DIFFERENTIATION OF C3B RECEPTORS ON HUMAN-LYMPHOCYTES, PHAGOCYTES, ERYTHROCYTES AND RENAL GLOMERULUS CELLS BY MONOCLONAL-ANTIBODIES

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  • 1 January 1982
    • journal article
    • research article
    • Vol. 45  (1) , 85-96
Abstract
C3b [complement component 3b] receptor protein was purified from human erythrocytes by 2 M KBr solubilization and affinity chromatography on C3-coated sepharose. This material served as antigen for raising monoclonal antibodies. To investigate the distribution and antigenetic relationship between the receptors for C3b on human erythrocytes, lymphoid and phagocytic cells, kidney cells, 3 monoclonal antibodies were selected which inhibited the binding of EAC14.degree.23b [sheep erythrocyte coated with antibody, Cl, C4, oxidized C2 and C3] to complement receptor-bearing cells. This could be shown for human erythrocytes by inhibiting the immune adherence reaction, for tonsil lymphocytes, Raji cells and guinea-pig spleen cells by inhibition of rosette formation of these cells with EAC14.degree.23b, and for human renal glomeruli by blocking of the adherence of EAC14.degree.23b to kidney sections. These monoclonal antibodies were not capable of inhibiting rosette formation of human granulocytes and monocytes with EAC14.degree.23b. The antibodies only interfered with the rosette formation, of EAC14.degree.23bi and EAC14.degree.23d with Raji cells and tonsil lymphocytes.sbd.if at all.sbd.at high concentrations; the rosette formation of Raji cells and tonsil lymphocytes with EAC14.degree.23b was influenced by supernatants of the selected clones up to a dilution of 1:103 to 1:105.

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