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• W2554092485 abstract "The aim of this study was to elucidate the normal kinetics of the p90rsk during in vitro maturation of porcine oocytes, to analyse interdependence with the MAPK, and to compare the in vitro obtained results with the findings during in vivo oocytes maturation. The overall success of IVP of embryos remains unsatisfactory low especially in the pig. Insufficient media compositions are thought to be one reason for these facts. To be able to improve the in vitro culture conditions it is necessary to throw light on the molecular basis of oocytes maturation. P90rsk and MAPK are two of the major protein kinases involved in the signal transduction pathway that leads to resumption of meiosis after its first arrest during oocyte maturation. Activation of these two protein kinases results from phosphorylation in which p90rsk is known to be activated by mitogen-activated protein kinase in vitro and probably in vivo via phosphorylation. Cumulus oocyte complexes were collected from slaughtered pigs and matured in vitro (0, 22, 26, 30, 34, 46 h) without and also with an addition of the MEK-specific inhibitor U0126. For in vivo maturation gilts were stimulated with eCG (600-800 IU). Maturation was induced 72 h later with hCG (500 IU). Oocytes were obtained surgically (0, 22, 30 h). The samples were submitted to electrophoresis and protein blotting analysis. Enhanced chemiluminescence was used for visualisation. The in vitro matured oocytes were further submitted to a radioactive kinase assay to determine the specific kinase activity. For the in vitro maturation process it was shown that p90rsk exists in porcine cumulus cells as well as in oocytes and that this kinase becomes phosphorylated during in vitro maturation. With protein blotting analysis of p90rsk, two high-mobility bands were detected prior to GVBD showing that p90rsk is partially phosphorylated already immediately following recovery of the oocytes from the follicles (0 h). The lowest-mobility bands corresponding to full phosphorylation of the molecule were then detected around GVBD and remained present until the end of maturation culture. In addition it was demonstrated that the phosphorylation of p90rsk coincides with the phosphorylation of MAPK. These findings indicated a MAPK dependent phosphorylation of p90rsk. This indication was substantiated by the results of maturation with an addition of the inhibitor U0126 to the maturation medium. Under these conditions GVBD was completely inhibited as well as the phosphorylation of MAPK and p90rsk. The kinase assay kit for activity analysis that was used in this study revealed an activity pattern resembling the activity pattern shown for the p70S6K in Xenopus and mouse oocytes. It was concluded that the kit is not appropriate to analyse specific p90rsk activity. Results with in vivo matured oocytes also show a partial phosphorylation at 0 h with a further phosphorylation of p90rsk after 22 h. As expected the phosphorylation of the in vitro matured oocytes was seen at 90 kDa. Instead phosphorylation of the in vivo matured oocytes occurred little below 200 kDa. This is presumably a molecule complex with MAPK not being a component. Therefore the p90rsk molecule in vivo exists as a dimer. It is concluded that fully grown porcine oocytes possess a partially phosphorylated p90rsk already at the GV stage with a further phosphorylation of the p90rsk molecule occurring between 22-24 h after initiation of cultivation respectively in vivo maturation." @default.
• W2554092485 created "2016-11-30" @default.
• W2554092485 creator A5082320873 @default.
• W2554092485 date "2005-01-01" @default.
• W2554092485 modified "2023-09-24" @default.
• W2554092485 title "Analysis of the protein kinase p90rsk during in vitro and in vivo maturation of porcine oocytes and its dependence on the mitogen-activated protein kinase (MAPK)" @default.
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