In vivo actions of protein phosphatase inhibitor‐2 in<i>Xenopus</i>oocytes
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TL;DR
The effect of phosphatase inhibitor‐2 was determined on the in vivo rate of dephosphorylation of phosphorylase a and on the rate of oocyte maturation, suggesting a possible role for protein phosph atase‐1 in the regulation of meiosis.
Abstract
Meiotic maturation of amphibian oocytes induced by progesterone is known to be regulated by protein phosphorylation. To investigate a possible role for protein phosphatase-1 in this process, the effect of phosphatase inhibitor-2 was determined on the in vivo rate of dephosphorylation of phosphorylase a and on the rate of oocyte maturation. Dephosphorylation of microinjected phosphorylase a was inhibited up to 40% in the presence of inhibitor-2, with half-maximal inhibition at an intracellular concentration of 0.6 microM. Inhibitor-2 also caused over a 3-fold increase in the half-time for maturation, suggesting a possible role for protein phosphatase-1 in the regulation of meiosis.
