Hydrogen sulfide (H2S) is a gaseous signaling molecule produced in the body by three enzymes: cystathionine-β-synthase (CBS), cystathionine-γ-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (3-MST). H2S is crucial in various physiological processes associated with female mammalian reproduction. These include estrus cycle, oocyte maturation, oocyte aging, ovulation, embryo transport and early embryo development, the development of the placenta and fetal membranes, pregnancy, and the initiation of labor. Despite the confirmed presence of H2S-producing enzymes in all female reproductive tissues, as described in this review, the exact mechanisms of H2S action in these tissues remain in most cases unclear. Therefore, this review aims to summarize the knowledge about the presence and effects of H2S in these tissues and outline possible signaling pathways that mediate these effects. Understanding these pathways may lead to the development of new therapeutic strategies in the field of women's health and perinatal medicine.

• Klíčová slova
• cystathionine beta synthase, cystathionine gamma lyase, early embryo development, female reproduction, gravidity, hydrogen sulfide, oocyte physiology, uterus,
• Publikační typ
• časopisecké články MeSH
• přehledy MeSH

The role of hydrogen sulfide (H2S) is addressed in Xenopuslaevis 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.

• Klíčová slova
• Xenopus laevis, cell cycle, hydrogen sulfide, meiosis, oocyte,
• MeSH
• apoptóza účinky léků   MeSH
• cyklin B metabolismus   MeSH
• cystathionin-beta-synthasa antagonisté a inhibitory   metabolismus   MeSH
• cystathionin-gama-lyasa antagonisté a inhibitory   metabolismus   MeSH
• cytoplazma metabolismus   MeSH
• faktor podporující zrání metabolismus   MeSH
• fosfatasy cdc25 metabolismus   MeSH
• katalasa metabolismus   MeSH
• meióza účinky léků   MeSH
• metafáze účinky léků   MeSH
• oocyty chemie   enzymologie   metabolismus   MeSH
• profáze meiózy I účinky léků   MeSH
• proteinkinasy metabolismus   MeSH
• proteiny buněčného cyklu metabolismus   MeSH
• proteiny Xenopus metabolismus   MeSH
• reaktivní formy kyslíku metabolismus   MeSH
• signální transdukce účinky léků   MeSH
• sulfan metabolismus   MeSH
• sulfidy metabolismus   farmakologie   MeSH
• sulfurtransferasy antagonisté a inhibitory   metabolismus   MeSH
• superoxiddismutasa metabolismus   MeSH
• viabilita buněk účinky léků   MeSH
• Xenopus laevis MeSH
• zvířata MeSH
• Check Tag
• ženské pohlaví MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• 3-mercaptopyruvate sulphurtransferase MeSH Prohlížeč
• CDC25C protein, human MeSH Prohlížeč
• CDK1 protein, Xenopus MeSH Prohlížeč
• cyklin B MeSH
• cystathionin-beta-synthasa MeSH
• cystathionin-gama-lyasa MeSH
• faktor podporující zrání MeSH
• fosfatasy cdc25 MeSH
• katalasa MeSH
• proteinkinasy MeSH
• proteiny buněčného cyklu MeSH
• proteiny Xenopus MeSH
• reaktivní formy kyslíku MeSH
• sodium bisulfide MeSH Prohlížeč
• sulfan MeSH
• sulfidy MeSH
• sulfurtransferasy MeSH
• superoxiddismutasa MeSH

Porcine oocytes that have matured in in vitro conditions undergo the process of aging during prolonged cultivation, which is manifested by spontaneous parthenogenetic activation, lysis or fragmentation of aged oocytes. This study focused on the role of hydrogen sulfide (H2S) in the process of porcine oocyte aging. H2S is a gaseous signaling molecule and is produced endogenously by the enzymes cystathionine-β-synthase (CBS), cystathionine-γ-lyase (CSE) and 3-mercaptopyruvate sulfurtransferase (MPST). We demonstrated that H2S-producing enzymes are active in porcine oocytes and that a statistically significant decline in endogenous H2S production occurs during the first day of aging. Inhibition of these enzymes accelerates signs of aging in oocytes and significantly increases the ratio of fragmented oocytes. The presence of exogenous H2S from a donor (Na2S.9H2O) significantly suppressed the manifestations of aging, reversed the effects of inhibitors and resulted in the complete suppression of oocyte fragmentation. Cultivation of aging oocytes in the presence of H2S donor positively affected their subsequent embryonic development following parthenogenetic activation. Although no unambiguous effects of exogenous H2S on MPF and MAPK activities were detected and the intracellular mechanism underlying H2S activity remains unclear, our study clearly demonstrates the role of H2S in the regulation of porcine oocyte aging.

• MeSH
• cystathionin-beta-synthasa metabolismus   MeSH
• cystathionin-gama-lyasa metabolismus   MeSH
• embryo savčí účinky léků   MeSH
• inhibitory enzymů farmakologie   MeSH
• kultivace embrya MeSH
• kultivované buňky MeSH
• oocyty účinky léků   fyziologie   MeSH
• partenogeneze účinky léků   MeSH
• prasata MeSH
• stárnutí buněk účinky léků   MeSH
• sulfan metabolismus   farmakologie   MeSH
• sulfurtransferasy metabolismus   MeSH
• zvířata MeSH
• Check Tag
• ženské pohlaví MeSH
• zvířata MeSH
• Publikační typ
• časopisecké články MeSH
• práce podpořená grantem MeSH
• Názvy látek
• 3-mercaptopyruvate sulphurtransferase MeSH Prohlížeč
• cystathionin-beta-synthasa MeSH
• cystathionin-gama-lyasa MeSH
• inhibitory enzymů MeSH
• sulfan MeSH
• sulfurtransferasy MeSH