Cytochemical localization of adenylate cyclase in the three developmental forms of Trypanosoma cruzi

We used ultrastructural cytochemistry to localize adenylate cyclase activity in the three evolutive forms of Trypanosoma cruzi. We detected the enzyme by using adenylimidodiphosphate as substrate, prostaglandin E1 as enzyme stimulator, theophylline as inhibitor of adenosine 3'-5'-monophosphate phosphodiesterase, and either cerium chloride or lead nitrate as capture agent. Deposition of imidodiphosphate was stronger in trypomastigotes than in amastigotes and epimastigotes. Differences in the reaction product levels between the nonproliferative form and both proliferative ones are in accordance with our previous work that showed the involvement of adenylate cyclase on the control of T. cruzi's cycle.