The heterogeneous nuclear ribonucleoprotein (hnRNP)-like estrogen response element-binding protein (ERE-BP) competes with estrogen receptor α (ERα) for occupancy of estrogen response elements (EREs). Here we report that ERE-BP potently stimulates osteoclastogenesis. ERE-BP mRNA and protein were found to be expressed ubiquitously in bone. Overexpression of ERE-BP in cultured osteoblasts stimulated expression of the receptor activator of NF-κB ligand (RANKL) and decreased osteoprotegerin (OPG). The effect of ERE-BP on RANKL was shown to be transcriptional in transient transfection assay and competed with via the ER. Constitutive expression of ERE-BP increased the sensitivity of cells toward 1,25-dihydroxyvitamin D(3) stimulation of RANKL expression. In contrast, knockdown of ERE-BP in stromal ST-2 cells decreased basal RANKL promoter activity. Cocultures of ERE-BP lentivirus-transduced ST-2 cells with spleen monocytes induced formation of multinucleated osteoclasts (OCs) characterized by tartrate-resistant acid phosphatase, calcitonin receptors, and functional calcium resorption from bone slices. Although ERα competed with ERE-BP for an ERE in a dose-dependent manner, ERE-BP was an independent and potent regulator of RANKL and osteoclastogenesis. In preosteoclastic RAW cells, overexpression of ERE-BP increased RANK, upregulated NF-κB signaling, and enhanced differentiation toward a mature OC phenotype independent of RANKL. These results identify ERE-BP as a potent modulator of osteoclastogenesis. We hypothesize that ERE-BP may play a critical role in the regulation of bone homeostasis as a modulator of estrogen sensitivity as well as by direct action on the transcription of critical osteoclastogenic genes.
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http://dx.doi.org/10.1002/jbmr.456 | DOI Listing |
Clin Biochem
November 2013
Hormone Receptor Laboratory, Department of Biochemistry & Molecular Biology, Brown Cancer Center, University of Louisville, Louisville, KY 40292, USA; Institute for Molecular Diversity & Drug Design, University of Louisville, Louisville, KY 40292, USA.
Background: While investigating estrogen response element (ERE) binding properties of human estrogen receptor-α (hERα) in breast cancer cytosols, other ERE-binding proteins (ERE-BP) were observed.
Design And Methods: Recognition properties of ERE-BP were evaluated by electrophoretic mobility shift assays (EMSA) with ERE sequences of the 5'-flanking region of the estrogen responsive gene vitellogenin A2 (VitA2). Cytosols were incubated 16 h, 4 °C with [32P]ERE sequences and separated by EMSA.
J Bone Miner Res
October 2011
Veterans Administration Medical Center and Division of Endocrinology, Metabolism, and Lipids, Department of Medicine, Emory University School of Medicine, Atlanta, GA, USA.
The heterogeneous nuclear ribonucleoprotein (hnRNP)-like estrogen response element-binding protein (ERE-BP) competes with estrogen receptor α (ERα) for occupancy of estrogen response elements (EREs). Here we report that ERE-BP potently stimulates osteoclastogenesis. ERE-BP mRNA and protein were found to be expressed ubiquitously in bone.
View Article and Find Full Text PDFEndocrinology
May 2009
Division of Endocrinology, Metabolism, and Lipids, Department of Medicine, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
Biological responses to estrogens are dependent on the integrated actions of proteins, including the estrogen receptor (ER)-alpha, that regulate the transcription of estrogen response element (ERE)-containing target genes. We have identified a naturally occurring ERE antagonist, termed an ERE-binding protein (BP). To verify that ERE-BP can induce estradiol (E(2)) resistance in vivo, we generated transgenic mice that overexpress this protein in breast tissue.
View Article and Find Full Text PDFAdv Exp Med Biol
July 2008
Hormone Receptor Laboratory, Department of Biochemistry and Molecular Biology, University of Louisville, Louisville, KY, USA.
Our goal is to identify new molecular targets for drug design and improve understanding of the molecular basis of clinical behavior and therapeutic response of breast cancer (BC). Pure populations of BC cells were procured by laser capture microdissection (LCM) from deidentified tissue specimens. RNA from either LCM-procured cells or whole tissue sections was extracted, purified, and quantified by RT-qPCR using beta-actin for relative quantification.
View Article and Find Full Text PDFMol Endocrinol
March 2008
Division of Endocrinology, Metabolism, and Lipids, Department of Medicine, Emory University School of Medicine, Atlanta, Georgia 30322, USA.
New World primates exhibit a form of resistance to estrogens that is associated with overexpression of an estrogen response element (ERE)-binding protein (ERE-BP) and an intracellular estradiol (E(2))-binding protein (IEBP). Both proteins suppress E(2)-mediated transcription when overexpressed in estrogen receptor-alpha (ERalpha)-positive cells. Although ERE-BP acts as a competitor for ERE occupancy by liganded ERalpha, the function of IEBP and its human homolog, heat-shock protein 27 (hsp27), is less clear.
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