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European Biopharmaceutical Review

Proteolytic Enzymes as Therapeutic Targets

The regulation of protein secretion is central to the proper functioning of eukaryotic organisms. One mode of protein secretion is the generation of soluble fragments of membrane-bound proteins by limited proteolysis through the action of proteases termed secretases, or sheddases. In general, cleavage occurs close to the extracellular face of the membrane, releasing active protein. Proteins secreted in this fashion include some membrane receptors and receptor ligands, ectoenzymes and cell adhesion molecules. Since the proteins concerned are involved in pathophysiological processes, such as neurodegeneration, inflammation and oncogenesis, inhibitors of respective secretases are emerging as promising therapeutic drugs. This article will review a number of methods that have allowed molecular cloning of secretases and discuss different approaches to discovering specific secretase inhibitors.


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By Dr Urs Lüthi, Senior Scientist at ESBATech

Dr Urs Lüthi carried out his PhD studies at ESBATech under the supervision of Dr Alcide Barberis and has recently completed his dissertation on the subject of functional screening systems in yeast to identify secretases, targets of secretases and modulators of secretase activity. An essential part of his work focused on the development of the cellular assay for BACE activity that is further developed for small compound inhibitors screens.
He will continue to develop his expertise as a Senior Scientist with ESBATech and will be responsible for the development of similar cell-based assay systems. Urs' academic work was presented at several international conferences and published in peer-reviewed journals.

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Dr Urs Lüthi
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