ABSTRACT
Investigations into the mechanism of amyloidogenesis have been performed either by using in vitro systems to study fibril assembly of isolated and synthetic amyloidogenic polypeptides, or by examination of different amyloids in situ. In vitro studies frequently employ non-physiological conditions for fibrillogenesis and fail to study biological factors promoting amyloidogenesis, while analysis of in vivo systems are hampered by a lack of control over a large number of potential variables. A cell culture model would provide a bridge between these two systems, and a monocytic cell culture system that appears to recapitulate all the main features of AA-amyloidogenesis is described. It has also allowed to demonstrate that a synthetic peptide (27-mer), corresponding to the heparan sulfate (HS) binding site of Serum amyloid A 1.1 is a potent inhibitor of amyloidogenesis providing direct evidence for the role of HS in the disease process.
