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Tiny molecules have big potential as cancer drugs, Stanford researcher believes

n. If one of the molecules turns out to vanquish tumors but not their hosts, it could become one of the first drugs of its kind, he said. "Most cancer drugs are very toxic," he said. "There are very few rationally designed oncology drugs in use today that are made with a specific target in mind."

Designing an inhibitor requires knowing which protein to inhibit and what the protein does. Finding out the latter is a particularly difficult task in the case of cathepsins because of the nature of proteases, Bogyo said. "Proteases take other proteins and degrade them into little bits, and so it's hard to figure out what those proteins were doing," he said. "We're beginning by focusing on individual proteases, seeing what happens when you shut down a specific member of that family. And I think we're going to find that some of those proteases are more important than others for promoting things like tumor growth and angiogenesis."

The implications of finding the right inhibitor would reach far, Bogyo said, since cathepsins are associated with many different cancers and are involved in processes such as blood vessel formation and tumor growth critical to all tumors. "It suggests that anything that's aggressive and metastatic may involve these proteases and respond to an inhibitor," he said, adding that the inhibitor would likely be used in conjunction with other therapies.


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Contact: Mitzi Baker
mitzibaker@stanford.edu
650-725-2106
Stanford University Medical Center
24-Aug-2004


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