Soluble immune complexes binding to human monocytes and polymorphonuclear leucocytes.
Soluble human serum albumin anti-albumin immune complexes (IC) have been shown to bind to freshly isolated human peripheral blood monocytes and polymorphonuclear leucocytes (PMN) in vitro. Binding sites on both cell types were saturable and specifically inhibited by heat aggregated IgG1 and IgG3 subclasses. PMN contained a greater number of binding sites than monocytes although the affinity was similar for both cell types. The enhanced binding of IC by both cell types observed after incubation at low pH (pH 6.0) was a consequence of increased affinity of the PMN binding site and an increase in the number of sites in monocytes. Binding of IC by both cell types was inhibited by normal human serum. Enhanced IC binding associated with enhanced affinity and number of sites was observed in PMN and monocytes preincubated in suspension with trypsin. However, monocytes exposed to trypsin while adherent to microexudate coated flasks demonstrated a marked increase in affinity without any change in the number of sites.
D000818:Animals; D000915:Antibody Affinity; D000936:Antigen-Antibody Complex / Q000276:immunology*; D001666:Binding Sites, Antibody; D002478:Cells, Cultured; D006801:Humans; D006863:Hydrogen-Ion Concentration; D007074:Immunoglobulin G / Q000276:immunology; D008297:Male; D009000:Monocytes / Q000276:immunology*; D009504:Neutrophils / Q000276:immunology*; D011817:Rabbits; D013997:Time Factors; D014357:Trypsin / Q000494:pharmacology
D000936:Antigen-Antibody Complex; D007074:Immunoglobulin G; D014357:Trypsin