Calcium mobilization by arachidonic acid in trypanosomatids

A recent report (Eintracht J, Maathai R, Mellors A, Ruben L. Calcium entry in Trypanosoma brucei is regulated by phospholipase A(2) and arachidonic acid, Biochem J 1998;336:659-66) provided evidence that calcium entry in Trypanosoma brucei bloodstream trypomastigotes is regulated via a signaling pathway involving phospholipase A(2)-mediated generation of arachidonic acid and stimulation of a plasma membrane-located calcium channel. Here we show that Ca2+ influx in T. brucei procyclic trypomastigotes, Leishmania donovani promastigotes and T. cruzi amastigotes was also stimulated in a dose-dependent manner (50-400 nM) by the amphiphilic peptide melittin. This effect was blocked by the phospholipase A(2) inhibitor 3-(4-octadecyl)-benzoylacrylic acid. The unsaturated fatty add arachidonic acid, in the range of 10-75 mu M, induced Ca2+ entry by a mechanism sensitive to LaCl3. However, both melittin and arachidonic acid induced an increase in [Ca2+](i) in T. brucei procyclic trypomastigotes incubated in Ca2+-free medium implying Ca2+ mobilization from intracellular stores. This hypothesis was supported by experiments showing that arachidonic acid promoted Ca2+ release from the acidocalcisomes of these cells. The results showing changes in mitochondrial membrane potential. release of acridine orange and Ca2+ from the acidocalcisomes and Ca2+ transport across the plasma membrane suggest that in addition to the possible stimulation of a Ca2+ channel-mediated process, arachidonic acid, in the range of concentrations used here: have other nonspecific effects on the trypanosomatids membranes. (C) 2000 Elsevier Science B.V. All rights reserved.105226127