8
Views
40
CrossRef citations to date
0
Altmetric
Gene Expression

Dynamic Cell Type Specificity of SRC-1 Coactivator in Modulating Uterine Progesterone Receptor Function in Mice

, , , , , & show all
Pages 8150-8165 | Received 11 Mar 2005, Accepted 29 Jun 2005, Published online: 27 Mar 2023

REFERENCES

  • Anzick, S. L., J. Kononen, R. L. Walker, D. O. Azorsa, M. M. Tanner, X. Y. Guan, G. Sauter, O. P. Kallioniemi, J. M. Trent, and P. S. Meltzer. 1997. AIB1, a steroid receptor coactivator amplified in breast and ovarian cancer. Science 277:965–968.
  • Biffo, S. 1992. In situ hybridization: optimization of the techniques for collecting and fixing the specimens. Liver 12:227–229.
  • Borud, B., T. Hoang, M. Bakke, A. L. Jacob, J. Lund, and G. Mellgren. 2002. The nuclear receptor coactivators p300/CBP/Cointegrator-Associated Protein (p/CIP) and Transcription Intermediary Factor 2 (TIF2) differentially regulate PKA-stimulated transcriptional activity of steroidogenic factor 1. Mol. Endocrinol. 16:757–773.
  • Buchholz, F., P. Angrand, and A. Stewart. 1996. A simple assay to determine the functionality of Cre or FLP recombination targets in genomic manipulation constructs. Nucleic Acids Res. 24:3118–3119.
  • Buchholz, F., P. O. Angrand, and A. F. Stewart. 1996. A simple assay to determine the functionality of Cre or FLP recombination targets in genomic manipulation constructs. Nucleic Acids Res. 24:3118–3119.
  • Das, S. K., J. Tan, D. C. Johnson, and S. K. Dey. 1998. Differential spatiotemporal regulation of lactoferrin and progesterone receptor genes in the mouse uterus by primary estrogen, catechol estrogen, and xenoestrogen. Endocrinology 139:2905–2915.
  • Dong, H., R. J. O'Brien, E. T. Fung, A. A. Lanahan, P. F. Worley, and R. L. Huganir. 1997. GRIP: a synaptic PDZ domain-containing protein that interacts with AMPA receptors. Nature 386:279–284.
  • Ellis, H. M., D. Yu, T. DiTizio, and D. L. Court. 2001. High efficiency mutagenesis, repair, and engineering of chromosomal DNA using single-stranded oligonucleotides. Proc. Natl. Acad. Sci. USA 98:6742–6746.
  • Finn, C. A., and A. M. Lawn. 1967. Specialized junctions between decidual cells in the uterus of the pregnant mouse. J. Ultrastruct. Res. 20:321–327.
  • Gehin, M., M. Mark, C. Dennefeld, A. Dierich, H. Gronemeyer, and P. Chambon. 2002. The function of TIF2/GRIP1 in mouse reproduction is distinct from those of SRC-1 and p/CIP. Mol. Cell. Biol. 22:5923–5937.
  • Gong, S., C. Zheng, M. L. Doughty, K. Losos, N. Didkovsky, U. B. Schambra, N. J. Nowak, A. Joyner, G. Leblanc, M. E. Hatten, and N. Heintz. 2003. A gene expression atlas of the central nervous system based on bacterial artificial chromosomes. Nature 425:917–925.
  • Halachmi, S., E. Marden, G. Martin, H. MacKay, C. Abbondanza, and M. Brown. 1994. Estrogen receptor-associated proteins: possible mediators of hormone-induced transcription. Science 264:1455–1458.
  • Heintz, N. 2000. Analysis of mammalian central nervous system gene expression and function using bacterial artificial chromosome-mediated transgenesis. Hum. Mol. Genet. 9:937–943.
  • Heintz, N. 2001. BAC to the future: the use of bac transgenic mice for neuroscience research. Nat. Rev. Neurosci. 2:861–870.
  • Hong, H., K. Kohli, M. J. Garabedian, and M. R. Stallcup. 1997. GRIP1, a transcriptional coactivator for the AF-2 transactivation domain of steroid, thyroid, retinoid, and vitamin D receptors. Mol. Cell. Biol. 17:2735–2744.
  • Ing, N. H., J. M. Beekman, S. Y. Tsai, M. J. Tsai, and B. W. O'Malley. 1992. Members of the steroid hormone receptor superfamily interact with TFIIB (S300-II). J. Biol. Chem. 267:17617–17623.
