Specific binding sites for platelet activating factor in human lung tissues

Biochem Biophys Res Commun. 1985 Apr 30;128(2):972-9. doi: 10.1016/0006-291x(85)90142-1.

Abstract

Specific and saturable binding of [3H]-labeled 1-0-alkyl-2-0-acetyl-sn-glycero-3-phosphocholine (PAF) to membrane preparations of human lung tissues is demonstrated. The equilibrium dissociation constant (KD) was determined by Scatchard analysis to be 4.9 (+/- 1.7) X 10(-10)M and the maximal number of binding sites was estimated to be 140 (+/- 37) fmole/mg protein. The binding site is PAF specific and its selectivity toward PAF analogs is very similar to that in rabbit platelets. Two PAF receptor antagonists, kadsurenone and ginkgolide B, previously characterized in platelet systems, also displace the binding of [3H]-PAF to human lung homogenates. These data indicate that human lung tissues contain PAF specific receptors, and binding of PAF to these receptor sites may be the first step to initiate PAF-induced lung pathophysiology.

MeSH terms

  • Binding Sites
  • Humans
  • Kinetics
  • Lung / metabolism*
  • Mathematics
  • Platelet Activating Factor / metabolism*
  • Platelet Membrane Glycoproteins*
  • Receptors, Cell Surface / metabolism*
  • Receptors, G-Protein-Coupled*

Substances

  • Platelet Activating Factor
  • Platelet Membrane Glycoproteins
  • Receptors, Cell Surface
  • Receptors, G-Protein-Coupled
  • platelet activating factor receptor