Effects of stimulators of protein kinases A and C and modulators of phosphorylation on plasminogen activator activity in porcine oocyte‐cumulus cell complexes during in vitro maturation

Kim, Nam Hyung; Menino, Alfred R.

doi:10.1002/mrd.1080400313

Cited by 29 publications

(23 citation statements)

References 44 publications

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“…In porcine oocytes, PKC was observed to participate in the regulation of the resumption of meiotic maturation (Jung et al, 1992;Coskun and Lin, 1995;Kim and Menino, 1995;Su et al, 1999;Shimada et al, 2001). Fan et al (2002b) demonstrated a change in the localization of PKC -α, -β I , -γ in maturing porcine oocytes and after their activation.…”

Section: Which Signalling Cascades Remained Silent In No-induced Oocymentioning

confidence: 99%

The role of nitric oxide in parthenogenetic activation of pig oocytes: A review

Petr¹,

Eva²,

Tůmová³

et al. 2007

CZECH J ANIM SCI

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Parthenogenetic activation of mammalian oocytes with artificial stimuli is commonly applied in various reproductive biotechniques, e.g. cloning using nuclear transfer. For this reason, many studies focus on oocyte activation in vitro. Recently we have described the activation of pig oocytes using nitric oxide. This activating stimulus is very specific in many aspects. However, it does not provide an adequate stimulus for parthenogenetic development. It was shown that nitric oxide stimulated some signalling pathways which are inactive in conventional treatments for parthenogenetic activation, e.g. the cGMP-dependent signalling cascade. On the other hand, nitric oxide does not stimulate certain signalling pathways involved in oocyte activation after calcium ionophore, e.g. the PKC signalling cascade. The aim of this review is to characterize the complex processes induced in oocytes after treatment with nitric oxide. Perspectives for further research and the application of nitric oxide for parthenogenetic activation of oocytes are outlined.

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Section: Which Signalling Cascades Remained Silent In No-induced Oocymentioning

confidence: 99%

The role of nitric oxide in parthenogenetic activation of pig oocytes: A review

Petr¹,

Eva²,

Tůmová³

et al. 2007

CZECH J ANIM SCI

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“…Studies in starfish, Xenopus, and mammalian oocytes have reached an identical conclusion that maintenance of a high level of cAMP and active PKA play a critical role in mei-otic arrest (Maller and Krebs, 1977;Speaker and Butcher, 1977;Sadler and Maller, 1981;Eppig and Downs, 1984;Bornslaeger et al, 1986;Eppig, 1989;Smith, 1989;Tornell and Hillensjo, 1993;Kim and Menino, 1995;Rose-Hellekant and Bavister, 1996). Pharmacological manipulations to increase cAMP levels or injection of PKA in mammalian oocytes isolated from their follicles invariably produce a blockade of meiotic resumption, and phosphodiesterase inhibitors, such as the xanthine IBMX, also block spontaneous mammalian oocyte maturation (Conti et al, 1998).…”

Section: Introductionmentioning

confidence: 99%

Protein kinase a modulates Cdc25B activity during meiotic resumption of mouse oocytes

Zhang

et al. 2008

Developmental Dynamics

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Protein kinase A (PKA) play a critical role in maintaining the meiotic arrest. However, the steps downstream of PKA remain largely unknown. In this study, we investigated the regulation of meiotic resumption by PKA/Cdc25B pathway in mouse oocytes. Injection of mRNA coding for Cdc25b-S321A had a more potent maturation-inducing ability than Cdc25b-WT. When co-injected with PKA inhibitor, Cdc25B-WT had similar activities with Cdc25B-S321A. Meanwhile, the phosphorylation of Cdc25B-S321 was detected in germinal vesicle (GV) oocytes by Western blotting with a phospho-Ser321-specific antibody and the band disappeared when oocytes reenter into the meiotic cell cycle. Furthermore, Cdc25B-WT translocated to the nucleus shortly before GV breakdown (GVBD), whereas phosphorylated Cdc25B-S321 expressed exclusively in the cytoplasm and the signal could not be detected in GVBD oocytes. Taken together, these data indicate that Cdc25B-Serine321 is the potential PKA target and Cdc25B subcellular localization determines its function during the process of maintaining GV arrest in mouse oocytes. Developmental Dynamics 237: 3777-3786, 2008.

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“…Degradation of cAMP by a phosphodiesterase type IIIA (PDE3A) leads to a decrease of PKA activity and initiates resumption of meiosis in rodent oocytes (Conti 2002, Kovo et al 2006. Similarly, in porcine oocytes, resumption of meiosis is also associated with a decrease in cAMP concentration and subsequent inactivation of PKA (Kim & Menino 1995).…”

Section: Introductionmentioning

confidence: 99%

AKT (protein kinase B) is implicated in meiotic maturation of porcine oocytes

Kalous¹,

Kubelka²,

Solc³

et al. 2009

Reproduction

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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 mM SH-6, a specific inhibitor of AKT. In SH-6-treated DOs, GVBD was not inhibited; on the contrary, a significant acceleration of meiosis resumption was observed. The dynamics of the Ser473 phosphorylation was not affected; however, phosphorylation of Thr308 was reduced, AKT activity was diminished at the time of GVBD, and meiotic progression was arrested in early MI-stage. Moreover, the activity of the cyclin-dependent kinase 1 (CDK1) and MAP kinase declined when SH-6-treated DOs underwent GVBD, indicating that AKT activity is involved in the regulation of CDK1 and MAP kinase. These results suggest that activity of AKT is not essential for induction of GVBD in porcine oocytes but plays a substantial role during progression of meiosis to MI/MII-stage. Reproduction (2009) 138 645-654

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Effects of stimulators of protein kinases A and C and modulators of phosphorylation on plasminogen activator activity in porcine oocyte‐cumulus cell complexes during in vitro maturation

Cited by 29 publications

References 44 publications

The role of nitric oxide in parthenogenetic activation of pig oocytes: A review

The role of nitric oxide in parthenogenetic activation of pig oocytes: A review

Protein kinase a modulates Cdc25B activity during meiotic resumption of mouse oocytes

AKT (protein kinase B) is implicated in meiotic maturation of porcine oocytes

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