MAJOR INVOLVEMENT OF CATHEPSIN-B IN THE INTRACELLULAR PROTEOLYTIC PROCESSING OF EXOGENOUS IGGS IN U937 CELLS

Monoclonal antibodies used for diagnostic and therapeutic purposes behave as antigens when injected into patients. They are recognized by T cells in a processed form and in a major histocompatibility complex class II restricted fashion. Monoclonal murine IgG2a were used as a model to analyse the early phase of antigen processing in U937 cells. IgG2a prebound to cell surface Fc receptors were rapidly internalized in the cells. During internalization, they were proteolysed with a time-dependent intracellular accumulation of 26, 25, 24, 22 and 14 kDa fragments. Comparison of in vitro IgG2a proteolysis by U937 subcellular fractions or by purified cathepsin B and their intracellular processing indicated that a major cathepsin B like protease is responsible for IgG2a intracellular processing in endo-lysosomal compartments of U937 cells.