The association of H-2 antigens and EAC receptors on the surface of peritoneal cells.
The exposure of murine peritoneal cells to anti-H-2 sera results in a diminished expression of H-2 antigen on the cell surface. Concomitant with this "H-2 modulation" the capacity of macrophages to bind sheep red blood cells coated with antibody and complement (EAC) was markedly diminished. In contrast, there was no change in the capacity of modulated macrophages to bind sheep red blood cells coated with antibody alone (EA). Antibodies to K end H-2 specificities were more effective in reducing the binding of EAC than antibodies to D end H-2 specificities. Exposure of peritoneal cells to O or Ly antisera had no effect on the formation of EAC rosettes. Exposure of peritoneal cells to anti-H-2 sera, under conditions which would not allow modulation of H-2 antigens, also prevented the reduction of EAC binding. Thus, the EAC receptors and H-2 antigenic specificities seem to be closely related on the surface of peritoneal cells, but constitute distinct cell surface structures. Preliminary evidence indicates that vinblastine, a microtubule depolymerizing agent, may disrupt the close association of EAC receptors and H-2 antigens. It is suggested that the association of EAC receptors and K end H-2 determinants on the membrane of macrophages may have implications for the regulation of the immune response by H-2-linked Ir genes.
D000818:Animals; D000906:Antibodies; D000918:Antibody Specificity; D001202:Ascitic Fluid / Q000166:cytology; D001665:Binding Sites; D003165:Complement System Proteins; D004912:Erythrocytes / Q000276:immunology*; D006649:Histocompatibility Antigens; D008264:Macrophages / Q000276:immunology*; D051379:Mice; D008815:Mice, Inbred Strains; D013499:Surface Properties
D000906:Antibodies; D006649:Histocompatibility Antigens; D003165:Complement System Proteins