Guest Lecture: Prof. Dr. Beate Kehrel

Prof. Beate Kehrel

(Department of Anesthesiology, Intensive Care and Pain Medicine, UKM, DE)

Misfolded proteins – role in inflammation and thrombosis!

Abstract:

So-called misfolded, amyloid-like proteins are known from neurodegeneration, but abnormalities in the process of well-defined 3-dimensional structure adoption of proteins have far further reaching consequences for human health and especially also for thrombosis. The ability to form amyloid-like structure is a generic property of polypeptides, and can be shown on proteins with complete different primary structures like ox-LDL, fibrin, thrombospondin-1, HOCl-modified proteins, vWF under shear stress, advanced glycation end products modified proteins and many others. Misfolded proteins can be found in neutrophil extracellular nets, linking inflammation with thrombosis. Some, maybe even all, oligomeric fibril precursors activate platelets, interact with the kallikrein pathway, interact with fibrinolysis and influence endothelial cell barriers.