Activation of protein kinase C after fertilization is required for remodeling the mouse egg into the zygote

Gallicano, G. Ian; McGaughey, Robert W.; Capco, David G.

doi:10.1002/(sici)1098-2795(199704)46:4<587::aid-mrd16>3.0.co;2-t

Cited by 89 publications

(32 citation statements)

References 55 publications

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“…There occurred processes that were typical of this activation (Bement and Capco, 1991;Colonna et al, 1997;Gallicano et al, 1997). According to other authors, however, the PKC activation does not result in the complete spectrum of processes typical of oocyte activation (Moore et al, 1995;Ducibella and Lefevre, 1997).…”

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

confidence: 97%

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: 97%

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

Petr¹,

Eva²,

Tůmová³

et al. 2007

CZECH J ANIM SCI

View full text Add to dashboard Cite

show abstract

“…MPF kinase activity was measured using histone H1 kinase assay (Gallicano et al, 1997). Five oocytes cultured in MB medium were collected, washed in collection buffer (PBS containing 1 mg/ml polyvinyl alcohol, 5 mM EDTA, 10 mM Na 3 VO 4 , and 10 mM NaF), and then transferred to an Eppendorf tube containing 5 l of the collection buffer.…”

Section: Assay Of Mpf and Pka Activitymentioning

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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“…MPF kinase activity was measured using histone H1 kinase assay (Gallicano et al, 1997). Ten embryos were collected and added to 5 ll of collection buffer (PBS containing 1 mg/ml polyvinyl alcohol, 5 mM EDTA, 10 mM Na 3 VO 4 , and 10 mM NaF III-s], and 1 mg/L each of leupeptin, aprotonin, pepstatin, chymostatin, and trypsinchymotrypsin inhibitor) was then added to the disrupted cells after freezing and thawing three times.…”

Section: Assay Of Mpf Activitymentioning

confidence: 99%

Characterization of p70 S6 kinase 1 in early development of mouse embryos

Zhang

et al. 2009

Developmental Dynamics

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The mTOR kinase controls cell growth, proliferation, and survival through two distinct multiprotein complexes mTORC1 and mTORC2. p70 S6 Kinase 1 (S6K1) is characterized as downstream effector of mTOR. Until recently, the connection between S6K1 and mTORC1 /mTORC2 during the early development of mouse embryos has not been well elucidated. Here, the expression level of total S6K1 and its phosphorylation at Thr389 was determined in four phases of one-cell embryos. S6K1 was active throughout the cell cycle especially with higher activity in G2 and M phases. Rapamycin decreased the activity of M-phase promoting factor (MPF) and delayed the first mitotic cleavage. Down-regulating mTOR and raptor reduced S6K1 phosphorylation at Thr389 in one-cell embryos. Furthermore, rapamycin and microinjection of raptor shRNA decreased the immunofluorescent staining of Thr389 phospho-S6K1. It is proposed that mTORC1 may be involved in the control of MPF by regulating S6K1 during the early development of mouse embryos. Developmental Dynamics 238:3025-3034,

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Activation of protein kinase C after fertilization is required for remodeling the mouse egg into the zygote

Cited by 89 publications

References 55 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

Characterization of p70 S6 kinase 1 in early development of mouse embryos

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