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Molecular discovery could lead to effective cancer cure

A collaborative effort between scientists from University of Copenhagen and the National Institutes of Health signals a step on the path to designing a more effective cure for cancer by mapping out a previously unknown molecular mechanism.

Foto: Colourbox

Researchers from the University of Copenhagen and the National Institutes of Health have obtained ground-breaking new knowledge about proteases - important enzymes which, among other things, play a role in the development of cancer cells. The findings may be significant for the development of cancer drugs.

Proteases are important enzymes which are responsible for maintaining different types of tissues in the body while also being involved in a range of diseases, including cancer. Cancer cells can exploit an over-production of proteases to force their way into the body so they can quickly grow and create a space for themselves in which to spread.

“So far, we have been unable to treat cancer patients with drugs which can effectively stop cancer cells from spreading, but having now discovered that an important function of proteases has been overlooked, we have the possibility of designing new drugs,” says Stine Friis, a postdoc at the Department of Cellular and Molecular Medicine at the University of Copenhagen. She has spearheaded the new research in collaboration with the National Institutes of Health.

Outside the box

"So far, cancer drugs have primarily been shaped to stop the proteases from cleaving and thereby activating processes, but this is probably insufficient. Surprisingly, our studies show that proteases perform another function in addition to cleaving; they are also able to bind to one another, besides from cleaving, and kick-starting various cellular processes,” she adds.

Through knowing about this previously overseen but vital function of how proteases activate the cell’s signals, researchers hope to improve our understanding of how proteases operate in the body.

“Hopefully our new findings will inspire others to think outside the box, opening the doors to innovation with drugs aimed at regulating protease activity, such as anticancer drugs. The drugs we design today are developed to halt the cleaving process, but even though it is stopped, some proteases can apparently continue to transmit signals by binding to instead of cleaving one another. If we can stop the binding, we should be able to develop better drugs, which in the long term will bring us closer to developing successful cancer treatments. If you only understand how one half of an engine functions, it’s almost impossible to repair it,” says Stine Friis.

- translated by Martin Havtorn Petersen

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