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A new mechanism for reversible proteasome inhibition
Date:12/13/2010

What makes cancer cells so dangerous is that they grow in an unregulated way and proliferate much faster than other cells. The proteasome, a large protein complex, plays a key role in this process: By breaking down used proteins for recycling, it clears the way for the next cycle. New hope was spawned several years ago with the discovery that inhibiting proteasomes can be used as a means to put the brakes on cell growth. In the mean time, the first drug using this approach, Bortezomib, generates revenues in excess of one billion U.S. dollars per year. However, it also inhibits other important proteins and thus sets off a host of severe side effects. Hence, there is a worldwide search for alternatives.

A variant of the proteasome, the immuno-proteasome, is a leading actor in another vital process: the immune reaction. The production of human insulin in genetically modified bacteria is a boon for diabetes patients. But calculating required doses and injecting insulin on a daily basis is a considerable burden. The transplantation of intact insulin-producing islet cells from pigs could be a solution, but the immune reaction stands in the way. If physicians were able to curb the immuno-proteasome temporarily, they could possibly get the rejection reaction under control.

In both cases, targeting the intervention as specifically as possible is essential to minimizing the damage caused by side effects. Besides Bortezomib two other proteasome inhibitors Carfilzomib and Salinosporamide A, derived from a poison produced by a marine bacterium are already in the human clinical trial stage. In earlier research, Professor Groll's team succeeded in explaining the mechanism of action of both substances. They follow the same principle, which is considerably more specific than Bortezomib in binding at the desired location in the proteasome and thus produce significantly fewer side effects. Yet, when they take effect, they destroy the proteasomes irreversibly
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Contact: Andreas Battenberg
battenberg@zv.tum.de
49-892-891-0510
Technische Universitaet Muenchen
Source:Eurekalert  

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A new mechanism for reversible proteasome inhibition
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