Enzyme to stop lung cancer is targeted

A Yale-led research team has found that a fundamental cellular process can be interrupted to disable certain cancerous cells.

During the process of glycosylation, an enzyme called oligosaccha-ryltransferase (OST) helps transfer chains of saccharides to specific proteins to help those proteins fold correctly. Scientists assumed tinkering with the glycosylation pathway would automatically harm all cells.

Joseph N. Contessa, M.D., Ph.D., associate professor of therapeutic radiology and of pharmacology, and colleagues isolated an inhibitor called ngi-1 that disrupted glycosylation by targeting the OST enzyme. They found it stopped cell division in lung cancer cells with epidermal growth factor (EGFR) and fibroblast growth factor (FGFR) receptor mutations. Noncancerous cells exposed to the ngi-1 inhibitor were unaffected.

The study was published Oct. 3 in Nature Chemical Biology. “The EGF and FGF receptors have a lot of sugars on them,” Contessa says, “so disrupting glycosylation on a cell heavily dependent on those receptors is a very targeted approach.”


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