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New molecular method reveals ‘conversations’ between proteins in cells

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30.10.2006

By further refining a molecular method they previously pioneered, researchers at Uppsala University have managed to uncover interactions between protein molecules in human cells. The method, described in the latest issue of the scientific journal Nature Methods, opens entirely new potential for understanding the role of proteins in various diseases.

 

Proteins build up the body’s cells and tissues, and knowledge of the human genome has entailed that scientists today know all the proteins our bodies can generate. It is known that many pathologies can be tied to changes in proteins, so it is important for us to increase our knowledge of what proteins bind to each other, how they work together in cells, and how these processes impact various disturbances.


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“With this new method we can see how individual proteins interact directly in cells, which has not been possible until now. In the past scientists have largely studied how much of a protein is present in various tissues, but now we can study how they function as well,” says researcher Ola Söderberg, a member of the team that carried out the study within the framework of the team’s research project on molecular tools.

The method is a further elaboration of the so-called proximity ligation test that was recently developed by the same research group. Proximity ligation means that proteins shown to be present bring about the formation of DNA strings that can be detected effectively and with a high degree of sensitivity. With the new modification, it is now possible to show just where in a cell or tissue sample the interacting proteins are to be found. Even individual protein molecules can be singled out.

“The method may be of great importance to scientists in their understanding of cell processes and ultimately may lead to more accurate examinations of tissue sample in diseases and to very early diagnosis,” says Professor Ulf Landegren, who directs the research team.

Anneli Waara | Source: alphagalileo
Further information: www.nature.com/nmeth/journal/vaop/ncurrent/index.html

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