The presence of cortisol receptors in the human amnion.

Cytosol extracts of human amnion tissue contained high affinity binding of cortisol (Ka=2.48+/-1.06 x 10(9) M(-1); n = 30) and low capacity binding of cortisol (Nmax=279+/-15.5 fmol mg(-1) protein). Kinetic studies of cortisol binding resulted in a similar value of Ka to that obtained by Scatchard analysis. Nuclear extracts of amnion tissue contained high affinity binding of cortisol (Ka=5.8+/-1.91 x 10(7) M[-1]) and low binding capacity (Nmax=91.4+/-21.4 fmol mg(-1) protein). Ka values were an order of magnitude higher in cytosol than in blood serum when amnion and blood were obtained from the same individuals. Differences in competitive ligand binding, especially dexamethasone, were observed between the amnion receptor and transcortin in serum. Gel permeation chromatography gave only one peak at 320 kDa for amnion receptor and only one peak at 48 kDa for transcortin from serum. When amnion tissue was incubated with or without cortisol, cytosol receptor activity was significantly lower in cortisol treated tissue than in control. The nuclear extracted receptor activity was significantly higher in cortisol treated tissue than control. The Ka values from cortisol treated tissue were significantly lower from control. Together the data support the presence of a specific cortisol receptor in the human amnion that is different from transcortin.