title: Reticular cells in peripheral lymphoid tissues express the phosphatidylinositol-linked BP-3 antigen.
abstract: The murine BP-3 antigen was initially described as a variably glycosylated cell surface protein of Mr 38,000 to 48,000 on lymphoid and myeloid cells. In the present experiments we found that this antigen is released from the surface of pre-B cells and macrophages by treatment with phosphatidylinositol-specific phospholipase C (PI-PLC), suggesting a glycosyl-phosphatidylinositol (GPI) linkage with the plasma membrane. When the tissue distribution of the BP-3-reactive cells was examined by immunohistology, high levels of the antigen were observed on brush borders of the intestinal epithelial cells, within collecting tubules of the kidney and on a subpopulation of reticular cells located on lymph nodes. Peyer's patches and the white pulp areas of the spleen. In contrast, reticular cells located in the thymus, bone marrow and splenic red pulp did not express the BP-3 antigen. Ontogenic studies revealed that BP-3 was expressed by the reticular cells in peripheral lymphoid tissues in the neonatal period near the time of lymphocyte immigration into these organs. BP-3+ reticular cells were observed in the collapsed periarterial lymphatic sheaths of adult mice depleted of T and B cells by cyclophosphamide treatment and in mice with severe combined immunodeficiency (scid), indicating that development of this reticular network is lymphocyte independent. The BP-3 antigen on the splenic reticular cells was also GPI anchored but its glycosylation pattern differed from that of the BP-3 molecules on pre-B cells. A specific subpopulation of reticular cells is thus marked by the BP-3 antigen, and the distribution and biochemical properties of the molecule make it an attractive candidate for a role in lymphocyte-stromal interactions in the peripheral lymphoid tissues.
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: R P
authors.initials: RP
authors.lastname: Bucy
authors.forename: M D
authors.initials: MD
authors.lastname: Cooper
mesh_terms: D000375:Aging / Q000378:metabolism; D000818:Animals; D002465:Cell Movement / Q000276:immunology; D006017:Glycolipids / Q000032:analysis; D017261:Glycosylphosphatidylinositols; D007153:Immunologic Deficiency Syndromes / Q000473:pathology; D007519:Isoantigens / Q000032:analysis; D008198:Lymph Nodes / Q000166:cytology; D008221:Lymphoid Tissue / Q000737:chemistry / Q000166:cytology*; D008562:Membrane Glycoproteins / Q000032:analysis*; D051379:Mice; D008805:Mice, Inbred A; D008807:Mice, Inbred BALB C; D009928:Organ Specificity; D010581:Peyer's Patches / Q000166:cytology; D043265:Phosphatidylinositol Diacylglycerol-Lyase; D010716:Phosphatidylinositols / Q000032:analysis; D054801:Phosphoinositide Phospholipase C; D010727:Phosphoric Diester Hydrolases; D013154:Spleen / Q000166:cytology
chemical_list: D006017:Glycolipids; D017261:Glycosylphosphatidylinositols; D007519:Isoantigens; D008562:Membrane Glycoproteins; D010716:Phosphatidylinositols; D010727:Phosphoric Diester Hydrolases; D054801:Phosphoinositide Phospholipase C; D043265:Phosphatidylinositol Diacylglycerol-Lyase