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*
The Trudeau Institute, Saranac Lake, NY, 12983;
Department of Pathology, Boston, Brigham and Woman’s Hospital, MA 02115; and
Department of Cell Biology, Yale University School of Medicine, New Haven, CT 06520
Currently, the involvement of classical vs novel endocytic compartments in the phenomenon of B cell receptor (BCR)-mediated Ag processing is a matter of considerable debate. In murine B cells, class II vesicles (CIIV) represent a novel endocytic compartment involved in BCR-mediated Ag processing and class II peptide loading. Alternatively, in human B cells, the MHC class II-enriched compartment (MIIC) represents a lysosome (L)-like endocytic compartment that appears to be involved in this process. Presently, the relationship between CIIV, MIIC, and classical endosomes and L remains to be determined. Using density gradient centrifugation, a subcellular compartment morphologically and immunologically similar to human MIIC has been identified, isolated, and characterized in murine B cells. These MIIC-like vesicles represent a population of class II-positive late endosomes (LE) and are distinct from CIIV. MIIC-like LE are uniquely marked by the thiol protease cathepsin B, and along with mature L, appear to be the major repository of DM molecules in these cells. Importantly, both MIIC-like LE and CIIV isolated from Ag-pulsed B cells contain BCR-internalized Ag as well as antigenic peptide-class II complexes.
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