Steroid-induced meiotic division in Xenopus laevis oocytes: surface and calcium

Baulieu, Étienne-Émile; Godeau, François; Schorderet, Michel; Schorderet‐Slatkine, Sabine

doi:10.1038/275593a0

Cited by 268 publications

(109 citation statements)

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“…Data on non-transcriptional effects of steroid hormones on cell metabolism are rare and are mainly restricted to the maturation of the amphibian oocyte (e.g. Baulieu et al, 1978;Godau et al, 1978;Blondau and Baulieu, 1984) and effects in the neurosystem (for review, see Schumacher, 1990).…”

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confidence: 99%

Developmentally Controlled Cleavage of the Calliphora Arylphorin Receptor and Posttranslational Action of the Steroid Hormone 20‐Hydroxyecysone

Burmester

Scheller

1997

European Journal of Biochemistry

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In response to a rise in ecdysteroid titre, fat body cells of insect larvae take up storage proteins from the haemolymph by receptor-mediated endocytosis. Here we show that the receptor responsible for incorporation of the major haemolymph protein arylphorin of the blowfly, Calliphora vicina, is subject to an unusual posttranslational processing that involves three distinct cleavage steps. After the removal of a 17-amino-acid signal peptide, a receptor precursor of 141 kDa is released. Before reaching the cell surface, the precursor is cleaved a second time, giving rise to the active 92-kDa arylphorin receptor, plus a 48-kDa peptide. The function of this 48-kDa peptide may be the prevention of premature ligandreceptor interaction in the endoplasmic reticulum. 20-Hydroxyecdysone initiates a third cleavage step of the arylphorin receptor, which results in a 62-kDa arylphorin binding protein and a 30-kDa peptide. Contrary to the standard model of steroid hormone action, the process which give rise to receptor cleavage can be induced by 20-hydroxyecdysone in vivo and in vitro even in absence of protein biosynthesis.

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confidence: 99%

Developmentally Controlled Cleavage of the Calliphora Arylphorin Receptor and Posttranslational Action of the Steroid Hormone 20‐Hydroxyecysone

Burmester

Scheller

1997

European Journal of Biochemistry

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“…These were determined as before (10) Reversal of Cholera Toxin-Induced Accumulation of cAMP by Progesterone in the Presence of Phosphodiesterase Inhibitors. Papaverine (0.1 mM), 3-isobutyl-1-methyl-xanthine (IBMX; 1 mM), and theophylline (10 mM) led to 2-to 3-fold increases in the cholera toxin-induced accumulation ofcAMP after 15 (1,(15)(16)(17) provided evidence that these were also able to decrease the level ofcAMP in oocytes (Fig. 3).…”

Section: Methodsmentioning

confidence: 99%

“…A large body ofdata suggests the involvement ofmembrane sites for progesterone and other steroidal and nonsteroidal inducers of in vitro meiosis reinitiation in Xenopus laevis (1)(2)(3). Membrane interactions are followed by intracellular events, such as Ca2" movements, nucleus-independent protein synthesis, protein phosphorylation/dephosphorylation, and the formation of a cytoplasmic "maturation-promoting factor" (MPF).…”

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confidence: 99%

“…Furthermore, MPF itself is able to decrease cAMP levels. The effects of various pharmacological agents known to mimic progesterone (1,(15)(16)(17) and those of agents devoid of meiotic-inducing capacity and antagonists to progesterone action were also investigated. It appears that, in order to allow germinal vesicle breakdown (GVBD) to occur, cAMP should remain below control levels from the beginning of exposure to progesterone or other active agents for up to 3-5 hr.…”

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confidence: 99%

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Cyclic AMP-mediated control of meiosis: effects of progesterone, cholera toxin, and membrane-active drugs in Xenopus laevis oocytes.

Schorderet‐Slatkine¹,

Schorderet²,

Baulieu³

1982

Proc. Natl. Acad. Sci. U.S.A.

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Progesterone depressed rapidly (50% at 1 min) and persistently cyclic AMP (cAMP) concentration that had been elevated by cholera toxin in Xenopus laevis oocytes. cAMP remained below 1 pmol per oocyte (mean basal level) for 1 hr and thereafter rose to =120% ofcontrol values, while germinal vesicle (nucleus) breakdown did not occur. In the absence ofcholera toxin, progesterone treatment for 6 hr maintained cAMP concentration below the basal level (but not lower than 80%), and germinal vesicle breakdown occurred. Experiments in the presence of phosphodiesterase inhibitors suggested that progesterone modulates adenylate cyclase activity. The maturation promoting factor, which is formed after 3-5 hr of progesterone treatment and provokes germinal vesicle breakdown after its injection into untreated oocytes, also decreased cAMP concentration, an observation that may explain its "autoamplification." Nonsteroidal inducers of meiosis reinitiation (e.g., propranolol, methoxyverapamil, mersalyl) diminished the cholera toxin-mediated accumulation of cAMP, in contrast to compounds devoid of meiotic-inducing capacity and antagonists to progesterone action, such as gammexane (an inositol analogue) and 5'-deoxy-S-(2-methylpropyl)-5'-thioadenosine (a methylase inhibitor), that increased the nucleotide level. The fine control, suggested by the effects of small changes in cAMP levels, gives evidence of great sensitivity to a critical determinant governing meiotic cell division.A large body ofdata suggests the involvement ofmembrane sites for progesterone and other steroidal and nonsteroidal inducers of in vitro meiosis reinitiation in Xenopus laevis (1-3). Membrane interactions are followed by intracellular events, such as Ca2" movements, nucleus-independent protein synthesis, protein phosphorylation/dephosphorylation, and the formation of a cytoplasmic "maturation-promoting factor" (MPF). MPF itself can induce meiotic cell division (maturation) in ==2-3 hr, when it is transferred into recipient oocytes that have not been exposed to progesterone (4,5).In addition, a regulatory role for cyclic AMP (cAMP) known to be implicated in the control of cell division processes (6, 7), has been suggested on the basis of two series of experiments. Purified subunits of cAMP-dependent protein kinase, isolated from rabbit muscle, have been injected into recipient oocytes (8). The catalytic subunit inhibited the progesterone-induced process, whereas the regulatory subunit directly induced cell division (as did the inhibitor ofthe catalytic subunit). Secondly, progesterone-induced reinitiation of meiosis was inhibited by cholera toxin. This observation led to experiments which suggested that cAMP is involved in the control of progesteroneinduced meiosis (9, 10). This, together with the results of MPF injected at various times into the oocytes (10), indicated a regulatory role for cAMP in MPF formation and amplification-i.e., during the 3-to 5-hr period of progesterone exposure. Measurements ofcAMP in progesterone-treated oocytes ofXenopus...

