Involvement of a calcium‐phospholipid‐dependent protein kinase in the maturation of <i>Xenopus laevis</i> oocytes

Laurent, Anne; Basset, M.; Dorée, Marcel; Peuch, Christian J. Le

doi:10.1016/0014-5793(88)81448-0

Cited by 19 publications

(12 citation statements)

References 22 publications

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“…Treatment of Xenopus oocytes with PMA has been reported to induce meiotic maturation in the absence of progesterone (Stith & Mailer, 1987;Laurent et al, 1988). In fact, in several aspects the PMA-induced changes in the properties of the oocyte plasma membrane observed here resemble those occurring during progesterone-induced maturation.…”

Section: Correlations To Meiotic Maturationmentioning

confidence: 52%

“…Activation of protein kinase C has been reported to be involved in stimulation of meiotic maturation (Laurent et al, 1988 and Methods). Under control conditions, the average capacitance is 179 -+ 5 nF.…”

Section: Capacitancementioning

confidence: 98%

“…For the Na+/K+-ATPase in somatic cells, it has been suggested that activation of protein kinase C by phorbol esters can modulate the rate of Na+/ K + pumping (Lynch et al, 1986;Hootman, Brown & Williams, 1987;Bertorello & Aperia, 1989). Phorbol esters have been demonstrated to activate protein kinase C also in Xenopus oocytes (Laurent et al, 1988), to modulate membrane currents (Dascal et al, 1985;Lupu-Meiri, Shapira & Oron, 1989), and to induce resumption of oogenesis (Bement & Capco, 1989).…”

Section: Introductionmentioning

confidence: 96%

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Activation of protein kinase C by phorbol ester induces downregulation of the Na+/K+-ATPase in oocytes ofXenopus laevis

et al. 1990

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Full-grown prophase-arrested oocytes of Xenopus laevis were treated with 50 nM phorbol 12-myristate 13-acetate (PMA), an activator of protein kinase C, or with 50 nM 4 alpha-phorbol 12,13-didecanoate (4 alpha PDD) that does not activate protein kinase C. The effect on membrane currents and capacitance, inulin uptake and ouabain binding, and on membrane morphology were analyzed. (i) During application of PMA, current generated by the Na+/K+ pump decreases; in addition, Cl- and K+ channels become inhibited. This general decrease in membrane conductance reaches steady state after about 60 min. 4 alpha PDD was ineffective. (ii) Ouabain binding experiments demonstrate that PMA (K1/2 = 7 nM), but not 4 alpha PPD, induces a reduction of the number of pump molecules in the surface membrane. Permeabilization of oocytes by digitonin plus 0.02% SDS renders all binding sites present prior to PMA treatment again accessible for ouabain. The KD value for ouabain binding is not influenced. 4 alpha PDD was ineffective. (iii) Exposure of oocytes to PMA reduces membrane capacitance and stimulates uptake of inulin suggesting an increase in endocytosis. Electron micrographs show that PMA reduces the number and length of microvilli, leading finally to a smooth membrane surface with a reduced surface area. From these results we conclude that stimulation of protein kinase C leads to downregulation of the sodium pump. A major portion of this inhibition is brought about by reduction in area of surface membrane with a concomitant internalization of pump molecules. In addition to this mode of downregulation, a direct effect of stimulation of protein kinase C on the pump molecule cannot be excluded.

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Section: Correlations To Meiotic Maturationmentioning

confidence: 52%

Section: Capacitancementioning

confidence: 98%

Section: Introductionmentioning

confidence: 96%

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Activation of protein kinase C by phorbol ester induces downregulation of the Na+/K+-ATPase in oocytes ofXenopus laevis

et al. 1990

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“…We therefore examined the role of PKC during cavitation. Protein kinase C can be activated by phorbol esters or synthetic diacylglycerols [32][33][34][35][36][37]. To establish that the phorbol ester PMA and the synthetic diacylglycerol OAG up-regulate PKC, we monitored the ability of these agents to induce compaction of early 8-cell embryos [37,38].…”

