Why do amyloid diseases strike different tissues?
[excerpt] Researchers at The Scripps Research Institute are reporting the results of a recent study that addresses why different tissues in the human body vary in their susceptibility to “amyloid” diseases, which include Alzheimer’s disease and a cluster of ailments called the familial amyloidoses. The familial amyloidoses, on which the researchers focused their study, are caused by various mutations to a human protein called transthyretin (TTR). These mutations render transthyretin unstable and predisposed to misfolding from a normal, safe structure into dangerous, sticky ones that glom together and form microscopic fibrils, which then cluster to form larger amyloid plaques that deposit in peripheral nerves, organs, and sometimes in the central nervous system. Strangely, some TTR mutations cause the fibrils to target the heart, others cause the fibrils to form in the peripheral nervous system, and still others cause the fibrils to form in the gut or in the brain. In the latest issue o