Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones

@article{Joab1984CommonNB,
  title={Common non-hormone binding component in non-transformed chick oviduct receptors of four steroid hormones},
  author={Irène Joab and Christine Radanyi and Michel Renoir and Thierry Buchou and Maria Grazia Catelli and Nadine Binart and J{\'a}n Mester and Etienne Emile Baulieu},
  journal={Nature},
  year={1984},
  volume={308},
  pages={850-853}
}
Steroid hormones produce a response in target cells by binding to hormone-specific soluble receptors, which undergo a transformational change, leading to their interaction with chromatin and to modified gene expression. In a previous paper1, we described a monoclonal antibody, BF4, that specifically recognizes and binds the non-transformed ‘8S’ form of chicken oviduct progesterone receptor (8S–PR). We now show that BF4 does not form an immune complex with the 4S transformed form of 3H-progestin… 
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It is concluded that in vivo or in vitro treatment of nuclear progesterone receptor with either progester one or R5020 or RU38 486 alone can lead to detection of high affinity complexes formed between the PRE and the receptor present in unpurified nuclear extracts.
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TLDR
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The results show that transformation of the 8S receptor components I and II can be achieved in the absence of other cytosolic factors.
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TLDR
An antibody which displaced progesterone binding in sucrose gradients and discovered a new receptor-associated protein, which turned out to be an abundant, cytosol, non-steroid-binding protein of 90 kDa, which could interact with other intracellular proteins such as oncogenic protein kinases.
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TLDR
An isolation procedure based on the observation that the protein is selectively shed from proteins adsorbed to heparin-agarose when molybdate is removed is developed, and the protein obtained is shown to be the same as that isolated from affinity-purified progesterone receptor as compared by protease digestion and one-dimensional peptide mapping.
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TLDR
The structure and composition of the avian progesterone receptor remain unclear, but the same protein has been shown to form complexes with other steroid receptors from the chicken, and may thus be a common element of all nontransformed receptors.
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TLDR
The concept of steroid action that necessarily involves the original formation of the hormone-receptor complexes in the cytoplasm before translocation to the nucleus, may have to be revised.
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TLDR
This work mainly reports on the purification of the cOvPR in different forms including the “native” 8S form containing a non-hormone binding protein referred to as a heat shock protein (hsp 90) of 90kDa molecular weight.
Human progesterone receptor binding to mouse mammary tumor virus deoxyribonucleic acid: dependence on hormone and nonreceptor nuclear factor(s).
TLDR
The results suggest that hormone or a hormone-dependent mechanism increases the intrinsic DNA-binding activity of receptors independent of receptor transformation from 8S to 4S, and experiments indicate that a nonreceptor activity in nuclear extracts can increase the sequence-specific DNA- binding activity of cytosol receptors.
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