Abstract
By means of two-dimensional polyacrylamide gel electrophoresis and Western blotting, it was demonstrated that most of the β2-microglobulin (β2-MG) forming amyloid fibrils which were isolated from the patients with dialysis related amyloidosis exhibited a more acidic pl value than normal β2-MG. Acidic β2-MG but not normal β2-MG was brown in color and fluoresced. lmmunochemical studies revealed that acidic β2-MG reacted with anti-AGE (advanced glycation end products) antibody and also with the antibody against an Amadori product. Purified AGE-modified β2-MG enhanced direct migration of human monocytes, but normal β2-MG did not enhance any migratory activity. AGE-modified β2-MG but not normal β2-MG, increased the secretion of IL-1β and TNF-α from macrophages.
AGE-modified β2-MG is a dominant constituent of the amyloid deposits and a major pathogenetic component in dialysis related amyloidosis.
