Formation of Amyloid-Like Substance from Beta-2-Microglobulin in vitro

Abstract

Although the pathogenesis has yet to be fully understood, beta 2-microglobulin (beta 2m) related amyloidosis is a frequent complication in long-term hemodialysis (HD) patients. In an attempt to clarify the association of two potential candidates with amyloidogenesis from beta 2m in HD patients, human urine-derived beta 2m solution alone or combined with glycosaminoglycans: hyaluronic acid, heparan sulfate, or serum amyloid P component (SAP) were dialyzed against physiological buffered solution (pH 7.4) using a microdialyzer in vitro for 72 h at 4 degrees C. This study demonstrates for the first time that SAP can play a crucial role in the formation of amyloid-like fibrils from beta 2m. This occurs by a direct influence on either the processing of a precursor protein, or protein folding, in vitro, by a short-period dialysis against a physiological buffered solution.