Rapid Progress Reported On New Class Of Anti-Cancer Drugs

DALLAS -- An enzyme critical to activating the protein called Ras, which triggers a wide range of cancers, is rapidly yielding its chemical secrets, researchers reported Monday.

What's more, the scientists say, drugs that inhibit the enzyme -- called farnesyl transferase (FTase) -- are proving in laboratory studies to effectively shut down cancer cells.

About one-fourth of all human cancers are caused by genetic malfunctions in the Ras biochemical pathway that result in the uncontrolled growth of cancers. These cancers include up to 90 percent of pancreatic cancers, half of all colon cancers and a quarter of all lung cancers.

The reports by university and pharmaceutical company researchers on progress in both understanding and inhibiting the enzyme were prepared for presentation at an American Chemical Society symposium on "Protein Prenylation."

FTase activates Ras by attaching a 15-carbon farnesyl molecule to the protein -- in the process called prenylation. The fatty farnesyl molecule, a member of a class of compounds called isoprenoids, tags the Ras protein for transport to the cell's outer membrane, where it transmits outside signals from hormones and growth factors that tell the cell to divide.

The symposium included:

Pat Casey, of the Duke University Medical Center, who reported on research by a collaboration of three Duke laboratories into the detailed structure and biochemical mechanism of FTase. According to Casey, these structural and mechanistic insights are providing pharmaceutical companies with many new insights into how to design specific inhibitors.

Dale Poulter, of the University of Utah, who reported on studies by him and his colleagues of how FTase binds the farnesyl molecule and the Ras protein, in preparation for enzymatically joining the two.

Samuel Graham, of the Merck Research Laboratories, who reported on

Contact: Dennis Meredith
Duke University

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