Hydrogen Sulfide Impairs Meiosis Resumption ...
Type de document :
Article dans une revue scientifique
DOI :
URL permanente :
Titre :
Hydrogen Sulfide Impairs Meiosis Resumption in Xenopus laevis Oocytes
Auteur(s) :
Gelaude, Armance [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Slaby, Sylvain [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Cailliau, Katia [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Marin, Matthieu [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Lescuyer, Arlette [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Molinaro, Caroline [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Nevoral, Jan [Auteur]
Czech University of Life Sciences Prague [CZU]
Kučerová-Chrpová, Veronica [Auteur]
Czech University of Life Sciences Prague [CZU]
Sedmikova, Marketa [Auteur]
Czech University of Life Sciences Prague [CZU]
Petr, Jaroslav [Auteur]
Martoriati, Alain [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Bodart, Jean-Francois [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Slaby, Sylvain [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Cailliau, Katia [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Marin, Matthieu [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Lescuyer, Arlette [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Molinaro, Caroline [Auteur]
Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Nevoral, Jan [Auteur]
Czech University of Life Sciences Prague [CZU]
Kučerová-Chrpová, Veronica [Auteur]
Czech University of Life Sciences Prague [CZU]
Sedmikova, Marketa [Auteur]
Czech University of Life Sciences Prague [CZU]
Petr, Jaroslav [Auteur]
Martoriati, Alain [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Bodart, Jean-Francois [Auteur]

Unité de Glycobiologie Structurale et Fonctionnelle - UMR 8576 [UGSF]
Titre de la revue :
Cells
Nom court de la revue :
Cells
Numéro :
9
Pagination :
237
Éditeur :
MDPI AG
Date de publication :
2020-01-17
ISSN :
2073-4409
Mot(s)-clé(s) en anglais :
meiosis
hydrogen sulfide
Xenopus laevis
oocyte
cell cycle
hydrogen sulfide
Xenopus laevis
oocyte
cell cycle
Discipline(s) HAL :
Chimie/Chimie théorique et/ou physique
Résumé en anglais : [en]
The role of hydrogen sulfide (H2S) is addressed in Xenopus laevis oocytes. Three enzymes involved in H2S metabolism, cystathionine β-synthase, cystathionine γ-lyase, and 3-mercaptopyruvate sulfurtransferase, were detected ...
Lire la suite >The role of hydrogen sulfide (H2S) is addressed in Xenopus laevis oocytes. Three enzymes involved in H2S metabolism, cystathionine β-synthase, cystathionine γ-lyase, and 3-mercaptopyruvate sulfurtransferase, were detected in prophase I and metaphase II-arrested oocytes and drove an acceleration of oocyte meiosis resumption when inhibited. Moreover, meiosis resumption is associated with a significant decrease in endogenous H2S. On another hand, a dose-dependent inhibition was obtained using the H2S donor, NaHS (1 and 5 mM). NaHS impaired translation. NaHS did not induce the dissociation of the components of the M-phase promoting factor (MPF), cyclin B and Cdk1, nor directly impacted the MPF activity. However, the M-phase entry induced by microinjection of metaphase II MPF-containing cytoplasm was diminished, suggesting upstream components of the MPF auto-amplification loop were sensitive to H2S. Superoxide dismutase and catalase hindered the effects of NaHS, and this sensitivity was partially dependent on the production of reactive oxygen species (ROS). In contrast to other species, no apoptosis was promoted. These results suggest a contribution of H2S signaling in the timing of amphibian oocytes meiosis resumption.Lire moins >
Lire la suite >The role of hydrogen sulfide (H2S) is addressed in Xenopus laevis oocytes. Three enzymes involved in H2S metabolism, cystathionine β-synthase, cystathionine γ-lyase, and 3-mercaptopyruvate sulfurtransferase, were detected in prophase I and metaphase II-arrested oocytes and drove an acceleration of oocyte meiosis resumption when inhibited. Moreover, meiosis resumption is associated with a significant decrease in endogenous H2S. On another hand, a dose-dependent inhibition was obtained using the H2S donor, NaHS (1 and 5 mM). NaHS impaired translation. NaHS did not induce the dissociation of the components of the M-phase promoting factor (MPF), cyclin B and Cdk1, nor directly impacted the MPF activity. However, the M-phase entry induced by microinjection of metaphase II MPF-containing cytoplasm was diminished, suggesting upstream components of the MPF auto-amplification loop were sensitive to H2S. Superoxide dismutase and catalase hindered the effects of NaHS, and this sensitivity was partially dependent on the production of reactive oxygen species (ROS). In contrast to other species, no apoptosis was promoted. These results suggest a contribution of H2S signaling in the timing of amphibian oocytes meiosis resumption.Lire moins >
Langue :
Anglais
Comité de lecture :
Oui
Audience :
Internationale
Vulgarisation :
Non
Établissement(s) :
Université de Lille
CNRS
CNRS
Équipe(s) de recherche :
Régulation des signaux de division
Date de dépôt :
2020-11-23T08:59:24Z
2020-11-24T15:24:13Z
2020-11-24T15:24:13Z
Fichiers
- cells-09-00237.pdf
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