Heterogeneity and mechanism of action of human natural killer lymphocytes: differential distribution of receptors for Helix pomatia haemagglutinin (HP receptors)

Scand J Immunol. 1979;10(2):109-18. doi: 10.1111/j.1365-3083.1979.tb03265.x.

Abstract

Neuraminidase-treated lymphocytes from the peripheral blood of normal human donors were fractionated on columns charged with Helix pomatia haemagglutinin (HP) coupled to Sepharose 4B. While lymphocytes lacking HP receptors (HP-) passed directly through the column (fraction I), lymphocytes with HP receptors (HP+) were subsequently eluted in two distinct fractions with two different concentrations of the competitive hapten N-acetyl-D-galactosamine (fraction II and III, respectively). The natural cytotoxicity of these lymphocytes to various tumour target cells (K562, T24, MANO, HCV29) was tested in a 51Cr release assay. Natural cytotoxicity was found in all three fractions recovered from the HP columns. In general, the cytotoxicity of the lymphocytes in fractions I and II was significantly enhanced over that of the unfractionated lymphocytes. Surface marker analysis and fractionation studies indicated that natural cytotoxicity in these target systems is exerted by both HP+ and HP- lymphocytes bearing Fc receptors for IgG. Since the HP receptor is considered to be a marker to T lymphocytes, the findings suggest that a significant fraction of these NK cells may be of T-cell lineage. The surface marker profiles of these NK cells are very similar to those of antibody-dependent K cells. Addition of Fab fragments of immunoadsorbent-purified rabbit antibodies to human immunoglobulin inhibited the natural cytotoxicity of HP-column-fractionated lymphocytes to various degrees, indicating that part but not all of it reflects antibody-dependent K-cell reactions. Since cytotoxicity in all three HP fractions was inhibitable in this way, the results suggest that immunoglobulin-dependent natural cytotoxicity may be displayed by both HP+ and HP- effector cells.

MeSH terms

  • Agglutinins / immunology*
  • Animals
  • Antibody-Dependent Cell Cytotoxicity*
  • Binding Sites, Antibody*
  • Cell Fractionation
  • Cell Separation
  • Helix, Snails
  • Hemagglutinins / immunology*
  • Humans
  • Immunoglobulin Fab Fragments
  • Immunoglobulin G
  • Killer Cells, Natural / immunology*
  • Neuraminidase / pharmacology
  • Rabbits
  • Receptors, Fc

Substances

  • Agglutinins
  • Hemagglutinins
  • Immunoglobulin Fab Fragments
  • Immunoglobulin G
  • Receptors, Fc
  • Neuraminidase