Abstract
Abstract
We have compared and contrasted the binding of Agg IgM and heavily sensitized EAB (IgM) complexes to the Fcμ receptor of normal and neoplastic human lymphocytes. Agg IgM binds uniformly to the entire Smlg+ B cell population yet normal lymphocytes require culture in order to achieve binding of EAB complexes to a subset of Smlg+ B cells. In blocking studies IgM complexes and IgM aggregates appear to detect the same receptor and with both reagents binding is influenced by the presence of Mg2+ but not Ca2+ and is inhibited by EDTA.
The percentage of cells binding EAB was highest in normal B lymphocyte fractions enriched for C'3 + cells (CRL+). EAB binding to cells in the CRL- fractions was negligible even though CRL- fractions contained cells which were Smlg+C3 -. EAB bound only to neoplastic chronic lymphocytic leukemia cells (CLL) that expressed a high percentage of C3 + cells. Clones lacking a C3 receptor failed to bind EAB. Thus, the binding of EAB complexes to B lymphocytes appears to be associated principally with a subset that expresses a C3 receptor whereas IgM aggregates bind to the entire Smlg+ B cell population.
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