A serine/threonine-specific protein kinase B (PKB), also known as Akt, is a key factor in the phosphoinositide 3-kinase (PI3K)/Akt signaling pathway that regulates cell survival, metabolism and proliferation. Akt phosphorylates many downstream specific substrates, which subsequently control the nuclear envelope breakdown (NEBD), centrosome maturation, spindle assembly, chromosome segregation, and cytokinesis. In vertebrates, Akt is also an important player during oogenesis and preimplantation development. In the signaling pathways regulating mRNA translation, Akt is involved in the control of mammalian target of rapamycin complex 1 (mTORC1) and thereby regulates the activity of a translational repressor, the eukaryotic initiation factor 4E (eIF4E) binding protein 1 (4E-BP1). In this review, we summarize the functions of Akt in mitosis, meiosis and early embryonic development. Additionally, the role of Akt in the regulation of mRNA translation is addressed with respect to the significance of this process during early development.

• Keywords
• Akt kinase, early embryo, mRNA translation, mTORC1, meiosis, mitosis, oocyte, spindle,
• MeSH
• Phosphatidylinositol 3-Kinase metabolism   MeSH
• Embryonic Development MeSH
• Phosphatidylinositol 3-Kinases * metabolism   MeSH
• Phosphoproteins metabolism   MeSH
• Phosphorylation genetics   MeSH
• Oocytes metabolism   MeSH
• Oogenesis MeSH
• Protein Serine-Threonine Kinases metabolism   MeSH
• Proto-Oncogene Proteins c-akt * metabolism   MeSH
• Mammals metabolism   MeSH
• Signal Transduction MeSH
• Animals MeSH
• Check Tag
• Animals MeSH
• Publication type
• Journal Article MeSH
• Research Support, Non-U.S. Gov't MeSH
• Review MeSH
• Names of Substances
• Phosphatidylinositol 3-Kinase MeSH
• Phosphatidylinositol 3-Kinases * MeSH
• Phosphoproteins MeSH
• Protein Serine-Threonine Kinases MeSH
• Proto-Oncogene Proteins c-akt * MeSH

The developmental potential of porcine oocytes cultured in vitro was remarkably enhanced in a medium containing FGF2, LIF and IGF1 (FLI) when compared to a medium supplemented with gonadotropins and EGF (control). We analyzed the molecular background of the enhanced oocyte quality by comparing the time course of MAPK3/1 and AKT activation, and the expression of genes controlled by these kinases in cumulus-oocyte complexes (COCs) cultured in FLI and the control medium. The pattern of MAPK3/1 activation in COCs was very similar in both media, except for a robust increase in MAPK3/1 phosphorylation during the first hour of culture in the FLI medium. The COCs cultured in the FLI medium exhibited significantly higher activity of AKT than in the control medium from the beginning up to 16 h of culture; afterwards a deregulation of AKT activity occurred in the FLI medium, which was not observed in the control medium. The expression of cumulus cell genes controlled by both kinases was also modulated in the FLI medium, and in particular the genes related to cumulus-expansion, signaling, apoptosis, antioxidants, cell-to-cell communication, proliferation, and translation were significantly overexpressed. Collectively, these data indicate that both MAPK3/1 and AKT are implicated in the enhanced quality of oocytes cultured in FLI medium.

• Keywords
• AKT kinase, FGF2, IGF1, LIF, MAP kinase 3/1, gene expression, oocyte competence, oocyte maturation,
• MeSH
• In Vitro Oocyte Maturation Techniques methods   veterinary   MeSH
• Culture Media chemistry   pharmacology   MeSH
• Cells, Cultured MeSH
• Meiosis drug effects   physiology   MeSH
• Mitogen-Activated Protein Kinase 1 physiology   MeSH
• Mitogen-Activated Protein Kinase 3 physiology   MeSH
• Oocytes cytology   drug effects   physiology   MeSH
• Oogenesis drug effects   physiology   MeSH
• Swine MeSH
• Proto-Oncogene Proteins c-akt physiology   MeSH
• Signal Transduction drug effects   physiology   MeSH
• Animals MeSH
• Check Tag
• Female MeSH
• Animals MeSH
• Publication type
• Journal Article MeSH
• Names of Substances
• Culture Media MeSH
• Mitogen-Activated Protein Kinase 1 MeSH
• Mitogen-Activated Protein Kinase 3 MeSH
• Proto-Oncogene Proteins c-akt MeSH