Concanavalin A stimulates phospholipid methylation and phosphatidylserine decarboxylation in rat mast cells.

Abstract

When histamine release from rat peritoneal mast cells is stimulated by concanavalin A, membrane phospholipids are methylated in the early stage of this process. Exogenously added phosphatidylserine enhances the concanavalin A-induced histamine release, and at the same time the lectin markedly stimulates the decarboxylation and methylation of phosphatidylserine. Within minutes after the addition of concanavalin A to rat mast cells, the newly methylated phospholipids begin to disappear and an increased formation of lysophosphatidylcholine is observed. When rat mast cells are treated with concanavalin A in the absence of Ca2+, phospholipid methylation is stimulated but no significant release of histamine is detected. The subsequent exposure of the pretreated cells to Ca2+ causes increased release of histamine and degradation of methylated phospholipids. The inhibition of either synthesis or degradation of methylated phospholipids results in the inhibition of histamine release. These observations suggest that the synthesis and degradation of methylated lipids are an intrinsic part of the biochemical mechanism that modulate histamine release from mast cells.