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Journal of Biomolecular Screening
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Article

A High-Content Glucocorticoid Receptor Translocation Assay for Compound Mechanism-of-Action Evaluation

Michele Agler*, Margaret Prack, Yingjie Zhu, Janet Kolb, Kimberly Nowak, Rolf Ryseck, Ding Shen, Mary Ellen Cvijic, John Somerville, Steve Nadler, and Taosheng Chen

Bristol Myers Squibb

* To whom correspondence should be addressed. E-mail: michele.agler{at}bms.com.


  Abstract
Ligand-induced cytoplasm to nucleus translocation is a critical event in the nuclear receptor (NR) signal transduction cascade. The development of green fluorescent proteins and their color variants fused with NRs, along with the recent developments in automated cellular imaging technologies, has provided unique tools to monitor and quantify the NR translocation events. These technology developments have important implications in the mechanistic evaluation of NR signaling and provide a powerful tool for drug discovery. The unique challenges for developing a robust NR translocation assay include cytotoxicity accompanied with chronic overexpression of NRs, basal translocation induced by serum present in culture medium, and interference from endogenous NRs, as well as subcellular dynamics. The authors have developed a robust assay system for the glucocorticoid receptor (GR) that was applied to a panel of nuclear receptor ligands. Using a high-content imaging system, ligand-induced, dose-dependent GR nuclear translocation was quantified and a correlation with other conventional assays established. (Journal of Biomolecular Screening XXXX:xx-xx)

First published on November 7, 2007, doi:10.1177/1087057107309353

Journal of Biomolecular Screening 2007;12:1029.

A more recent version of this article appeared on December 1, 2007

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