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High-content assay to study protein prenylation.

Marjo Simonen1, Yvonne Ibig-Rehm, Gabriele Hofmann

  • 1Novartis Institutes for BioMedical Research, CH-4002 Basel, Switzerland. marjo.simonen@novartis.com

Journal of Biomolecular Screening
|May 30, 2008
PubMed
Summary

A new high-content imaging assay enables efficient study of protein prenylation, a key process in the mevalonate pathway. This method aids in drug discovery for diseases like cancer and high cholesterol.

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Area of Science:

  • Biochemistry
  • Cell Biology
  • Drug Discovery

Background:

  • The mevalonate pathway is crucial for synthesizing cholesterol and isoprenoid lipids.
  • Protein prenylation, mediated by prenyltransferases, is essential for the function of small GTP-binding proteins.
  • Dysregulation of this pathway is implicated in diseases such as cancer, osteoporosis, and high cholesterol.

Purpose of the Study:

  • To develop a high-throughput, imaging-based assay for studying protein prenylation.
  • To provide a more efficient method for drug screening targeting the mevalonate pathway.

Main Methods:

  • Development of a green fluorescent protein (GFP) reporter assay utilizing the H-Ras prenylation motif.
  • Utilizing automated microscopy and image analysis in 96- or 384-well formats.

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  • Validation with mevalonate pathway inhibitors and siRNA against farnesyl pyrophosphate synthase.

    • Main Results:

    • The assay successfully monitors GFP localization, indicating successful or inhibited protein prenylation.
    • Automated analysis provides cell number and nuclear intensity data, useful for toxicity assessment.
    • Validated assay performance using known pathway inhibitors and gene silencing.

    Conclusions:

    • The developed assay is a robust and efficient tool for studying protein prenylation.
    • This high-content imaging assay facilitates drug discovery and development for mevalonate pathway-related diseases.
    • The assay provides valuable insights into compound toxicity during screening.