Abstract
In this study evidence for the presence of specific cytosolic platelet-activating factor (PAF) binding sites has been presented. The equilibrium dissociation constant (Kd) as determined by Scatchard analysis was 4.29 × 10−9 M for the cytosolic and 3.71 × 10−9 M for the membrane fraction. The maximal number of binding sites estimated were 219 fmol/100 μg protein for the cytosol and 154 fmol/100 μg protein for the membrane, respectively. The specific receptor binding of [3H]PAF to cytosol could be displaced by two potent specific PAF receptor antagonists, BN 50739 and WEB 2086, the equilibration inhibition constants (Ki) being 1.27 × 10−7 M and 5.7 × 10−6 M, respectively. These data demonstrate clearly the role of intracellularly synthesized PAF as a second messenger in the receptor-mediated neutrophil activation.
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