Human erythrocytes incubated with an iron catalyst ADP-chelated Fe3+ u
ndergo oxidative damage of the membrane including lipid peroxidation,
protein oxidation, and protein aggregation, and become susceptible to
recognition by human macrophages. Ln order to clarify the membrane com
ponents of macrophages responsible for the recognition of the oxidized
erythrocytes, binding of the oxidized cells to dot and Western blots
of solubilized membrane of macrophages was investigated. The oxidized
erythrocytes but not unoxidized cells bound to the dot blots. The bind
ing was effectively inhibited by saccharide chains of band 3, a major
glycoprotein of human erythrocytes, and lowered when the saccharide ch
ains of band 3 were removed from the cell surface by pretreatment of t
he cells with endo-beta-galactosidase which specifically cleaves the p
olylactosaminyl saccharide chains of band 3. The oxidized erythrocytes
bound to the membrane proteins of macrophages with molecular mass of
about 50, 80, and 120 kDa on Western blots depending on the saccharide
chains of band 3 on their surface. The results suggest that the oxida
tively damaged erythrocytes are specifically recognized by these prote
ins of macrophage membrane having saccharide binding ability.