Ligand-Modulated Regulation of Progesterone Receptor Messenger Ribonucleic Acid and Protein in Human Breast Cancer Cell Lines (original) (raw)
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1Department of Physiology and Biophysics, University of Illinois and, University of Illinois College of Medicine Urbana, Illinois 61801; Ben May Laboratory for Cancer Research, University of Chicago Chicago, Illinois 60637
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1Department of Physiology and Biophysics, University of Illinois and, University of Illinois College of Medicine Urbana, Illinois 61801; Ben May Laboratory for Cancer Research, University of Chicago Chicago, Illinois 60637
Search for other works by this author on:
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1Department of Physiology and Biophysics, University of Illinois and, University of Illinois College of Medicine Urbana, Illinois 61801; Ben May Laboratory for Cancer Research, University of Chicago Chicago, Illinois 60637
Search for other works by this author on:
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1Department of Physiology and Biophysics, University of Illinois and, University of Illinois College of Medicine Urbana, Illinois 61801; Ben May Laboratory for Cancer Research, University of Chicago Chicago, Illinois 60637
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Benita S. Katzeneilenbogen
1Department of Physiology and Biophysics, University of Illinois and, University of Illinois College of Medicine Urbana, Illinois 61801; Ben May Laboratory for Cancer Research, University of Chicago Chicago, Illinois 60637
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This work was supported by NIH Grants HD-21524 and CA-18119 (to B.S.K.) and CA-02897 and ACS-BC86 (to G.L.G). Portions of this work were presented at the Meadowbrook Conference on Steroid Receptors in Health and Disease. (Oakland, Ml, 1987, p. 37 (Abstract 21).
Supported by 5T32HD-7028 from NIH.
Received:
21 October 1987
Accepted:
16 December 1987
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Linnea D. Read, Catherine E. Snider, Jean S. Miller, Geoffrey L. Greene, Benita S. Katzeneilenbogen, Ligand-Modulated Regulation of Progesterone Receptor Messenger Ribonucleic Acid and Protein in Human Breast Cancer Cell Lines, Molecular Endocrinology, Volume 2, Issue 3, 1 March 1988, Pages 263–271, https://doi.org/10.1210/mend-2-3-263
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Abstract
We have examined the effects of estrogen and progestin agonist and antagonist ligands on regulation of progesterone receptor (PR) protein and mRNA levels in a variety of human breast cancer cell lines. By Northern blot analysis, using human PR cDNA probes, PR mRNA in T47D and MCF-7 cells appears as five species of approximately 11.4, 5.8, 5.3, 3.5, and 2.8 kilobases. PR mRNA species are not detected in the PR protein-negative breast cancer cell lines MDA-MB-231 and LY2. T47D cells contain high levels of PR mRNA and protein (detected by hormone binding assay or Western blot analysis), and the PR protein and mRNA content of T47D cells are reduced to about 10% of the control level within 48 h of treatment with 10 n_m_ promegestone; 17,21-dimethyl-19-nor-pregna-4,9-diene-3, 20-dione (R5020) or 16α-ethyl-21-hydroxy-19-nor-pregn-4-ene-3,20-dione (ORG2058), both potent progestins. In contrast, treatment of T47D cells with the antiprogestin 17β-hydroxy-110-[4-dimethylaminophenyl]-17α-(1-propynyl)-estra-4, 9-dien-3-one) (RU38486)reduces PR protein and mRNA levels only transiently. PR protein and mRNA are virtually undetectable in control MCF-7 cells grown in the absence of estrogens. When estradiol is administered to MCF-7 cells, the PR mRNA and protein levels increase gradually and proportionately (10- or 40-fold, respectively, in 3 days). This estradiol stimulation of PR is repressed to basal levels if MCF-7 cells receive a 100-fold excess of the antiestrogen 6-hydroxy-2-(_p_-hydroxyphenyl)benzo(b)thien-3-yl-_p_-[2-1 -pyrrolidinyl) ethoxy]phenylketone; LY117018) concomitantly. After estrogen stimulation of PR in MCF-7 cells, treatment with R5020 or RU38486 results in aca. 50% decrease in PR protein and mRNA content by 2 days. These studies reveal a close correspondence between changes in PR mRNA content and the PR protein content of cells in response to estrogen, antiestrogen, progestin, or antiprogestin exposure, suggesting that the changes in cellular PR protein are accounted for predominantly by changes at the transcriptional (RNA) level.
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Author notes
This work was supported by NIH Grants HD-21524 and CA-18119 (to B.S.K.) and CA-02897 and ACS-BC86 (to G.L.G). Portions of this work were presented at the Meadowbrook Conference on Steroid Receptors in Health and Disease. (Oakland, Ml, 1987, p. 37 (Abstract 21).
*
Supported by 5T32HD-7028 from NIH.
Copyright © 1988 by The Endocrine Society
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