  • Jackson, T. A., J. K. Richer, D. L. Bain, G. S. Takimoto, L. Tung, and K. B. Horwitz. 1997. The partial agonist activity of antagonist-occupied steroid receptors is controlled by a novel hinge domain-binding coactivator L7/SPA and the corepressors N-CoR or SMRT. Mol. Endocrinol. 11:693–705.
  • Kershah, S. M., M. M. Desouki, K. L. Koterba, and B. G. Rowan. 2004. Expression of estrogen receptor coregulators in normal and malignant human endometrium. Gynecol. Oncol. 92:304–313.
  • Lee, E. C., D. Yu, J. Martinez de Velasco, L. Tessarollo, D. A. Swing, D. L. Court, N. A. Jenkins, and N. G. Copeland. 2001. A highly efficient Escherichia coli-based chromosome engineering system adapted for recombinogenic targeting and subcloning of BAC DNA. Genomics 73:56–65.
  • Li, H., P. J. Gomes, and J. D. Chen. 1997. RAC3, a steroid/nuclear receptor-associated coactivator that is related to SRC-1 and TIF2. Proc. Natl. Acad. Sci. USA 94:8479–8484.
  • Li, X., J. Wong, S. Y. Tsai, M. J. Tsai, and B. W. O'Malley. 2003. Progesterone and glucocorticoid receptors recruit distinct coactivator complexes and promote distinct patterns of local chromatin modification. Mol. Cell. Biol. 23:3763–3773.
  • Liu, C. Q., Z. X. Wang, and Y. Yuan. 2002. Effect of mifepristone on uterine receptivity in guinea pigs. Acta. Pharmacol. Sin. 23:177–182.
  • Lydon, J. P., F. J. DeMayo, O. M. Conneely, and B. W. O'Malley. 1996. Reproductive phenotpes of the progesterone receptor null mutant mouse. J. Steroid Biochem. Mol. Biol. 56:67–77.
  • Lydon, J. P., F. J. DeMayo, C. R. Funk, S. K. Mani, A. R. Hughes, C. A. Montgomery, Jr., G. Shyamala, O. M. Conneely, and B. W. O'Malley. 1995. Mice lacking progesterone receptor exhibit pleiotropic reproductive abnormalities. Genes Dev. 9:2266–2278.
  • Matsumoto, H., X. Zhao, S. K. Das, B. L. Hogan, and S. K. Dey. 2002. Indian hedgehog as a progesterone-responsive factor mediating epithelial-mesenchymal interactions in the mouse uterus. Dev. Biol. 245:280–290.
  • McKenna, N. J., and B. W. O'Malley. 2002. Combinatorial control of gene expression by nuclear receptors and coregulators. Cell 108:465–474.
  • Noda, N., H. Minoura, R. Nishiura, N. Toyoda, K. Imanaka-Yoshida, T. Sakakura, and T. Yoshida. 2000. Expression of tenascin-c in stromal cells of the murine uterus during early pregnancy: induction by interleukin-1{alpha}, prostaglandin E2, and prostaglandin F2{alpha}. Biol. Reprod. 63:1713–1720.
  • Onate, S. A., S. Y. Tsai, M. J. Tsai, and B. W. O'Malley. 1995. Sequence and characterization of a coactivator for the steroid hormone receptor superfamily. Science 270:1354–1357.
  • Shao, W., S. Halachmi, and M. Brown. 2002. ERAP140, a conserved tissue-specific nuclear receptor coactivator. Mol. Cell. Biol. 22:3358–3372.
  • Smith, C. L., Z. Nawaz, and B. W. O'Malley. 1997. Coactivator and corepressor regulation of the agonist/antagonist activity of the mixed antiestrogen, 4-hydroxytamoxifen. Mol. Endocrinol. 11:657–666.
  • Smith, D. F., and D. O. Toft. 1992. Composition, assembly and activation of the avian progesterone receptor. J. Steroid Biochem. Mol. Biol. 41:201–207.
  • Suen, C. S., T. J. Berrodin, R. Mastroeni, B. J. Cheskis, C. R. Lyttle, and D. E. Frail. 1998. A transcriptional coactivator, steroid receptor coactivator-3, selectively augments steroid receptor transcriptional activity. J. Biol. Chem. 273:27645–27653.
  • Takamoto, N., B. Zhao, S. Y. Tsai, and F. J. DeMayo. 2002. Identification of Indian hedgehog as a progesterone-responsive gene in the murine uterus. Mol. Endocrinol. 16:2338–2348.
