ABSTRACT
The formation of amyloid fibrils from soluble polypeptide chains represents a fundamental biochemical process in the initiation and progression of the various amyloid diseases. These fibrils occur in tissues in association with a range of chemically heterogeneous substances that includes glycosaminoglycans, proteins, such as SAP, and lipids. The lipids possess a typical pattern that is rich in sphingolipids and cholesterol. The high content of unsaturated molecular species point out against degradation processes that could give raise to the lipid pattern. An improved understanding of lipids and their fatty acid composition in amyloid deposits represents a prerequisite for addressing their possible involvement in amyloid diseases. The chapter analyzes the molecular species of membrane lipid components of 3 human AA and 6 AL amyloid deposits that had been purified from the surrounding tissues by the method described by Pras.
