RECOGNITION OF POLY-N-ACETYLLACTOSAMINYL SACCHARIDE CHAINS ON IRON-OXIDIZED ERYTHROCYTES BY HUMAN MONOCYTIC LEUKEMIA-CELL LINE THP-1 DIFFERENTIATED INTO MACROPHAGES
M. Beppu et al., RECOGNITION OF POLY-N-ACETYLLACTOSAMINYL SACCHARIDE CHAINS ON IRON-OXIDIZED ERYTHROCYTES BY HUMAN MONOCYTIC LEUKEMIA-CELL LINE THP-1 DIFFERENTIATED INTO MACROPHAGES, Biological & pharmaceutical bulletin, 19(2), 1996, pp. 188-194
The cells of the human monocytic leukemia cell line THP-1 differentiat
ed into macrophages bound to human erythrocytes oxidized with adenosin
e 5'-diphosphate (ADP)-Fe3+ chelate (ADP/Fe3+) in the absence of serum
. The binding was prevented when the cells were treated with ADP/Fe3in the presence? of antioxidants, indicating that oxidation of the cel
ls is responsible for the increased susceptibility to the THP-1 cell b
inding. Galactose, fucose, mannose and mannan partially inhibited the
binding. Glycoproteins containing poly-N-acetyllactosaminyl saccharide
chains such as band 3 glycoprotein isolated from human erythrocyte me
mbrane and lactoferrin. and their oligosaccharides, strongly inhibited
the binding, On the other hand, glycoproteins with non-poly-N-acetyll
actosaminyl saccharide chains such as glycophorin A isolated from the
erythrocyte membrane fetuin and alpha(1)-acid glycoprotein, little or
partially inhibited the binding. The inhibitory activity of band 3 oli
gosaccharides and lactoferrin oligosaccharides was little affected by
treatment with endo-beta-galactosidase, which specifically cleaves pol
y-N-acetyllactosamine to shorter oligosaccharides. Removal of the nonr
educing terminal region of the saccharide chains of band 3 on the eyth
rocyte surface by treatment of the cells with endo-beta-galactosidase
resulted in a decrease in the susceptibility of the cells to the THP-1
cell binding. These results suggest that THP-1 cells which have been
differentiated into macrophages bind the oxidized erythrocytes primari
ly through the recognition of poly-N-acetyllactosaminyl saccharide cha
ins of band 3, and the site of the recognition exists in the nonreduci
ng terminal region of the saccharide chains, Clustering of band 3 mole
cules is proposed as a possible alteration of oxidized erythrocyte mem
brane which promotes the interaction of the saccharide receptor on THP
-1 cells with the saccharide chains of band 3 on erythrocytes.