thers 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.
Proteases are important enzymes which, among other things, play a role in the development of cancer cells. The proteases in our bodies are active all the time. In connection with wound healing, the process of proteolysis is initiated to repair the damaged tissue.
Proteolysis is the molecular mechanism whereby a protease cleaves and activates the next protease, which then cleaves and activates a third protease, and so on. The mechanism is a kind of domino effect, whereby a single protease can issue a little signal to a whole string of proteases.
It is important to have balanced protease levels when they are out of balance and there is too much of them, things go wrong.
Researchers have produced models of mice with excessive levels of the proteases matriptase and prostasin, and those mice with too much protease develop a predisposition to skin cancer. The mice are used to study proteolysis.
Cancer does not necessarily develop in all cases where the mice have excessive protease levels, but when it specifically involves matriptase and prostasin, it does. Previous research has also shown that cancer patients have raised matriptase levels.
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