Monoclonal antibody directed to MHC class I antigen (Bra23/9): characterization and utilization for study of antigen expression in differentiation of U 937 cell line.

The monoclonal antibody Bra23/9 (IgG2a) elicited by a non-T, non-B ALL cell line (REH), reacted in microscopic immunofluorescence, enzyme-linked immunoassay (ELISA), complement-dependent cytotoxicity tests and immunocytofluorometric measurements with hemopoietic cell lines and peripheral blood lymphocytes, monocytes and granulocytes from healthy donors in a pattern characteristic for MHC class I antigens. Immunoprecipitation of lactoperoxidase radioiodinated cell surface proteins and surface sialoglycoproteins radiolabeled by sodium metaperiodate/tritiated sodium borohydride technique confirmed the structure gp44,p12 (consisting of a 44 kDa glycopeptide linked with a nonglycosylated 12 kDa peptide) typical for MHC class I antigen(s) as a structure recognized by the Bra23/9 monoclonal antibody. The increase of MHC class I antigen density (immunofluorescence intensity) induced by a phorbol ester (TPA) in monoblast U 937 lymphoma cell line was observed by immunocytofluorometry as a predominant tendency in several TPA-induction experiments, where a certain variability among individual experiments in TPA-induced MHC class I antigen alterations was observed.