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
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