Enhanced adhesion of oxidized mouse polymorphonuclear leukocytes to macrophages by a cell-surface sugar-dependent mechanism

Citation
M. Beppu et al., Enhanced adhesion of oxidized mouse polymorphonuclear leukocytes to macrophages by a cell-surface sugar-dependent mechanism, BIOL PHAR B, 24(1), 2001, pp. 19-26
Citations number
55
Language
INGLESE
art.tipo
Article
Categorie Soggetti
Pharmacology & Toxicology
Journal title
BIOLOGICAL & PHARMACEUTICAL BULLETIN
ISSN journal
0918-6158 → ACNP
Volume
24
Issue
1
Year of publication
2001
Pages
19 - 26
Database
ISI
SICI code
0918-6158(200101)24:1<19:EAOOMP>2.0.ZU;2-R
Abstract
Mouse thioglycollate-induced peritoneal macrophages effectively, in the abs ence of serum, recognized mouse polymorphonuclear leukocytes (PMNs) mildly oxidized with diamide, superoxide (hypoxanthine/xanthine oxidase) or t-buty lhydroperoxide, or modified with N-ethylmaleimide (NEM). The recognition re ached a maximum when PMNs were treated with each of the reagents at relativ ely low concentrations, and the recognition was decreased on treatment with reagents at higher concentrations. Glutathione depletion in the diamide-ox idized PMNs may cause enhanced adhesion to macrophages. Sialylated sugar ch ains attached to a peptide chain in glycophorin A and sialylated poly-N-ace tyllactosaminyl sugar chains in lactoferrin and band 3 glycoprotein effecti vely inhibited the increased adhesion of the diamide-oxidized PMNs. Enzymat ic removal of sialyl residues and the degradation of poly-N-acetyllactosami nyl sugar chains by pretreatment of PMNs with neuraminidase or endo-beta -g alactosidase, respectively, lost their increasing ability for macrophages a dhesion after oxidation with diamide, superoxide or t-butylhydroperoxide. C lustered sialylated poly-N-acetyllactosaminyl sugar chains on the cell surf ace may be involved in the increased adhesion of the oxidized PMNs to macro phages.