Abstract
Human monocytes constitutively express the intermediate-affinity interleukin-2 receptor (IL2R) p75, while freshly isolated monocytes lack the low-affinity IL2R p55 (Tac antigen, CD25). Lipopolysaccharide (LPS) upregulates expression of p75 and effectively induces surface expression of CD25 on human monocytes within 18 h, as detected by two-colour FACS analysis on 59.5 +/- 7.6% of cells. ...
Abstract
Human monocytes constitutively express the intermediate-affinity interleukin-2 receptor (IL2R) p75, while freshly isolated monocytes lack the low-affinity IL2R p55 (Tac antigen, CD25). Lipopolysaccharide (LPS) upregulates expression of p75 and effectively induces surface expression of CD25 on human monocytes within 18 h, as detected by two-colour FACS analysis on 59.5 +/- 7.6% of cells. IL2-binding studies using biotinylated IL2 reveal the presence of a functional high-affinity receptor on LPS-activated monocytes. Soluble CD25 (sCD25) is not released into supernatants of elutriation-purified monocytes cultured for 24 h with 100 ng/ml LPS. When these monocytes are cultured for up to 7 days in the presence of serum to induce differentiation into macrophages, increasing amounts of sCD25 can be measured in the 24-h supernatants induced with LPS (173 +/- 86 U/ml at day 7), whereas the percentage of CD25+ cells (14.8 +/- 14.1% at day 7) is significantly lower than in monocytes. Thus, the cell surface expression and release of CD25 is differentially regulated in activated monocytes and macrophages.
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