Membrane expression and synthesis of p23,30 (HLA-DR antigen) by human peripheral blood monocytes.

The synthesis and expression of protein complexes of 23,000 and 30,00 dalton (p23,30) HLA-DR antigen, and of 44,000 and 12,000 dalton (p44,12) HLA-A,B antigen and beta 2-microglobulin was demonstrated on human peripheral blood monocytes and in cultures of purified, adherent monocytes. In indirect immunofluorescence assays, a gradation in the intensity of staining with rabbit anti-p23,30 serum was present but clearly p23,30-negative, actively phagocytic monocytes were not found. In contrast the fluorescence intensity of staining with a serum to p44,12 (HLA-A,B antigens and beta 2-microglobulin) was constant on all macrophages. Macrophage HLA-DR antigen was shown in SDS gels of immunoprecipitates of 35S-methionine-labeled, detergent-solubilized membrane proteins to be composed of 29,000 and 34,000 dalton, noncovalently linked chains, which form was indistinguishable from that of B lymphoblastoid cell line HLA-DR antigens. The rate of synthesis of HLA-DR antigen was about 17% of that of synthesis of HLA-A,B antigens in adherent macrophage populations. The variable expression of p23,30 on peripheral blood monocytes was consistent with the view of the existence of subsets of such monocyte populations. These findings were compared to studies by others of the variable expression of Ia antigens on human, murine and guinea pig monocytes populations.