Binding and Metabolism of Platelet-Activating Factor (PAF) by Isolated Rat Type II Pneumonocytes

The specific binding of platelet-activating factor (PAF) to isolated type II pneumonocytes from rat lung has been investigated employing an intact cell preparation. The dissociation constant (Kd) for the autacoid has been determined to be 0.46 × 10−9 M and approximately 3000 receptor sites per cell are present. In studies conducted on the metabolism of PAF in these cells, it was demonstrated that PAF is rapidly converted into 1-alkyl-2-acylglycerophosphocholine (alkyl-acyl GPC). After longer time intervals there was a substantial conversion of alkyl-acyl GPC into alkyl-acylglycerophosphoethanolamine (allkyl-acyl GPE). Both the alkyl-acyl GPC and alkyl-acyl GPE fractions were devoid of plasmalogens. The alkyl-acyl GPC fraction was further characterized and a distinct double peak could be visualized following thin-layer chromatography and the same lyso-compound was produced from both peaks following mild alkaline hydrolysis. By using appropriate standards it was concluded that the dual alkyl-acyl GPC peaks represent differences in the fatty acid present in the sn-2 position. One peak corresponds to the presence of saturated fatty acid in the sn-2 position and is probably due to the characteristic high capacity of the type II cells to produce disaturated glycerophospholipids.