Characterization of an oligopeptide chemoattractant receptor on human blood monocytes using a new radioligand

Blood. 1984 Mar;63(3):588-92.


The study of chemoattractant receptors on human monocytes had been limited by the lack of a radioligand suitable for use with the small numbers of cells routinely available from human donors. A new synthetic oligopeptide radioligand f[35S]met-leu-phe, with a higher specific radioactivity than was available with the tritiated compound, was used to characterize a chemoattractant receptor on freshly isolated human blood monocytes. These cells bind f[35S]met-leu-phe with a dissociation constant (KD) of 30.2 +/- 5.6 nM and contain 84,000 +/- 11,300 receptors per cell. f[35S]met-leu-phe does not bind specifically to blood lymphocytes. The specificity of the oligopeptide receptor on monocytes is indistinguishable from the oligopeptide chemoattractant receptor on human polymorphonuclear leukocytes. Using f[35S]met-leu-phe, it will now be feasible to study the chemotactic peptide receptor on small numbers of partially purified peripheral blood monocytes from patients with defects of immune function.

Publication types

  • Comparative Study
  • Research Support, U.S. Gov't, P.H.S.

MeSH terms

  • Animals
  • Binding, Competitive
  • Guinea Pigs
  • Humans
  • Monocytes / metabolism*
  • N-Formylmethionine Leucyl-Phenylalanine / metabolism
  • Neutrophils / metabolism
  • Oligopeptides / blood*
  • Radioligand Assay*
  • Receptors, Cell Surface / analysis*
  • Receptors, Formyl Peptide
  • Sulfur Radioisotopes
  • Tritium


  • Oligopeptides
  • Receptors, Cell Surface
  • Receptors, Formyl Peptide
  • Sulfur Radioisotopes
  • Tritium
  • N-Formylmethionine Leucyl-Phenylalanine