Protein kinase Cδ (PKCδ) involved in the regulation of pAkt1 (Ser473) on the release of mouse oocytes from diplotene arrest
Abstract
Defects in meiotic maturation may lead to chromosome segregation errors and genomic instability. Previous reports indicated that protein kinase C delta (PKCδ) may interact with microtubule organizing center-associated protein to play a role on meiotic spindle organization of mammalian oocytes. In this study, we explored the potential role of protein kinase B alpha (PKBα/Akt1), PKCδ, and their relationship on meiotic maturation of mouse oocytes. We examined the expression and localization of pAkt1 (Ser473) and/or pPKCδ (Thr505) under the treatment of SH-6 or Sotrastaurin. With the increasing of SH-6 concentrations, we observed that the protein levels of pAkt1 (Ser473) and the percentages of GVBD were decreased gradually. And the distribution of pAkt1 (Ser473), Cdc25B, pCdc2 (Tyr15), and α-tubulin around nucleus was also highly disordered under the treatment of 10-μM SH-6, a special inhibitor of pAkt1 (Ser473). In addition, the levels of pAkt1 (Ser473) were decreased with the treatment of Sotrastaurin, an inhibitor of PKCδ, suggesting that Akt1 may be one of the downstream targets of PKCδ. So, we deduced that PKCδ may be involved in regulating the release from diplotene arrest of mouse oocytes by controlling the levels of pAkt1 S...Continue Reading
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AKT Pathway
This feed focuses on the AKT serine/threonine kinase, which is an important signaling pathway involved in processes such as glucose metabolism and cell survival.