Acylphosphatase synergizes with progesterone during maturation of Xenopus laevis oocytes.
Xenopus laevis oocytes are physiologically arrested in the G2/M phase border of the first meiotic division. A number of different stimuli can trigger off the re-entry into the cell cycle as a consequence of activation of either membrane-dependent or -independent intracellular signals. This system has been widely used to study signal transduction mechanisms induced by hormones. Among those more intensively researched, special attention has been devoted to elucidate the mechanism of activation induced by progesterone. However, despite intense efforts to understand the intracellular signalling mechanism of progesterone, a clear notion of the most relevant events involved in this process has not yet been elucidated. We provide evidence that acylphosphatase, an enzyme responsible for the regulation of membrane pumps in eukaryotic cells, synergizes with progesterone for induction of oocyte maturation. We deduced that this synergism may be related to the regulation of intracellular Ca2+ levels for several reasons: (1) maturation of oocytes by extracellular Ca2+ is blocked by acylphosphatase; (2) both progesterone and acylphosphatase drastically reduced Ca2+ uptake; (3) progesterone-induced maturation does not depend on a rise in intracellular Ca2+, since microinjection of EGTA, a calcium chelator, does not affect maturation induced by progesterone.
Instituto de Investigaciones Biomédicas, CSIC, Madrid, Spain.
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Dolfi
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Carnero
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Cuadrado
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Ramponi
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Lacal
D017766:Acid Anhydride Hydrolases; D000818:Animals; D002118:Calcium / Q000378:metabolism; D005260:Female; D006706:Homeostasis; D008540:Meiosis; D008845:Microinjections; D009865:Oocytes / Q000166:cytology*; D010744:Phosphoric Monoester Hydrolases / Q000502:physiology*; D011374:Progesterone / Q000502:physiology*; D014982:Xenopus laevis; D000097024:Acylphosphatase
D017766:Acid Anhydride Hydrolases; D002118:Calcium; D010744:Phosphoric Monoester Hydrolases; D011374:Progesterone; D000097024:Acylphosphatase