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

Abstract:

:Mouse thioglycollate-induced peritoneal macrophages effectively, in the absence of serum, recognized mouse polymorphonuclear leukocytes (PMNs) mildly oxidized with diamide, superoxide (hypoxanthine/xanthine oxidase) or t-butyhydroperoxide, or modified with N-ethylmaleimide (NEM). The recognition reached a maximum when PMNs were treated wtih each of the reagents at relatively low concentrations, and the recognition was decreased on treatment with reagents at higher concentrations. Glutathione depletion in the diamide-oxidized PMNs may cause enhanced adhesion to macrophages. Sialylated sugar chains attached to a peptide chain in glycophorin A and sialylated poly-N-acetyllactosaminyl sugar chains in lactoferrin and band 3 glycoprotein effectively inhibited the increased adhesion of the diamide-oxidized PMNs. Enzymatic removal of sialyl residues and the degradation of poly-N-acetyllactosaminyl sugar chains by pretreatment of PMNs with neuraminidase or endo-beta-galactosidase, respectively, lost their increasing ability for macrophage adhesion after oxidation with diamide, superoxide or t-butylhydroperoxide. Clustered sialylated poly-N-acetyllactosaminyl sugar chains on the cell surface may be involved in the increased adhesion of the oxidized PMNs to macrophages.

journal_name

Biol Pharm Bull

authors

Beppu M,Yokoyama N,Motohashi M,Kikugawa K

doi

10.1248/bpb.24.19

subject

Has Abstract

pub_date

2001-01-01 00:00:00

pages

19-26

issue

1

eissn

0918-6158

issn

1347-5215

journal_volume

24

pub_type

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