane repolarization, with no concurrent alteration of the membrane current. The magnitude of the underlying uncontrolled extra phase of Ca2+ release correlated well with the peak calcium release during the pulse. Results suggest that MCa binds to RYr that open on membrane depolarization and that this interaction specifically alters the process of repolarization-induced closure of the channels.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
Megjelenés:Biophysical Journal. - 91 : 6 (2006), p. 2206-2215. -
További szerzők:Csernoch László (1961-) (élettanász) Allard, Bruno Sabatier, Jean Marc De Waard, Michel Ronjat, Michel Jacquemond, Vincent
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10.

001-es BibID:BIBFORM096379
035-os BibID:(Scopus)85100993394
Első szerző:Sanchez, Colline
Cím:Detection of Ca2+ transients near ryanodine receptors by targeting fluorescent Ca2+ sensors to the triad / Colline Sanchez, Christine Berthier, Yves Tourneur, Laloé Monteiro, Bruno Allard, Laszlo Csernoch, Vincent Jacquemond
Dátum:2021
ISSN:0022-1295 1540-7748
Megjegyzések:In intact muscle fibers, functional properties of ryanodine receptor (RYR)?mediated sarcoplasmic reticulum (SR) Ca2+ release triggered by activation of the voltage sensor CaV1.1 have so far essentially been addressed with diffusible Ca2+-sensitive dyes. Here, we used a domain (T306) of the protein triadin to target the Ca2+-sensitive probe GCaMP6f to the junctional SR membrane, in the immediate vicinity of RYR channels, within the triad region. Fluorescence of untargeted GCaMP6f was distributed throughout the muscle fibers and experienced large Ca2+-dependent changes, with obvious kinetic delays, upon application of voltage-clamp depolarizing pulses. Conversely, T306-GCaMP6f localized to the triad and generated Ca2+-dependent fluorescence transients of lower amplitude and faster kinetics for low and intermediate levels of Ca2+ release than those of untargeted GCaMP6f. By contrast, model simulation of the spatial gradients of Ca2+ following Ca2+ release predicted limited kinetic differences under the assumptions that the two probes were present at the same concentration and suffered from identical kinetic limitations. At the spatial level, T306-GCaMP6f transients within distinct regions of a same fiber yielded a uniform time course, even at low levels of Ca2+ release activation. Similar observations were made using GCaMP6f fused to the ?1 auxiliary subunit of CaV1.1. Despite the probe's limitations, our results point out the remarkable synchronicity of voltage-dependent Ca2+ release activation and termination among individual triads and highlight the potential of the approach to visualize activation or closure of single groups of RYR channels. We anticipate targeting of improved Ca2+ sensors to the triad will provide illuminating insights into physiological normal RYR function and its dysfunction under stress or pathological conditions.
Tárgyszavak:Orvostudományok Elméleti orvostudományok idegen nyelvű folyóiratközlemény külföldi lapban
folyóiratcikk
SKELETAL-MUSCLE FIBERS
CALCIUM-RELEASE
SARCOPLASMIC-RETICULUM
MEMBRANE DEPOLARIZATION
VOLTAGE-DEPENDENCE
MYOPLASMIC CALCIUM
ELEMENTARY EVENTS
MOUSE
CALSEQUESTRIN
EXPRESSION
Megjelenés:Journal of General Physiology. - 153 : 4 (2021), p. e202012592. -
További szerzők:Berthier, Christine Tourneur, Yves Monteiro, Laloé Allard, Bruno Csernoch László (1961-) (élettanász) Jacquemond, Vincent
Pályázati támogatás:GINOP-2.3.2-15-2016-00044
GINOP
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