Selective inhibitor can target specific enzyme that promotes cancer

Molecule designed to arrest tumor growth and spread

A selective molecule able to target specific enzymes that help spread cancer may stop the development of some tumors, according to research presented in the July 19 edition of the Journal of the American Chemical Society, published by the world's largest scientific society.

The molecule is able to selectively inhibit gelatinases, enzymes involved in the growth and spread of cancerous tumors, according to Shahriar Mobashery, Ph.D., who headed the research team at Wayne State University in Detroit. It represents the first success in designing a molecule that can specifically target the enzymes that helps tumors to spread. Potential applications include treatment of tumors found in breast and prostate cancers, he said. Based on further research, the inhibitor also may apply to other cancers and inflammations.

Gelatinases are part of a family of proteins known as matrix metalloproteinases, or MMPs, which are responsible for tissue growth, among other things, in plants and animals. Examples of MMP activity range from the healing process after you get a paper cut to the growth of a fetus inside the womb. Cancerous tumors, however, use MMPs to supply themselves with the blood needed for survival and to aid the spread of tumor cells throughout the body.

Since gelatinases help supply blood to tumors, the inhibitor is designed to prevent the blood flow without stopping the normal functions of other MMPs, Mobashery said. The current research is still in the pre-clinical testing stage, meaning much more testing is needed to determine a delivery system and dosage of any possible drug.

Because MMPs are necessary to many functions in the human body, stopping the actions of a select few that have harmful effects has been the goal of many research teams. Other attempts at creating similar drugs have failed because they have not able to target a specific enzyme, Mobashery said.

"We have show

Contact: Beverly Hassell
American Chemical Society

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