Degradation of red cell membrane phospholipids by sea anemone nematocyst venom

Abstract

Sea anemone ( Aiptasia pallida) nematocyst venom exhibited phospholipase A activity on red cell membrane phospholipids. Phospholipase A, purified from the venom, converted four of the major membrane phospholipids to their respective lysoderivatives, and to water-soluble phosphorus compounds. The production of these water-soluble derivatives appears to be due to the action of a lysolecithinase intrinsic to red cell membranes. Thus, the extent of membrane phospholipid hydrolysis by venom phospholipase A was determined either by direct measurements of the decrease in phospholipid content, or by adding the increase in lysophospholipids to the increase in water-soluble phosphorus compounds. These findings suggest that the underlying mechanism of nematocyst venom-induced hemolysis is due to the enzymatic action of venom phospholipase A on membrane phospholipids.