Abstract:
:Cytosol preparations of human term placenta in Tris-HCl buffer containing dithiothreitol were incubated with [3H]dexamethasone at 4 degrees C. Under these conditions the specific binding of [3H]dexamethasone was low when compared with cytosol preparations of sheep fetal lung or ovine placenta. The inclusion of sodium molybdate in the homogenization buffer and the removal of endogenous steroids by treating the cytosol with charcoal before incubation led to a faster and increased uptake of [3H]dexamethasone by human placenta. Scatchard plot analysis of the data showed that the placenta possesses a single class of high-affinity (Kd = 13 +/- 2 nM) low-capacity (193 +/- 34 fmol/mg protein) binding sites for [3H]dexamethasone. The binding of [3H]dexamethasone was reversible and was not due to plasma contamination. The specificity of the binding sites was confirmed by competition experiments in which the highest displacement of [3H]dexamethasone from the binding sites was caused by natural and synthetic corticosteroids. These findings indicate that the human placenta at term contains specific glucocorticoid receptors in high concentrations.
journal_name
Placentajournal_title
Placentaauthors
López Bernal A,Anderson AB,Turnbull ACdoi
10.1016/s0143-4004(84)80054-5subject
Has Abstractpub_date
1984-03-01 00:00:00pages
105-16issue
2eissn
0143-4004issn
1532-3102pii
S0143-4004(84)80054-5journal_volume
5pub_type
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