Beta 2-microglobulin is the main protein constituent of hemodialysis-r
elated amyloidosis. However, other proteins are present in amyloid dep
osits in addition to beta 2-microglobulin. We have studied the protein
constituents of amyloid deposits surgically removed from 15 dialysis
patients in renal replacement therapy. The proteins were characterized
by sodium dodecylsulfate polyacrylamide gel electrophoresis and two d
imensional gel electrophoresis (2D-PAGE). The identification of the pr
oteins was performed by immunological techniques (Western blotting, im
munohistology and electron microscopy with immunogold labelling). The
analyses showed the presence of globin chains, alpha 2-macroglobulin,
amyloid P component, albumin, hemopexin and lambda and kappa light cha
ins of immunoglobulins in amyloid deposits. 2D-PAGE confirmed that bet
a 2-microglobulin from amyloid deposits consisted of four or more isof
orms. Although the pathogenesis of dialysis-related amyloidosis is not
completely understood, it seems highly unlikely that modifications in
beta 2-microglobulin entirely explain the amyloid fibril formation. T
herefore, in the study of the pathogenesis of amyloidosis, it appears
important to take into account all the constituents of amyloid deposit
s. A possible role for the proteins reported here should not be neglec
ted and further studies aiming to precise their putative participation
could provide new insights in the understanding of the mechanisms ind
ucing amyloid fibril formation.