Protein phosphatase activity in the rat ovary throughout pregnancy and pseudopregnancy.

Specific protein phosphatase activity against protein kinase C-phosphorylated substrate was measured in the rat ovary during pseudopregnancy and pregnancy. Tissues were processed in the presence of sodium fluoride and inorganic phosphate to inhibit the phosphatase and thereby prevent autodephosphorylation of the type 2A protein phosphatase (PP2A) during homogenization. Manganese was added at the time of enzyme assay to reactivate the phosphatase. The specific activity of the protein phosphatase did not vary significantly across pseudopregnancy (p > 0.05). In contrast, the specific activity of protein phosphatase decreased significantly between Day 7 and Day 10 of pregnancy (28.8 +/- 5 pmol/min x microg protein and 20.7 +/- 2 pmol/min x microg protein, respectively; p < 0.05) and remained at the decreased value for the remainder of pregnancy. To determine whether hormones of pregnancy could regulate PP2A activity in the ovaries, pseudopregnant rats were treated with prolactin (3 IU twice a day), bromocriptine (100 microg twice a day), or estradiol benzoate (50 microg). Bromocriptine and estradiol treatments caused a decrease in PP2A-specific activity, but prolactin had no effect. Bromocriptine treatment caused a decrease in the protein content of the PP2A catalytic subunit, but prolactin and estradiol treatments had no effect. The data suggest that the specific activity and protein content of PP2A in the rat ovary are hormonally regulated.