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Journal of Biomolecular Screening
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Article

A High-Throughput Liposome Substrate Assay with Automated Lipid Extraction Process for PI 3-Kinase

Trupti Lingaraj, John Donavan, Zhi Li, Ping Li, Amanda Doucette, Sean Harrison, Jeffrey A. Ecsedy, Lenny Dang, and Wenhai Zhang*

* To whom correspondence should be addressed. E-mail: wenhai.zhang{at}mpi.com.


  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)P2 to PI (3,4,5)P3, which acts as a lipid second messenger to activate mitogenic signaling cascades. Recently, p110{alpha}, 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. (Journal of Biomolecular Screening XXXX:xx-xx)

First published on September 23, 2008, doi:10.1177/1087057108324498

Journal of Biomolecular Screening 2008;13:906.

A more recent version of this article appeared on October 1, 2008

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D. J. Demian, S. L. Clugston, M. M. Foster, L. Rameh, D. Sarkes, S. A. Townson, L. Yang, M. Zhang, and M. E. Charlton
High-Throughput, Cell-Free, Liposome-Based Approach for Assessing In Vitro Activity of Lipid Kinases
J Biomol Screen, August 1, 2009; 14(7): 838 - 844.
[Abstract] [PDF]