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“…This resumption leads to the dissolution of the nuclear membrane, followed by chromosome condensation and the meiotic divisions up to the second metaphase . Several observations have led to the suggestion that a progesterone-induced increase in intracellular free calcium may be a necessary first step for the resumption of meiosis (1,15,17,30) . Recently, we have demonstrated directly, using the calcium-specific photoprotein aequorin, that progesterone does cause a rapid, but only transient increase in the free calcium level in oocytes (32) .…”

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Calmodulin triggers the resumption of meiosis in amphibian oocytes.

Wasserman¹,

Smith²

1981

The Journal of Cell Biology

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The calcium-binding protein, caimodulin, has been purified from Xenopus laevis oocytes. This 18,500-dalton protein, pl 4.3, has two high-affinity calcium-binding sites per mole protein having a dissociation constant of 2 .8 X 10 -6 M .Full-grown Xenopus oocytes, arrested in late G2 of the meiotic cell cycle, resumed meiosis when microinjected with 60-80 ng (3-4 pmol) of calmodulin in the form of a calciumcalmodulin complex . The timing of the meiotic events in these recipient oocytes was the same as that normally induced by progesterone .Xenopus ovarian calmodulin stimulated bovine brain phosphodiesterase (PDE) 3-to 10-fold in a calcium-dependent manner, but it had no apparent effect on ovarian PDE activity . A calcium-calmodulin-dependent protein kinase has been isolated from Xenopus oocytes using a calmodulin-Sepharose 413 affinity column . The possible role for this kinase in regulating the G2-M transition in oocytes has been discussed .Amphibian oocytes, arrested in late prophase of meiosis (G2), resume meiosis in response to progesterone (26,31) . This resumption leads to the dissolution of the nuclear membrane, followed by chromosome condensation and the meiotic divisions up to the second metaphase . Several observations have led to the suggestion that a progesterone-induced increase in intracellular free calcium may be a necessary first step for the resumption of meiosis (1,15,17,30) . Recently, we have demonstrated directly, using the calcium-specific photoprotein aequorin, that progesterone does cause a rapid, but only transient increase in the free calcium level in oocytes (32) . The mechanism by which an increased calcium activity might regulate the G 2 -M transition remains unsolved at this time .Increasing evidence indicates that a calcium-binding protein, designated calmodulin, plays a key role in regulating many calcium-dependent processes . Calmodulin is a highly conserved protein that has been identified in a variety of cell types; we have presented preliminary evidence suggesting that Xenopus oocytes also contain this protein (27) . In the current study, we have more fully characterized oocyte calmodulin with respect to its physical and biological properties . More significantly, we demonstrate that oocyte calmodulin, in the form of a calcium-calmodulin complex, can trigger the resumption of THE JOURNAL OF CELL BIOLOGY " VOLUME 89 JUNE 1981 389-394 ©The Rockefeller University Press -0021-9525/81/06/0389/06 $1 .00 meiosis (oocyte maturation) when injected into full-grown Xenopus oocytes.We have attempted to elucidate the mechanism by which calmodulin induces the resumption of meiosis in oocytes. The results indicate that oocyte calmodulin does*not regulate ovarian phosphodiesterase but may be involved in the activation of oocyte protein kinases . MATERIALS AND METHODS Isolation of Calmodulin from Xenopus Oocytes and Bovine BrainApproximately 75 g (wet wt) of Xenopusovary were processed as described by Dedman et al . (5) for the preparation of rat testis calmodulin, with the following m...

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Steroid-induced meiotic division in Xenopus laevis oocytes: surface and calcium

Cited by 268 publications

References 69 publications

Developmentally Controlled Cleavage of the Calliphora Arylphorin Receptor and Posttranslational Action of the Steroid Hormone 20‐Hydroxyecysone

Developmentally Controlled Cleavage of the Calliphora Arylphorin Receptor and Posttranslational Action of the Steroid Hormone 20‐Hydroxyecysone

Cyclic AMP-mediated control of meiosis: effects of progesterone, cholera toxin, and membrane-active drugs in Xenopus laevis oocytes.

Calmodulin triggers the resumption of meiosis in amphibian oocytes.

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