Acyltransferase-catalyzed transfer of arachidonic acid to lysophospholipids in rat pancreatic acini.

The conversion of 2-lysophospholipids into corresponding phospholipids via acyl-CoA acyltransferase was demonstrated in homogenates of rat pancreatic acini. Arachidonic acid was greatly preferred over stearic acid as the acyl donor. Lysophophosphatidylinositol and lysophosphatidylcholine acyltransferases were distributed in subcellular fractions of acinar homogenates with specific activity highest in the fractions known to contain secretory organelles and mitochondria. The distribution of lysophosphatidylinositol acyltransferase paralleled that of a mitochondrial marker (succinate cytochrome C reductase). These findings extend the evidence implicating arachidonate release and reincorporation into phospholipids as a link in the pathway that culminates in pancreatic secretion.