Identification and characterization of the human Pgp-1 glycoprotein

Immunogenetics. 1986;23(5):326-32. doi: 10.1007/BF00398797.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Age Factors
  • Antibodies, Monoclonal / immunology*
  • Antigens, Surface / immunology
  • Antigens, Surface / isolation & purification*
  • Flow Cytometry
  • Glycoproteins / immunology
  • Glycoproteins / isolation & purification
  • Hematopoietic Stem Cells / immunology
  • Hematopoietic Stem Cells / metabolism
  • Humans
  • Peptide Fragments / analysis
  • Phosphoproteins / immunology
  • Phosphoproteins / metabolism
  • Receptors, Lymphocyte Homing
  • Thymus Gland / immunology
  • Tissue Distribution

Substances

  • Antibodies, Monoclonal
  • Antigens, Surface
  • Glycoproteins
  • Peptide Fragments
  • Phosphoproteins
  • Receptors, Lymphocyte Homing