. "10"^^ . . "000270806100004" . "Kubelka, Michal" . "\u0160u\u0161or, Andrej" . "AKT (protein kinase B) is implicated in meiotic maturation of porcine oocytes" . "5"^^ . "AKT (protein kinase B) is implicated in meiotic maturation of porcine oocytes"@en . "302268" . "RIV/67985904:_____/09:00329884!RIV10-AV0-67985904" . "5"^^ . . "AKT (protein kinase B) is implicated in meiotic maturation of porcine oocytes"@en . "1470-1626" . "-" . . . "Motl\u00EDk, Jan" . . . "GB - Spojen\u00E9 kr\u00E1lovstv\u00ED Velk\u00E9 Brit\u00E1nie a Severn\u00EDho Irska" . "[665DBA6DB207]" . . . . "Reproduction" . . "138" . "protein kinase; porcine oocyte; oocyte maturation"@en . . . "P(GA204/06/1297), P(GA523/03/0857), P(GA524/07/1087), Z(AV0Z50450515)" . "The aim of this study was to investigate the involvement of the serine/threonine protein kinase AKT (also called protein kinase B) in the control of meiosis of porcine denuded oocytes (DOs) matured in vitro. Western blot analysis revealed that the two principal AKT phosphorylation sites, Ser473 and Thr308, are phosphorylated at different stages of meiosis. In freshly isolated germinal vesicle (GV)-stage DOs, Ser473 was already phosphorylated. After the onset of oocyte maturation, the intensity of the Ser473 phosphorylation increased, however, which declined sharply when DOs underwent GV breakdown (GVBD) and remained at low levels in metaphase I- and II-stage (MI- and MII-stage). In contrast, phosphorylation of Thr308 was increased by the time of GVBD and reached maximum at MI-stage. A peak of AKT activity was noticed around GVBD and activity of AKT declined at MI-stage. To assess the role of AKT during meiosis, porcine DOs were cultured in 50 mikroM SH-6, a specific" . . . . . . . . . "\u0160olc, Petr" . "AKT (protein kinase B) is implicated in meiotic maturation of porcine oocytes" . "The aim of this study was to investigate the involvement of the serine/threonine protein kinase AKT (also called protein kinase B) in the control of meiosis of porcine denuded oocytes (DOs) matured in vitro. Western blot analysis revealed that the two principal AKT phosphorylation sites, Ser473 and Thr308, are phosphorylated at different stages of meiosis. In freshly isolated germinal vesicle (GV)-stage DOs, Ser473 was already phosphorylated. After the onset of oocyte maturation, the intensity of the Ser473 phosphorylation increased, however, which declined sharply when DOs underwent GV breakdown (GVBD) and remained at low levels in metaphase I- and II-stage (MI- and MII-stage). In contrast, phosphorylation of Thr308 was increased by the time of GVBD and reached maximum at MI-stage. A peak of AKT activity was noticed around GVBD and activity of AKT declined at MI-stage. To assess the role of AKT during meiosis, porcine DOs were cultured in 50 mikroM SH-6, a specific"@en . "Kalous, Jaroslav" . "RIV/67985904:_____/09:00329884" . . .