A monoclonal antibody to sialophorin (CD43) induces homotypic adhesion and activation of human monocytes

Y. H. Nong, E. Remold-O'Donnell, T. W. LeBien, H. G. Remold

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Treatment of human monocytes for 24-48 h with the anti-CD43 mAb L10 caused five- to sevenfold stimulation of hydrogen peroxide-producing capacity, an established characteristic of activated monocyts. Peroxide-producing capacity induced by L10 antibody (1.6 ± 0.3 nmol H2O2/μg DNA/h) was comparable with that induced by IFN-γ (1.3 ± 0.4 H2O2/μg DNA/h), but appeared more rapidly (maximal at 24 h) than in the IFN-γ-treated monocytes (maximal at 48 h). Treatment of monocytes with L10 mAb also caused dramatic increase in aggregation (homotypic adhesion). Induction of monocyte aggregation by L10 mAb required incubation for 1-8 h in the presence of Mg2+ and was abrogated by TA-1, and anti-LFA-1-α mAb. Thus, L10-induced monocyte activation proceeds via a Mg2+ requiring aggregation stage involving LFA-1. Whereas the extent of monocyte aggregation induced by L10 mAb and by IFN-γ were comparable, the L10-induced aggregation occurred more rapidly (maximal at 8 h) than the IFN-γ induced aggregation (maximal at 24 h). The more rapid appearance of aggregation and increased hydrogen peroxide capacity in L10-treated monocytes suggests that the L10-induced activation pathway is independent of IFN-γ and IFN-γ-R dependent events. These findings suggest that the surface molecule CD43 is the receptor of an independent activation pathway that leads in lymphocytes to proliferation and in monocytes to activation.

Original languageEnglish (US)
Pages (from-to)259-267
Number of pages9
JournalJournal of Experimental Medicine
Issue number1
StatePublished - 1989


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