Characterization of PAF receptors on human neutrophils using the specific antagonist, WEB 2086 Correlation between receptor binding and function
Open Access
- 27 February 1989
- journal article
- Published by Wiley in FEBS Letters
- Vol. 244 (2) , 365-368
- https://doi.org/10.1016/0014-5793(89)80564-2
Abstract
The antagonism of PAF effects by WEB 2086 and the receptor binding of [3H]WEB 2086 were investigated in isolated human neutrophils. WEB 2086 inhibited PAF‐induced β‐glucuronidase release and [3H]WEB 2086 bound specifically to high‐affinity sites on the cells. Close concordance between affinity constants for WEB 2086 from functional and radioligand‐binding studies suggests that WEB 2086 interacts with the neutrophil PAF receptors and that [3H]WEB 2086 may be a useful ligand in investigation of these receptors.Keywords
This publication has 6 references indexed in Scilit:
- Radioligand binding of antagonists of platelet‐activating factor to intact human plateletsFEBS Letters, 1988
- PAF-acether specific binding sites: 1. quantitative SAR study of PAF-acether isosteresTrends in Pharmacological Sciences, 1986
- Binding and metabolism of platelet-activating factor by human neutrophils.Journal of Clinical Investigation, 1986
- Specific inhibition of PAF-acether-induced platelet activation by BN 52021 and comparison with the PAF-acether inhibitors kadsurenone and CV 3988European Journal of Pharmacology, 1986
- Specific receptor sites for 1-0-alkyl-2-0-acetyl-sn-glycero-3-phosphocholine (platelet activating factor) on rabbit platelet and guinea pig smooth muscle membranesBiochemistry, 1983
- Complement and immunoglobulins stimulate superoxide production by human leukocytes independently of phagocytosis.Journal of Clinical Investigation, 1975