Identification and characterization of the human Pgp-1 glycoprotein.
Two monoclonal antibodies have been raised against human Pgp-1 by the immunization of mice with human fibroblasts. The human molecule, like the previously identified mouse counterpart, is an abundant membrane protein (Mr approximately 95 000) with a broad tissue distribution. Pgp-1 is phosphorylated, and phosphoamino acid analysis demonstrates that this occurs exclusively on serine residues. A major difference between the mouse and the human is that 50-60% of human thymocytes are Pgp-1+ compared to 5-10% of mouse thymocytes at an equivalent stage in development. Immunofluorescence studies of cryostat sections showed that the majority of human medullary thymocytes are strongly stained with Pgp-1-specific antibody, whereas the expression of Pgp-1 on cortical thymocytes is much more heterogeneous.
D000367:Age Factors; D000911:Antibodies, Monoclonal / Q000276:immunology*; D000954:Antigens, Surface / Q000276:immunology / Q000302:isolation & purification*; D005434:Flow Cytometry; D006023:Glycoproteins / Q000276:immunology / Q000302:isolation & purification; D006412:Hematopoietic Stem Cells / Q000276:immunology / Q000378:metabolism; D006801:Humans; D010446:Peptide Fragments / Q000032:analysis; D010750:Phosphoproteins / Q000276:immunology / Q000378:metabolism; D016201:Receptors, Lymphocyte Homing; D013950:Thymus Gland / Q000276:immunology; D014018:Tissue Distribution
D000911:Antibodies, Monoclonal; D000954:Antigens, Surface; D006023:Glycoproteins; D010446:Peptide Fragments; D010750:Phosphoproteins; D016201:Receptors, Lymphocyte Homing