Phosphotryptic peptide analysis of human progesterone receptor. New phosphorylated sites formed in nuclei after hormone treatment.

@article{Sheridan1989PhosphotrypticPA,
  title={Phosphotryptic peptide analysis of human progesterone receptor. New phosphorylated sites formed in nuclei after hormone treatment.},
  author={Philip L. Sheridan and Ronald M Evans and Kathryn B. Horwitz},
  journal={The Journal of biological chemistry},
  year={1989},
  volume={264 11},
  pages={6520-8}
}
Human progesterone receptors (PR) exist as two independent naturally occurring steroid-binding forms of approximately 120 kDa (B-receptors) and 94 kDa (A-receptors). Both are phosphorylated in hormone-untreated T47Dco breast cancer cells. Hormone treatment leads to receptor transformation and an increased phosphorylation state: the 32P-labeling intensity is 3-5 times higher after progestin treatment and 8-10 times higher after RU 486 treatment. Only serine residues are phosphorylated. To… CONTINUE READING
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