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Prolexys Pharmaceuticals and Columbia University Researchers,Publish Study on Anti-Tumor Properties of a Selective Small,Molecule Anti-Tumor Agent With Novel Mechanism of Action

SALT LAKE CITY, June 14, 2007 /PRNewswire/ -- Prolexys Pharmaceuticals and announced today a publication describing the properties of the selective small molecule anti-tumor agent, erastin. Prolexys and Columbia applied the company's chemi-proteomics technology to understand the mechanism of action of erastin. The results, to be published in the June 14, 2007 issue of the journal Nature reveal that erastin binds to mitochondrial voltage- dependent anion channels (VDACs) -- a novel target for anti-cancer drugs. Knock-down of VDAC2 and VDAC3 gene expression causes resistance to erastin, implicating the involvement of these two proteins in erastin-mediated cell death. Treatment of cells with erastin results in VDAC-protein-mediated mitochondrial dysfunction, release of oxidative species and, ultimately, cell death. This process has a degree of selectivity for cells with aberrantly active RAS pathway. In normal cells, RAS pathway is involved in growth and differentiation of cells; however the aberrant activation of this pathway results in uncontrolled tumor growth.

Dr. Brent Stockwell, currently an Associate Professor of Biological Sciences and of Chemistry at , identified erastin as a small molecule anti-cancer agent that exhibits lethality in human tumor cells with mutations in RAS-related cancer genes such as HRAS, KRAS or BRAF, beginning when he was a Fellow at the Whitehead Institute for Biomedical Research. In February 2005, Prolexys signed an exclusive licensing agreement with the Massachusetts Institute of Technology, as the licensing agent of , and the Whitehead Institute, which provides Prolexys with exclusive, worldwide rights to a patent estate covering selective anti-tumor compounds in the erastin family. "This paper demonstrates that it is feasible to discover compounds that produce cancer-cell-selective toxicity and to use these to understand cell death mechanisms in cancer cells; furthermore,
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