Thomas Hurley

Differential effects of placental lactogen, growth hormone and prolactin on rat liver ornithine decarboxylase activity in the perinatal period.

Abstract Ovine placental lactogen, (oPL), ovine growth hormone, (oGH), and ovine prolactin, (oPRL) are present in high concentrations in the fetal circulation late in gestation. To determine if these hormones stimulate the activity of ornithine decarboxylase (ODC), an enzyme widely implicated in the control of cellular growth, rat fetuses were injected in utero with 100 μg of oPL, oGH, oPRL, rat growth hormone (rGH) or rat prolactin (rPRL) and ODC activity in the livers, hearts, and brains of the fetuses was measured 2, 4, and 6 hours after injection. OPL stimulated fetal liver ODC activity by 282 ± 45% (mean ± SEM) as compared to litter mates injected with buffer alone but oGH, oPRL, rGH and rPRL had no effect on fetal liver ODC activity. However, in neonatal rats 24–48 hours old all five hormones significantly increased liver ODC activity. ODC activities in the hearts and brains of the fetuses and neonates were unaffected by any of the five hormones. In other experiments 50 μg of oPL significantly stimulated fetal liver ODC activity while 250 μg of oGH were without effect. However 25 μg of oGH significantly stimulated liver ODC activity in rat pups 1–2 days after birth. These results suggest that oPL, by its stimulation of ODC activity, has somatotropic effects in the fetus and that rat liver ODC activity becomes responsive to growth hormone and prolactin in the perinatal period.

Evidence for homology between ovine and human placental lactogens

The biological and immunological properties of highly purified ovine placental lactogen (oPL) and human placental lactogen (hPL) have been compared. Like hPL and ovine prolactin (oPR). oPL stimulates lactation in vivo and in vitro and binds to prolactin receptors from mammary tissue. Like hPL and ovine growth hormone (oGH), oPL binds to growth hormone receptors from liver. OPL of equivalent activity to hPL in the prolactin receptor assay is approximately 20 times more active than hPL (but 5 times less active than oGH) in the growth hormone receptor assay. Immunologically, oPL cross-reacts with oGH but not with hPL. The striking homologies between oPL, and hPL indicate that sheep is an excellent animal model in which to study placental lactogen physiology.

Ovine placental lactogen stimulation of ornithine decarboxylase activity in brain and liver of neonatal rats.

Abstract Ovine placental lactogen (oPL), growth hormone (oGH), prolactin (oPRL) and human placental lactogen (hPL) were administered intracisternally (ic) or intraperitoneally (ip) to 17 day old rats and brain and liver ODC activities determined four hours later. When given ic, oPL, oGH and oPRL caused significant increases in brain ODC activity, while hPL had no significant effect. After ip administration, oPL and oGH also caused a significant increase in brain as well as liver ODC activity but oPRL and hPL were without significant effect. The stimulation of polyamine metabolism by oPL together with earlier reports of its potent somatotropic effects and its high concentration in the fetus supports the hypothesis that oPL may be important in the regulation of fetal growth.

Development of the sheep as an animal model to study placental lactogen physiology

Ovine placental lactogen, purified from term sheep cotyledons, has been found to have chemical and biologic properties similar to those of human placental lactogen, ovine growth hormone, and ovine prolactin. OPL stimulates lactation in vivo and in vitro and binds to prolactin and growth hormone membrane receptors. Its binding to growth hormone receptors is approximately 20 times greater than that of hPL, suggesting that its somatotrophic potency is greater than that of hPL. Preliminary in vivo studies in the sheep indicate that oPL affects maternal carbohydrate, lipid, and protein metabolism and that its effects are, in part, similar to those of hPL and growth hormone.

Synthesis of Prolactin by Human Decidua in Vitro

To determine whether human decidua and/or chorion synthesizes and secretes prolactin, explants of decidua obtained at Caesarian section and explants of chorion from the membranes separating dizygotic twins were cultured for periods of up to 6 days. The decidual explants released 366 +/- 37 ng prolactin/100 mg tissue (mean +/- S.D.) during each day in culture and incorporated 3H-labelled amino acids into immunoprecipitable prolactin. In the radioimmunoassay for prolactin, serial dilutions of incubation medium displaced 125I-labelled prolactin parallel to the displacement by pituitary prolactin and the prolactin in the medium eluted from Sephadex G-150 in a position indentical to that of pituitary prolactin. Chorionic explants released prolactin into the incubation medium during day 1 of culture only and did not incorporate 3H-labelled amino acids into prolactin. These results demonstrate that prolactin is synthesized by the decidua and not by the chorion and suggest that the decidua is the source of prolactin in amniotic fluid.

Prolactin Synthesis by Human Chorion-Decidual Tissue: A Possible Source of Prolactin in the Amniotic Fluid

Explants of human chorion-decidual tissue obtained at delivery from normal, full-term pregnancies synthesize and secrete prolactin. This hormone is indistinguishable from pituitary prolactin by chromatographic, electrophoretic, immunologic, and receptor assay techniques. These results suggest that chorion-decidua may be the source of the large quantities of prolactin in amniotic fluid.