Endogenous aggregates of amyloidogenic cystatin C variant are removed by THP-1 cells in vitro and induce differentiation and a proinflammatory response.

A mutation in the human cystatin C gene leads to familial cerebral amyloid angiopathy. This disease is known as "hereditary cerebral hemorrhage with amyloidosis-Icelandic type" or "hereditary cystatin C amyloid angiopathy." The mutant cystatin C protein forms aggregates and amyloid, within the central nervous system almost exclusively in connection with the vascular system.

Isolation of amyloid by solubilization in water.

Amyloid fibrils are highly insoluble in neutral aqueous media of regular ionic strengths making solubilization a difficult task that normally calls for extremely harsh treatment. This is among the reasons for the routine employment of synthetic proteins in amyloid research, where the amylogenic components are needed. Here we describe a process for solubilizing amyloid in pure water that we adopted from a method developed by Mordechai Pras and associates.