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      Proteomics analysis of the estrogen receptor alpha receptosome.

      Molecular & Cellular Proteomics : MCP

      Animals, Cell Line, Electrophoresis, Gel, Two-Dimensional, Endosomes, chemistry, metabolism, Estrogen Receptor alpha, genetics, Estrogen Receptor beta, Estrogens, Humans, Macromolecular Substances, Molecular Sequence Data, Proteome, analysis, Proteomics, Response Elements, Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization, methods

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          Abstract

          The estrogen receptors (ERs) are ligand-dependent transcription factors that activate transcription by binding to estrogen response elements. Estrogen-mediated effects are tissue- and cell type-specific, determined by the cofactor recruitment to the ERs among other factors. To understand these differences in estrogen action, it is important to identify the various compositions of the ER complexes (ER receptosomes). In this report, we describe a fast and efficient method for the isolation of the ERalpha receptosome for proteomics analysis. Using immobilized estrogen response element on a Sepharose column in combination with two-dimensional electrophoresis and MALDI-TOF MS, significant amounts of proteins could be isolated and identified. Differences in ERalpha complex composition with the ER ligands 17beta-estradiol, 4-hydroxytamoxifen, and ICI-182,780 could also be observed. Thus, this approach provides an easy and relevant way of identifying ERalpha cofactor and transcription factor recruitment under different conditions.

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          Author and article information

          Journal
          20348541
          2938095
          10.1074/mcp.M900457-MCP200

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