New discovery by EU-funded researchers could lead to improved treatment of allergies and asthma
Researchers working in two EU-funded research projects have unravelled the structure of a key enzyme that can trigger allergies and asthma. This breakthrough opens up the possibility of the development of new drugs for treating these and other conditions which are tailor-made for patients, making them more effective. The enzyme, termed LTC4 synthase, is part of the complex process that leads to the production of leukotrienes, which cause allergic symptoms, and motors the inflammatory reaction which causes asthma attacks. Some existing medicines block the effect of this enzyme, but only after the process has taken place. Thanks to these latest findings, published today in the leading scientific magazine Nature, scientists will now be able to tailor new molecules that block LTC4 before it can act. The two projects, named EICOSANOX and E-MeP, are headed by professors from Karolinska Institutet in Stockholm, and one, EICOSANOX, has one Nobel-Prize winning scientist in its team. Together, the two projects received EUR 20 million funding from the EU's Sixth Research Framework Programme.
EU-funded research projects
have unravelled the structure of a key enzyme.
Inflammatory diseases, such as rheumatoid arthritis, allergic rhinitis (hay fever), arteriosclerosis, inflammatory bowel disease and asthma, are serious endemic, disabling and sometimes fatal illnesses. They cause tremendous human suffering and are an increasing burden on European societies and health care systems. For some of these diseases, important underlying mechanisms and mediators have been identified. Thus, human bronchial asthma and hay fever may be caused by the over production of leukotrienes.
During an asthmatic attack, an inflammatory reaction develops in the respiratory system, which leads to narrowing of the airways, the gathering of fluid in the body, especially lungs and mucus secretion. Asthma medicines often aim at blocking the downstream effects of LTC4 synthase. However, there is a need for new pharmaceutical alternatives, since not all patients respond to the existing medicines.
The EU-funded teams have developed the highest ever resolution picture of the structure of LTC4 synthase. This greater clarity of the structure of the enzyme means that scientists now have a much better understanding of how it is formed and how it works. This knowledge can then be used to develop more effective therapies. Scientists from around the world have been working on unravelling the structure of LTC4 synthase and the results of two such projects are described in Nature this week. The European team, however, has managed to produce the highest resolution information, therefore providing a much better template for drug design.
These two projects are part of a range of research projects funded by the EU to understand proteins within the body that are important for medical knowledge and drug design. In addition to the EUR 20 million given to these two projects, a further EUR 24 million should be allocated before the beginning of 2008.
To restrict search results to articles in the Information Centre, i.e. this site, use this search box rather than the one at the top of the page.
After searching, you can expand the results to include the whole Research and Innovation web site, or another section of it, or all Europa, afterwards without searching again.
Please note that new content may take a few days to be indexed by the search engine and therefore to appear in the results.