摘要
Spermidine or spermine but not putrescine inhibited progesterone induced Bufo bufo gargarizans oocyte maturation.The ID50 for spermine inhibition via intra -oocyte microinjection on maturation induced by progesterone was 6.8mM(100nl).Spermine could inhibit MPF induced toad oocyte maturation with a much higher ID50.A 55 kD protein was dephosphorylated during the process of progesterone induced oocyte maturation .Spermine selectively promoted the level of phosphorylation of this protein in both progesterone-stimulated and hormone-untreated oocytes.The extent of its dephosphorylation was fairly Correlated with the percentage of GVBD in the hormone stimulated oocytes.The level of endogenous spermine was reduced by 28% between the perod of 0.40 GVBD50 and 0.60 GVBD50,at which 55 kD protein was dephosphorylated.Spermine inhibited progesterone-stimulated protein synthesis in almost the same dose dependent manner as its inhititory effect on the hormone-induced maturation,The endogenous spermine regulated 55 kD protein dephosphorylation which may trigger the increase of protein dephosphorylation which may trigger the increase of protein synthesis and in turn promote the activation of MPF,It is possible that 55 kD protein may be one of the components of messenger ribonucleoprotein(mRNP) particles.
Spermidine or spermine but not putrescine inhibited progesterone induced Bufo bufo gargarizans oocyte maturation. The ID50 for spermine inhibition via intra - oocyte mi-croinjection on maturation induced by progesterone was 6. 8 mM(100 nl). Spermine could inhibit MPF induced toad oocyte maturation with a much higher ID50.
A 55 kD protein was dephosphorylated during the process of progesterone induced oocyte maturation. Spermine selectively promoted the level of phosphorylation of ?this protein in both progesterone - stimulated and hormone - untreated oocytes. The extent of its dephosphorylation was fairly correlated with the percentage of GVBD in the hormone stimulated oocytes.
The level of endogenous spermine was reduced by 28% between the period of 0. 40 GVBD50 and 0. 60 GVBD50, at which 55 kD protein was dephosphorylated.
Spermine inhibited progesterone - stimulated protein synthesis in almost the same dose dependent manner as its inhibitory effect on the hormone - induced maturation. The endogenous spermine regulated 55 kD protein dephosphorylation which may trigger the increase of protein synthesis and in turn promote the activation of MPF. It is possible that 55 kD protein may be one of the components of messenger ribonucleoprotein (mRNP) particles.
