Hydrogen Sulfide Impairs Meiosis Resumption ...
Document type :
Article dans une revue scientifique
DOI :
Permalink :
Title :
Hydrogen Sulfide Impairs Meiosis Resumption in Xenopus laevis Oocytes
Author(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]
Journal title :
Cells
Abbreviated title :
Cells
Volume number :
9
Pages :
237
Publisher :
MDPI AG
Publication date :
2020-01-17
ISSN :
2073-4409
English keyword(s) :
meiosis
hydrogen sulfide
Xenopus laevis
oocyte
cell cycle
hydrogen sulfide
Xenopus laevis
oocyte
cell cycle
HAL domain(s) :
Chimie/Chimie théorique et/ou physique
English abstract : [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 ...
Show more >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.Show less >
Show more >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.Show less >
Language :
Anglais
Peer reviewed article :
Oui
Audience :
Internationale
Popular science :
Non
Administrative institution(s) :
Université de Lille
CNRS
CNRS
Research team(s) :
Régulation des signaux de division
Submission date :
2020-11-23T08:59:24Z
2020-11-24T15:24:13Z
2020-11-24T15:24:13Z
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