Cellular progesterone receptor phosphorylation in response to ligands activating protein kinases |
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| Authors: | K V Rao W D Peralta G L Greene C F Fox |
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| Affiliation: | 1. Department of Emergency Medicine, Stanford University School of Medicine, Palo Alto, Calif;2. Stanford Emergency Medicine Residency, Stanford University School of Medicine, Palo Alto, Calif;3. Department of Computational Science, University of Colorado, Golden;4. MountainView Regional Medical Center, Las Cruces, NM;5. Stanford University School of Medicine, Palo Alto, Calif;6. Medical Service, VA Puget Sound Health Care System, and Division of Pulmonary, Critical Care, and Sleep Medicine, University of Washington, Seattle;1. Department of Kinesiology and Physical Education, McGill University, Montréal, QC, Canada;2. MD Program, Faculty of Medicine and Dentistry, University of Alberta, Edmonton, AB, Canada;3. EWI Works International, Edmonton, AB, Canada |
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| Abstract: | Progesterone receptors were immunoprecipitated with monoclonal antibodies KD68 from lysates of human breast carcinoma T47D cells labelled to steady state specific activity with 32Pi. The 120 kDa 32P-labelled progesterone receptor band was resolved by polyacrylamide gel electrophoresis and identified by autoradiography. Phosphoamino acid analysis revealed serine phosphorylation, but no threonine or tyrosine phosphorylation. Treatment of the 32Pi-labelled cells with EGF, TPA or dibutyryl cAMP had no significant quantitative effect on progesterone receptor phosphorylation, though the EGF receptor and the cAMP-dependent protein kinases have been reported to catalyze phosphorylation of purified avian progesterone receptor preparations in cell free systems. Progesterone receptor phosphorylation on serine residues was increased by 2-fold in cells treated with 10 nM progesterone; EGF had no effect on progesterone-mediated progesterone receptor phosphorylation. |
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