[Demonstration of a nuclear androgen receptor in erythroblasts obtained by culture of human bone marrow].
The new techniques of culture of bone marrow have shown that androgens and 5 beta steroids exert a direct effect on erythroid precursor cells from human or animal bone marrow. By contrast, the mechanisms of the intracellular actions of those compounds are poorly understood. Tritiated methyltrienolone (R 1881), a synthetic androgen that highly binds to androgen receptor, has been used for the study of a binding activity in nuclear extracts of cultured erythroblasts from human bone marrow. The nuclear extracts contain binding sites saturable at low concentrations of 3H-R 1881 (20-30 nM). Scatchard analysis revealed that the R 1881-nuclear complex has a dissociation constant (Kd) of 25-50 nM, and the number of binding sites was 235-370 fmoles/mg protein. The complex sedimented on 5-20% sucrose gradient in the 3.9 S region and 5 beta dihydrotestosterone compete strongly with R 1881 for binding sites. This binding component has characteristics of high affinity, low-capacity, sedimentation behaviour, and specificity commonly attributed to "androgen receptors".
D001667:Binding, Competitive; D001854:Bone Marrow Cells; D002467:Cell Nucleus / Q000378:metabolism / Q000648:ultrastructure*; D002478:Cells, Cultured; D004900:Erythroblasts / Q000166:cytology* / Q000378:metabolism; D004963:Estrenes / Q000378:metabolism; D006801:Humans; D007700:Kinetics; D015741:Metribolone; D011944:Receptors, Androgen / Q000032:analysis* / Q000378:metabolism; D045165:Testosterone Congeners / Q000378:metabolism
D004963:Estrenes; D011944:Receptors, Androgen; D045165:Testosterone Congeners; D015741:Metribolone
Mise en évidence d'un récepteur nucléaire des androgènes dans les érythroblastes obtenus par culture de moelle osseuse humaine.