WP 2 Dissection of the amyloid deposits
When Rudolf Virchow first described amyloid in the 19th century he used the greek term for starch “amylum” to describe what he believed was a starch-like (i.e. “amyloid”) substance. He came to this conclusion since tissue samples laden with amyloid stained bluish after they were treated with iodine and changed into violet after the superimposition of sulphuric acid. This reaction can also be observed when applied to starch and sugar. We now know that amyloid is a complex, non-random mixture of proteins, sugars (gylcosaminoglycans) and lipids. The hallmark of amyloid is the formation of protein aggregates arranged in a cross--sheet structure. Within the last 40 years more than 25 different proteins were identified that are able to form amyloid. Each of these proteins stands for at least one specific type of amyloid disease. Amyloid is not a single disease entity but a heterogeneous group of diseases. The formation of amyloid in tissues and organs ultimately disrupts organ function, i.e. amyloidosis in its closer sense, and can be life threatening. While the protein component is the hallmark of amyloid, the glycosaminoglycan- and lipid- components of amyloid also contribute to its pathology and pathogenesis.
Workpackage No. 2 of the EURAMY-project aims to dissect the complex nature of amyloid by identifying the various components of amyloid with far more modern techniques Rudolf Virchow had at his hands. The nature of amyloid is more complicated and deciphering the complex interactions between sugars, lipids and the protein moiety of amyloid hopefully will lead to the development of novel “disease-specific” drugs.