Expression of the binding molecules for factor B and its fragment, Bb, of human complement on human monocytes after in vitro cultivation.
We have examined the expression of the binding molecules for Bb of human complement on the surface of resting and cultured human monocytes. Flow cytometry using biotinylated anti-B antibodies and phycoerythrin-avidin showed that although resting monocytes did not bind Bb significantly, monocytes cultivated for 24 h in the presence of fetal calf serum were capable of binding with Bb and its precursor B, but not with Ba fragment. The Bb-binding molecules were pronase-sensitive, suggesting that membrane proteins are associated with the Bb-binding molecules. In addition to human monocytes, liquid paraffin-induced guinea pig inflammatory macrophages were also found to express Bb-binding molecules on their surface. This implies that Bb receptor-like molecules become expressed during activation and differentiation of monocytes, just as observed with the C3d-receptor of monocytes.
Saeki
T
T
Department of Hygienic Chemistry, Faculty of Pharmaceutical Sciences, Hokkaido University, Sapporo, Japan.
Nagasawa
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S
D000818:Animals; D001665:Binding Sites; D051561:Complement C3 Convertase, Alternative Pathway; D003179:Complement C3b / Q000378:metabolism*; D011415:Complement Factor B / Q000378:metabolism*; D004792:Enzyme Precursors / Q000378:metabolism*; D005455:Fluorescent Antibody Technique; D006168:Guinea Pigs; D006801:Humans; D066298:In Vitro Techniques; D008264:Macrophages / Q000276:immunology / Q000378:metabolism; D009000:Monocytes / Q000276:immunology* / Q000378:metabolism; D010446:Peptide Fragments / Q000378:metabolism*; D011951:Receptors, Complement / Q000378:metabolism*
D004792:Enzyme Precursors; D010446:Peptide Fragments; D011951:Receptors, Complement; D003179:Complement C3b; D051561:Complement C3 Convertase, Alternative Pathway; D011415:Complement Factor B