title: Recognition of poly-N-acetyllactosaminyl saccharide chains on iron-oxidized erythrocytes by human monocytic leukemia cell line THP-1 differentiated into macrophages.
abstract: The cells of the human monocytic leukemia cell line THP-1 differentiated into macrophages bound to human erythrocytes oxidized with adenosine 5'-diphosphate (ADP)-Fe3+ chelate (ADP/Fe3+) in the absence of serum. The binding was prevented when the cells were treated with ADP/Fe3+ in the presence of antioxidants, indicating that oxidation of the cells is responsible for the increased susceptibility to the THP-1 cell binding. 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 membrane and lactoferrin, and their oligosaccharides, strongly inhibited the binding. On the other hand, glycoproteins with non-poly-N-acetyllactosaminyl 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 oligosaccharides and lactoferrin oligosaccharides was little affected by treatment with endo-beta-galactosidase, which specifically cleaves poly-N-acetyllactosamine to shorter oligosaccharides. Removal of the nonreducing terminal region of the saccharide chains of band 3 on the erythrocyte 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 primarily through the recognition of poly-N-acetyllactosaminyl saccharide chains of band 3, and the site of the recognition exists in the nonreducing terminal region of the saccharide chains. Clustering of band 3 molecules is proposed as a possible alteration of oxidized erythrocyte membrane which promotes the interaction of the saccharide receptor on THP-1 cells with the saccharide chains of band 3 on erythrocytes.
authors.affiliation: School of Pharmacy, Tokyo University of Pharmacy and Life Science, Japan.
authors.forename: M
authors.initials: M
authors.lastname: Beppu
authors.forename: S
authors.initials: S
authors.lastname: Eda
authors.forename: M
authors.initials: M
authors.lastname: Fujimaki
authors.forename: E
authors.initials: E
authors.lastname: Hishiyama
authors.forename: K
authors.initials: K
authors.lastname: Kikugawa
mesh_terms: D000244:Adenosine Diphosphate / Q000494:pharmacology; D001457:Anion Exchange Protein 1, Erythrocyte / Q000378:metabolism*; D004912:Erythrocytes / Q000378:metabolism*; D006801:Humans; D007501:Iron / Q000494:pharmacology*; D007781:Lactoferrin / Q000378:metabolism; D007951:Leukemia, Myeloid / Q000378:metabolism*; D008264:Macrophages / Q000378:metabolism*; D010084:Oxidation-Reduction; D010587:Phagocytosis; D011134:Polysaccharides / Q000378:metabolism*; D014407:Tumor Cells, Cultured
chemical_list: D001457:Anion Exchange Protein 1, Erythrocyte; D011134:Polysaccharides; D000244:Adenosine Diphosphate; C037199:poly-N-acetyllactosamine; D007501:Iron; D007781:Lactoferrin