Evidence that C1q, a subcomponent of the first component of complement, is an Fc receptor of peritoneal and alveolar macrophages.

Guinea pig peritoneal macrophages were cultured for 24 h in the presence of two inhibitors of the biosynthesis of collagen-like molecules such as C1q : 10(-3) M 3,4-dehydroproline or 10(-4) M 2,2'-dipyridyl. Their Fc-receptor activity was measured by rosette formation, using sheep erythrocytes (E) coated with rabbit anti-sheep IgG (EAIgG). The Fc-receptor activity was decreased by 40 to 70% of control cultures depending on the amount of IgG on the E. The activity of a second receptor on the macrophages, mediating the binding of C3b coated E, was not altered by this treatment. Rat alveolar macrophages were depleted of their Fc-receptor activity by pronase treatment (1.5 mg/ml) in the presence of 2,2'-dipyridyl. After washing the cells, the EAIgG-binding activity was restored to about half of the initial level within 2 h. With 2,2'-dipyridyl also present during the second incubation, the re-expression of the Fc-receptor activity was suppressed further. Preincubation of guinea pig peritoneal macrophages with anti-C1q-F(ab')2 for 45 min at 37 degrees C caused a dose-dependent reduction of the Fc receptor activity, but not C3b receptor activity. These results support our hypothesis that C1q synthesized and secreted by macrophages serves as an Fc-receptor in the membrane during the secretion.