Találati lista | Tudóstér

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
Internet cím:	DOI elektronikus változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM018361
Első szerző:	Oláh Tamás (élettanász)
Cím:	Trisk 32 regulates IP3 receptors in rat skeletal myoblasts / Oláh Tamás, Fodor János, Oddoux Sarah, Ruzsnavszky Olga, Marty Isabelle, Csernoch László
Dátum:	2011
ISSN:	0031-6768
Megjegyzések:	To date, four isoforms of triadins have been identified in rat skeletal muscle. While the function of the 95-kDa isoform in excitation-contraction coupling has been studied in detail, the role of the 32-kDa isoform (Trisk 32) remains elusive. Here, Trisk 32 overexpression was carried out by stable transfection in L6.G8 myoblasts. Co-localization of Trisk 32 and IP(3) receptors (IP(3)R) was demonstrated by immunocytochemistry, and their association was shown by co-immunoprecipitation. Functional effects of Trisk 32 on IP(3)-mediated Ca(2+) release were assessed by measuring changes in [Ca(2+)](i) following the stimulation by bradykinin or vasopressin. The amplitude of the Ca(2+) transients evoked by 20 mikroM bradykinin was significantly higher in Trisk 32-overexpressing (p<0.01; 426 ±84 nM, n=27) as compared to control cells (76±12 nM, n=23). The difference remained significant (p<0.02; 217±41 nM, n=21, and 97±29 nM, n=31, respectively) in the absence of extracellular Ca(2+). Similar observations were made when 0.1 mikroM vasopressin was used to initiate Ca(2+) release. Possible involvement of the ryanodine receptors (RyR) in these processes was excluded, after functional and biochemical experiments. Furthermore, Trisk 32 overexpression had no effect on store-operated Ca(2+) entry, despite a decrease in the expression of STIM1. These results suggest that neither the increased activity of RyR, nor the amplification of SOCE, is responsible for the differences observed in bradykinin- or vasopressin-evoked Ca(2+) transients; rather, they were due to the enhanced activity of IP(3)R. Thus, Trisk 32 not only co-localizes with, but directly contributes to, the regulation of Ca(2+) release via IP(3)R.
Tárgyszavak:	Természettudományok Biológiai tudományok idegen nyelvű folyóiratközlemény külföldi lapban Inositol 1,4,5-trisphosphate Skeletal muscle Myoblasts Calcium transient Endoplasmic reticulum
Megjelenés:	Pflügers Archiv. - 462 : 4 (2011), p. 599-610. -
További szerzők:	Fodor János (1973-) (élettanász, biotechnológus) Oddoux, Sarah Ruzsnavszky Olga (1983-) (élettanász) Marty, Isabelle Csernoch László (1961-) (élettanász)
Internet cím:	Szerző által megadott URL DOI Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon:

001-es BibID:	BIBFORM050230
Első szerző:	Szentesi Péter (élettanász)
Cím:	The role of triadin isoforms in skeletal muscle Ca2+ homeostasis / Szentesi P., Fodor J., Oddoux S., Sztretye M., Dienes B., Olah T., Marty I., Csernoch L.
Dátum:	2010
ISSN:	0231-424X 1588-2683
Tárgyszavak:	Orvostudományok Elméleti orvostudományok idézhető absztrakt
Megjelenés:	Acta Physiologica Hungarica. - 97 (2010), p. 139. -
További szerzők:	Fodor János (1973-) (élettanász, biotechnológus) Oddoux, Sarah Sztretye Mónika (1981-) (élettanász, elektrofiziológus) Dienes Beatrix (1972-) (élettanász, molekuláris biológus) Oláh Tamás (1983-) (élettanász) Marty, Isabelle Csernoch László (1961-) (élettanász)
Internet cím:	Intézményi repozitóriumban (DEA) tárolt változat
Borító:
Saját polcon: