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IMAGE: To describe the structure of properdin oligomers, the researchers used two independent techniques. In the panels with a dark background, the properdin molecule is seen as a light triangular molecule. view more
Credit: Dennis Vestergaard Pedersen and Gregers Rom Andersen
After seven years of intense research, a research group from Aarhus University has succeeded - through an interdisciplinary collaboration - in understanding why a very extended structure is important for an essential protein from the human immune system. The new results offer new opportunities for adjusting the activity of the immune system both up and down. Stimulation is interesting in relation to cancer treatment, while inhibition of the immune system is used in treatment of autoimmune diseases.
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IMAGE: Researchers from Aarhus University have discovered that ITIH4 inhibits proteases in the innate immune system via an unknown mechanism. Figure: Rasmus Kjeldsen Jensen. view more
Credit: Rasmus Kjeldsen Jensen, Aarhus University
Although the protein ITIH4 is found in large amounts in the blood, its function has so far been unknown. By combining many different techniques, researchers from Aarhus University have discovered that ITIH4 inhibits proteases in the innate immune system via an unknown mechanism. The research results have just been published in the prestigious scientific journal
Science Advances.
Proteases are enzymes that cleave other proteins. Most often, proteases occur in cascade networks, where a particular event triggers a chain reaction in which several proteases cleave and thereby activate each other. Most well known is probably the coagulation cascade, which causes clotting of our blood when a vessel is punctured.