A high-throughput liposome substrate assay with automated lipid extraction process for PI 3-kinase

J Biomol Screen. 2008 Oct;13(9):906-11. doi: 10.1177/1087057108324498. Epub 2008 Sep 23.

Abstract

The signaling pathways involving lipid kinase class I phosphatidylinositol 3-kinases (PI 3-kinases) regulate cell growth, proliferation, and survival. Class I PI 3-kinases catalyze the conversion of PI (4,5)P(2) to PI (3,4,5)P(3), which acts as a lipid second messenger to activate mitogenic signaling cascades. Recently, p110alpha, a class IA PI 3-kinase, was found to be mutated frequently in many human cancers. Therefore, it is increasingly studied as an anticancer drug target. Traditionally, PI 3-kinase activities have been studied using liposome substrates. This method, however, is hampered significantly by the labor-intensive manual lipid extraction followed by a low-throughput thin-layer chromatography analysis. The authors describe a high-throughput liposome substrate-based assay based on an automated lipid extraction method that allows them to study PI 3-kinase enzyme mechanism and quantitatively measure inhibitor activity using liposome substrates in a high-throughput mode. This improved assay format can easily be extended to study other classes of phosphoinositide lipid kinases.

MeSH terms

  • Adenosine Triphosphate / chemistry
  • Automation
  • Biochemistry / methods
  • Chromatography, Thin Layer / methods
  • Humans
  • Inhibitory Concentration 50
  • Kinetics
  • Lipids / chemistry
  • Liposomes / chemistry*
  • Neoplasms / diagnosis*
  • Neoplasms / metabolism
  • Phosphatidylinositol 3-Kinases / chemistry*
  • Phosphatidylinositol 3-Kinases / metabolism
  • Phosphorylation
  • Signal Transduction
  • Substrate Specificity
  • Time Factors

Substances

  • Lipids
  • Liposomes
  • Adenosine Triphosphate
  • Phosphatidylinositol 3-Kinases