title: BP-3 alloantigen. A cell surface glycoprotein that marks early B lineage cells and mature myeloid lineage cells in mice.
abstract: To explore the cell surface molecules expressed on pre-B cells we have produced a panel of alloantibodies against transformed pre-B cells from BALB/c mice by immunizing a wild mouse, Mus spretus. One of these antibodies, BP-3, recognized glycoproteins of Mr 38,000 to 48,000 on pre-B cells transformed either by the Abelson murine leukemia virus or an erb B oncogene construct. Removal of N-linked oligosaccharides from the BP-3 Ag revealed a single core protein of Mr 32,000. The Ag was expressed by bone marrow cells in all but one (A/J) of the inbred mouse strains tested and in wild mice of biochemical groups Mus-1 and Mus-2. Analysis of the tissue distribution revealed expression of the BP-3 reactive molecule on normal pre-B and B cells in the bone marrow, 35% of B cells in the circulation, 30% of the B cells in the spleen, and less than or equal to 20% of B cells in lymph nodes, peritoneal cavity, and Peyer's patches. The subpopulation of BP-3+ B cells in bone marrow and peripheral tissues displayed an immature phenotype (IgM IgD +/- ). Examination of a panel of transformed B lineage cells confirmed the early stage-specific expression of the BP-3 alloantigen. In addition, a myeloid cell line and normal myeloid cells were found to express the BP-3 alloantigen. In contrast to B lineage cells, the level of BP-3 expression increased as a function of myeloid cell differentiation. Myeloid cells in the bone marrow expressed relatively little Ag, whereas circulating neutrophils and peritoneal macrophages expressed relatively high levels of the BP-3 alloantigen with Mr 38,000, 41,000, and 46,000. The data suggest that this variably glycosylated cell surface protein could play different roles in the differentiation of B lineage and myeloid lineage cells. The BP-3 alloantigen appears to be a useful marker for virgin B cells that have recently migrated from the bone marrow to the periphery.
authors.affiliation: Division of Developmental and Clinical Immunology, University of Alabama, Birmingham 35294.
authors.forename: K M
authors.initials: KM
authors.lastname: McNagny
authors.forename: P A
authors.initials: PA
authors.lastname: Cazenave
authors.forename: M D
authors.initials: MD
authors.lastname: Cooper
mesh_terms: D036541:ADP-ribosyl Cyclase; D000818:Animals; D000911:Antibodies, Monoclonal / Q000096:biosynthesis; D015703:Antigens, CD; D000944:Antigens, Differentiation, B-Lymphocyte / Q000302:isolation & purification*; D000951:Antigens, Neoplasm / Q000276:immunology / Q000302:isolation & purification; D000954:Antigens, Surface / Q000302:isolation & purification; D001402:B-Lymphocytes / Q000276:immunology* / Q000502:physiology; D014408:Biomarkers, Tumor / Q000302:isolation & purification; D001853:Bone Marrow / Q000276:immunology*; D002460:Cell Line; D058851:GPI-Linked Proteins; D006412:Hematopoietic Stem Cells / Q000276:immunology*; D007519:Isoantigens / Q000276:immunology / Q000302:isolation & purification*; D008562:Membrane Glycoproteins / Q000302:isolation & purification*; D051379:Mice; D008806:Mice, Inbred AKR; D008807:Mice, Inbred BALB C; D008809:Mice, Inbred C3H; D008810:Mice, Inbred C57BL; D008808:Mice, Inbred CBA; D008811:Mice, Inbred DBA; D008814:Mice, Inbred NZB; D009115:Muridae; D013045:Species Specificity; D014018:Tissue Distribution
chemical_list: D000911:Antibodies, Monoclonal; D015703:Antigens, CD; D000944:Antigens, Differentiation, B-Lymphocyte; D000951:Antigens, Neoplasm; D000954:Antigens, Surface; D014408:Biomarkers, Tumor; D058851:GPI-Linked Proteins; D007519:Isoantigens; D008562:Membrane Glycoproteins; D036541:ADP-ribosyl Cyclase; C087521:ADP-ribosyl cyclase 2