Germ line origin and somatic mutations determine the target tissues in systemic AL-amyloidosis.

ABSTRACT:

Background

Amyloid is insoluble aggregated proteins deposited in the extra cellular space. About 25 different proteins are known to form amyloid in vivo and are associated with severe diseases such as Alzheimer's disease, prion diseases and type-2 diabetes. Light chain (AL) -amyloidosis is unique among amyloid diseases in that the fibril protein, a monoclonal immunoglobulin light chain, varies between individuals and that no two AL-proteins with identical primary structures have been described to date. The variability in tissue distribution of amyloid deposits is considerably larger in systemic AL-amyloidosis than in any other form of amyloidosis. The reason for this variation is believed to be based on the differences in properties of the amyloidogenic immunoglobulin light chain.

SUBMITTER: Enqvist S 

PROVIDER: S-EPMC1989140 | biostudies-literature | 2007 Oct

REPOSITORIES: biostudies-literature