  • Takeshita, A., G. R. Cardona, N. Koibuchi, C. S. Suen, and W. W. Chin. 1997. TRAM-1, A novel 160-kDa thyroid hormone receptor activator molecule, exhibits distinct properties from steroid receptor coactivator-1. J. Biol. Chem. 272:27629–27634.
  • Tibbetts, T. A., M. Mendoza-Meneses, B. W. O'Malley, and O. M. Conneely. 1998. Mutual and intercompartmental regulation of estrogen receptor and progesterone receptor expression in the mouse uterus. Biol. Reprod. 59:1143–1152.
  • Torchia, J., D. W. Rose, J. Inostroza, Y. Kamei, S. Westin, C. K. Glass, and M. G. Rosenfeld. 1997. The transcriptional co-activator p/CIP binds CBP and mediates nuclear-receptor function. Nature 387:677–684.
  • Tsai, M., and B. W. O'Malley. 1994. Molecular mechanisms of action of steroid/thyroid receptor superfamily members. Annu. Rev. Biochem. 63:451–486.
  • Voegel, J., M. Heine, C. Zechel, P. Chambon, and H. Gronemeyer. 1996. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15:3667–3675.
  • Voegel, J. J., M. J. Heine, C. Zechel, P. Chambon, and H. Gronemeyer. 1996. TIF2, a 160 kDa transcriptional mediator for the ligand-dependent activation function AF-2 of nuclear receptors. EMBO J. 15:3667–3675.
  • Wagner, B. L., J. D. Norris, T. A. Knotts, N. L. Weigel, and D. P. McDonnell. 1998. The nuclear corepressors NCoR and SMRT are key regulators of both ligand- and 8-bromo-cyclic AMP-dependent transcriptional activity of the human progesterone receptor. Mol. Cell. Biol. 18:1369–1378.
  • Wewer, U. M., A. Damjanov, J. Weiss, L. A. Liotta, and I. Damjanov. 1986. Mouse endometrial stromal cells produce basement-membrane components. Differentiation 32:49–58.
  • Xie, W., H. Hong, N. N. Yang, R. J. Lin, C. M. Simon, M. R. Stallcup, and R. M. Evans. 1999. Constitutive activation of transcription and binding of coactivator by estrogen-related receptors 1 and 2. Mol. Endocrinol. 13:2151–2162.
  • Xu, J., L. Liao, G. Ning, H. Yoshida-Komiya, C. Deng, and B. W. O'Malley. 2000. The steroid receptor coactivator SRC-3 (p/CIP/RAC3/AIB1/ACTR/TRAM-1) is required for normal growth, puberty, female reproductive function, and mammary gland development. Proc. Natl. Acad. Sci. USA 97:6379–6384.
  • Xu, J., Y. Qiu, F. J. DeMayo, S. Y. Tsai, M. J. Tsai, and B. W. O'Malley. 1998. Partial hormone resistance in mice with disruption of the steroid receptor coactivator-1 (SRC-1) gene. Science 279:1922–1925.
  • Yang, X. W., C. Wynder, M. L. Doughty, and N. Heintz. 1999. BAC-mediated gene-dosage analysis reveals a role for Zipro1 (Ru49/Zfp38) in progenitor cell proliferation in cerebellum and skin. Nat. Genet. 22:327–335.
  • Yu, D., and D. L. Court. 1998. A new system to place single copies of genes, sites and lacZ fusions on the Escherichia coli chromosome. Gene 223:77–81.
  • Yu, D., H. M. Ellis, E. C. Lee, N. A. Jenkins, N. G. Copeland, and D. L. Court. 2000. An efficient recombination system for chromosome engineering in Escherichia coli. Proc. Natl. Acad. Sci. USA 97:5978–5983.

Reprints and Corporate Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

To request a reprint or corporate permissions for this article, please click on the relevant link below:

Academic Permissions

Please note: Selecting permissions does not provide access to the full text of the article, please see our help page How do I view content?

Obtain permissions instantly via Rightslink by clicking on the button below:

If you are unable to obtain permissions via Rightslink, please complete and submit this Permissions form. For more information, please visit our Permissions help page.