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
• Cystathionine beta-Synthase metabolism   MeSH
• Cystathionine gamma-Lyase metabolism   MeSH
• Embryo, Mammalian drug effects   MeSH
• Enzyme Inhibitors pharmacology   MeSH
• Embryo Culture Techniques MeSH
• Cells, Cultured MeSH
• Oocytes drug effects   physiology   MeSH
• Parthenogenesis drug effects   MeSH
• Swine MeSH
• Cellular Senescence drug effects   MeSH
• Hydrogen Sulfide metabolism   pharmacology   MeSH
• Sulfurtransferases metabolism   MeSH
• Animals MeSH
• Check Tag
• Female MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Names of Substances
• 3-mercaptopyruvate sulphurtransferase MeSH Browser
• Cystathionine beta-Synthase MeSH
• Cystathionine gamma-Lyase MeSH
• Enzyme Inhibitors MeSH
• Hydrogen Sulfide MeSH
• Sulfurtransferases MeSH