Section: Resultsmentioning

confidence: 99%

Regulation of Blastocoele Formation by Intracellular Calcium Release is Mediated through a Phospholipase C-Dependent Pathway in Mice1

Stachecki¹,

Armant²

1996

Biology of Reproduction

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Calcium signaling plays a critical role in the regulation of mouse preimplantation development, in part through the activation of calmodulin. Calcium transients in mouse morulae appear to be generated predominantly through the production of inositol 1,4,5-trisphosphate (IP3) by phospholipase C (PLC). IP3 receptors predominate in mouse embryos as regulators of calcium release. Exposure to the PLC inhibitors ET-18-OCH3 or U73122 resulted in a dose-dependent, reversible inhibition of cavitation, while the inactive analogue U73343 did not alter the rate of cavitation, as compared to that in controls. U73122 inhibited the release of calcium from intracellular stores after exposure to ethanol or lysophosphatidic acid, suggesting that PLC is required for blastocoele formation in the mouse and that calcium signaling may be PLC-dependent. In addition to IP3, PLC activation generates diacylglycerol, which stimulates protein kinase C (PKC) and could also alter the rate of embryonic development. However, activation of PKC with phorbol ester or synthetic diacylglycerol was not sufficient to accelerate development, although embryo culture in medium containing PKC inhibitors did delay cavitation. Exposure to a PKC inhibitor during ethanol-induced calcium signaling did not attenuate the ensuing acceleration of cavitation. These results demonstrate that a PLC-mediated signaling pathway is required for blastocoele formation and that the generation of IP3, but not diacylglycerol, is critical for accelerating preimplantation development.

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“…Weak support for a link between DAG levels and PKC activity was found by Laurent et al (1988), who reported that PKC activity is low in eggs obtained an unknown number of hours after white spot appearance (although MPF activity was higher in eggs). This agrees with the decline in DAG levels after 0.85 GVBD,,.…”

Section: Comparison Of the Action Of Three Hormonesmentioning

confidence: 90%

Insulin‐like growth factor 1, insulin, and progesterone induce early and late increases in Xenopus oocyte sn‐1, 2‐diacylglycerol levels before meiotic cell division

Stith¹,

Kirkwood²,

Wohnlich³

1991

Journal Cellular Physiology

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After a 3 to 6 hour incubation, addition of progesterone (the most effective), insulin-like growth factor 1 (IGF-1; the second most effective), or insulin induces meiotic cell division in Xenopus oocytes. Measurement of an endogenous activator of protein kinase C, sn-1,2-diacylglycerol (DAG), by an enzymatic method recording mass demonstrates that all three hormones alter DAG levels. Five seconds after addition, only progesterone transiently reduces DAG levels by about 25%. At 15 minutes after addition, all three hormones produce a peak of DAG (115% to 160% of control values), with the more effective hormones producing a larger increase in DAG. Insulin produces the smallest DAG increase, but the DAG release is longer lasting. Finally, all three hormones induce a second peak in DAG levels just before white spot appearance (at 0.85 GVBD50, where 1.0 GVBD50 is when 50% of the cells have divided). With these data and since an activator of protein kinase C, a phorbol ester, has been found to induce meiosis, the kinase may play a role in early proliferative events at the plasma membrane and in late events at the nucleus.

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Involvement of a calcium‐phospholipid‐dependent protein kinase in the maturation of Xenopus laevis oocytes

Cited by 19 publications

References 22 publications

Activation of protein kinase C by phorbol ester induces downregulation of the Na+/K+-ATPase in oocytes ofXenopus laevis

Activation of protein kinase C by phorbol ester induces downregulation of the Na+/K+-ATPase in oocytes ofXenopus laevis

Regulation of Blastocoele Formation by Intracellular Calcium Release is Mediated through a Phospholipase C-Dependent Pathway in Mice1

Insulin‐like growth factor 1, insulin, and progesterone induce early and late increases in Xenopus oocyte sn‐1, 2‐diacylglycerol levels before meiotic cell division

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