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Evidence for the presence of specific high affinity cytosolic binding sites for platelet-activating factor in human neutrophils.

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 x 10(-9) M for the cytosolic and 3.71 x 10(-9) M for the membrane fraction. The maximal number of binding sites estimated were 219 fmol/100 micrograms protein for the cytosol and 154 fmol/100 micrograms 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 x 10(-7) M and 5.7 x 10(-6) M, respectively. These data demonstrate clearly the role of intracellularly synthesized PAF as a second messenger in the receptor-mediated neutrophil activation.

journal_name

Biochem Biophys Res Commun

journal_title

Biochemical and biophysical research communications

authors

Svetlov S,Nigam S

doi

10.1006/bbrc.1993.1025

subject

Has Abstract

pub_date

1993-01-15 00:00:00

pages

162-6

issue

1

eissn

0006-291X

issn

1090-2104

pii

S0006-291X(83)71025-9

journal_volume

190

pub_type

杂志文章

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