Characterization of PAF receptors on human neutrophils using the specific antagonist, WEB 2086 Correlation between receptor binding and function

FEBS Letters

Ukena, Dieter¹  Dent, Gordon¹  Sybrecht, Gerhard²  Barnes, Peter¹  Chanez, Pascal¹ 

[1] Department of Thoracic Medicine, National Heart & Lung Institute, Dovehouse Street, London SW3 6LY, England;Abteilung für Pneumologie, Medizinische Universitätsklinik, Homburg (Saar), FRG

关键词: Platelet-activating factor;    Platelet-activating factor antagonist;    Platelet-activating factor receptor;    (Neutrophil);    BSA;    bovine serum albumin;    PAF;    plateletactivating factor;   

DOI  :  10.1016/0014-5793(89)80564-2

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

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.

【 授权许可】

Unknown