Scientists from DZNE - the German Centre for Neurodegenerative Diseases and LMU, Ludwig-Maximilians-Universitaet Munich have discovered that a protein called the ADAM10 can inhibit the formation of beta-amyloid, the peptide that triggers Alzheimer’s.

Research showed that ADAM10 is a key molecule in Alzheimer's treatment, as it cuts the cuts the protein which beta-amyloid is formed, thus preventing the formation of beta-amyloid. The results of this study were published in the online edition of the EMBO Journal.

Dr. Stefan Lichtenthaler and his team observed that in the brains Alzheimer patients are big amounts of beta-amyloids, under the form of plaques. The disease is caracterized by memory loss problems, which are believed to be triggered by the precursors of these plaques which begin by causing nerve cell loss.
Having all this information, the best way of stopping the disease is to prevent the beta-amyloids formation.

Researchers from DZNE and LMU have identified an enzyme called alpha secretase, that splits the amyloid precursor protein (APP) without forming beta-amyloid. Previous research has shown that there are three different candidates for this function and now the team has been able to show that the only responsible for the specific separation is the enzyme ADAM10. They managed to do that thanks to RNA interference, a method they tested on mice.

“In ADAM10 we have identified a target molecule that plays a central role in the development of the molecular processes in Alzheimer’s disease. We know that ADAM10 is less active in Alzheimer patients,” Dr. Lichtenthaler says.

He adds that “It is possible that less ADAM10 activity could increase susceptibility to Alzheimer’s disease. If that is the case, stimulating ADAM10 could be an important mechanism for therapy. But our antibodies also open up new possibilities for diagnosing and preventing the disease.”

Doctors could use these antibodies to measure ADAM10 activity in spinal fluid and foresee which people have a high risk of developing Alzheimer’s disease.