Secretion of phospholipase A1 by bone marrow-derived macrophages.

Bone marrow-derived macrophages contain phospholipase activity of the A1 and A2 types, active at acid or neutral pH and with different specificities for the fatty acid to be liberated. In contrast to this variety, only one single phospholipase could be detected in extracellular fluids of these cells. Surprisingly, this phospholipase was of the A1 type and active at about pH 8. It exhibited a restricted substrate specificity in that, of the various substrates tested, only phosphatidylcholine containing palmitic acid in position 2 was degraded. This total restriction was not detected with phosphatidylethanolamine substrates. In addition to phospholipase A1, extracellular fluids exhibited lipase activity. A modulation of enzyme secretion could not be achieved by lymphokines or phorbol esters. However, release could be blocked by treating cells with cycloheximide (5 micrograms/ml) or tunicamycin (0.5 micrograms/ml). Phospholipase A1 was also released by thioglycollate-induced peritoneal macrophages.