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In this study, we performed the molecular and biochemical characterization of an ecto-enzyme present in  Trypanosoma rangeli  that is involved with the hydrolysis of extracellular inorganic pyrophosphate. PCR analysis identified a putative proton-pyrophosphatase (H + -PPase) in the epimastigote forms of  T. rangeli . This protein was recognized with Western blot and flow cytometry analysis using an antibody against the H + -PPase of  Arabidopsis thaliana . Immunofluorescence microscopy confirmed that this protein is located in the plasma membrane of  T. rangeli . Biochemical assays revealed that the optimum pH for the ecto-PPase activity was 7.5, as previously demonstrated for other organisms. Sodium fluoride (NaF) and aminomethylenediphosphonate (AMDP) were able to inhibit approximately 75% and 90% of the ecto-PPase activity, respectively. This ecto-PPase activity was stimulated in a dose-dependent manner by MgCl 2 . In the presence of MgCl 2 , this activity was inhibited by millimolar concentrations of CaCl 2 . The ecto-PPase activity of  T. rangeli  decreased with increasing cell proliferation  in vitro , thereby suggesting a role for this enzyme in the acquisition of inorganic phosphate (Pi). Moreover, this activity was modulated by the extracellular concentration of Pi and increased approximately two-fold when the cells were maintained in culture medium depleted of Pi. All of these results confirmed the occurrence of an ecto-PPase located in the plasma membrane of  T. rangeli  that possibly plays an important role in phosphate metabolism of this protozoan.

Identification and Characterization of an Ecto-Pyrophosphatase Activity in Intact Epimastigotes of Trypanosoma rangeli