Structure-Activity of Three Phospholipid Analogues Towards Inhibition of Phospholipase A2 in Macrophages

Author: Letourneux Y.   Bourass J.   Boucrot P.   Elkihel L.   Petit J.Y.  

Publisher: Academic Press

ISSN: 1043-6618

Source: Pharmacological Research, Vol.35, Iss.1, 1997-01, pp. : 73-78

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Abstract

At concentrations 1-20 gm M in culture medium of rat peritoneal macrophages which were stimulated with ionophore A23187, the phospholipid analogues 1-decyl-2-octyl-glycero- phosphocholine and 1-dodecyl-2-octanamido-2-deoxy glycerophosphocholine were found more potent inhibitors than 1-octyl-2-octylthio-2-deoxy glycerophosphocholine to lower the phospholipase A 2 activities. The inhibitory effect was measured by [ 3 H] eicosatetraenoic acid ([ 3 H]20:4) release in macrophages and extracellular fluids and synthesis of [ 3 H] eicosanoids after incubation of macrophages with traces of the molecular species of lecithin 1-octadecanoyl-2-[ 3 H] eicosatetraenoyl glycerophosphocholine. The three phospholipid analogues developed higher inhibitory effects than mepacrine, dexamethasone or bromophenacyl bromide, at corresponding concentrations in medium.

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