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Related Experiment Video

Updated: May 21, 2026

Quantitative and Qualitative Method for Sphingomyelin by LC-MS Using Two Stable Isotopically Labeled Sphingomyelin Species
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Quantitative and Qualitative Method for Sphingomyelin by LC-MS Using Two Stable Isotopically Labeled Sphingomyelin Species

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A high-throughput sphingomyelinase assay using natural substrate.

Miao Xu1, Ke Liu, Noel Southall

  • 1National Center for Advancing Translational Sciences, National Institutes of Health, Bethesda, MD 20892-3370, USA.

Analytical and Bioanalytical Chemistry
|June 20, 2012
PubMed
Summary
This summary is machine-generated.

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Researchers developed a high-throughput assay to find sphingomyelinase inhibitors. This assay screened 300,000 compounds, identifying eight potential inhibitors for therapeutic development against diseases like diabetes and obesity.

Area of Science:

  • Biochemistry
  • Enzymology
  • Drug Discovery

Background:

  • Sphingomyelinases hydrolyze sphingomyelin into ceramide, a key signaling molecule.
  • Ceramide regulates cellular processes including proliferation, apoptosis, and inflammation.
  • Inhibiting sphingomyelinase is a potential therapeutic strategy for atherosclerosis, diabetes, obesity, and infections.

Purpose of the Study:

  • To develop a high-throughput assay for identifying novel sphingomyelinase inhibitors.
  • To screen a large compound library for potential therapeutic agents targeting sphingomyelinase.

Main Methods:

  • Developed a 1,536-well plate assay using the natural substrate sphingomyelin.
  • Validated assay robustness with signal-to-basal ratios of 6.1 (pH 5.0) and 4.3 (pH 6.5).

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Last Updated: May 21, 2026

Quantitative and Qualitative Method for Sphingomyelin by LC-MS Using Two Stable Isotopically Labeled Sphingomyelin Species
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  • Screened approximately 300,000 compounds to identify inhibitors.

    • Main Results:

    • Identified eight compounds exhibiting sphingomyelinase inhibitory activity (IC50s ranging from 1.7 to 38.2 µM).
    • Observed differential activity between the natural substrate assay and a profluorescence substrate assay.
    • Demonstrated the assay's effectiveness in identifying inhibitors with varying profiles.

    Conclusions:

    • The developed natural substrate sphingomyelinase assay is robust and effective for high-throughput screening.
    • The identified compounds represent potential leads for developing therapeutics targeting sphingomyelinase-related diseases.
    • This assay facilitates the discovery of novel sphingomyelinase inhibitors for diverse therapeutic applications.