Trypanosoma rangeli: An alkaline ecto-phosphatase activity is involved with survival and growth of the parasite

Dos-Santos, André L.A.; Dick, Claudia F.; Silveira, Timotheo Souza; Fonseca-de-Souza, André Luiz; Meyer‐Fernandes, José Roberto

doi:10.1016/j.exppara.2013.08.014

Cited by 7 publications

(3 citation statements)

References 36 publications

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“…Levamizole, an alkaline phosphatase inhibitor, had no effect on ectophosphatase activity, corroborating the results showing lower ectophosphatase activity under alkaline pH conditions and ruling out the hypothesis of alkaline ecto-phosphatase activity (Dos-Santos et al, 2013).…”

Section: Discussionsupporting

confidence: 82%

Ectophosphatase activity in the triple‐negative breast cancer cell line MDA‐MB‐231

Lacerda-Abreu

Russo‐Abrahão

Aguiar

et al. 2020

Cell Biology International

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Breast cancer is one of the most common cancers in the female population worldwide, and its development is thought to be associated with genetic mutations that lead to uncontrolled and accelerated growth of breast cells. This abnormal behavior requires extra energy, and indeed, tumor cells display a rewired energy metabolism compared to normal breast cells. Inorganic phosphate (Pi) is a glycolytic substrate of glyceraldehyde‐3‐phosphate dehydrogenase and has an important role in cancer cell proliferation. For cells to obtain Pi, ectoenzymes in the plasma membrane with their catalytic site facing the extracellular environment can hydrolyze phosphorylated molecules, and this is an initial and possibly limiting step for the uptake of Pi by carriers that behave as adjuvants in the process of energy harvesting and thus partially contributes to tumor energy requirements. In this study, the activity of an ectophosphatase in MDA‐MB‐231 cells was biochemically characterized, and the results showed that the activity of this enzyme was higher in the acidic pH range and that the enzyme had a Km = 4.5 ± 0.5 mM para‐nitrophenylphosphate and a Vmax = 2280 ± 158 nM × h−1 × mg protein−1. In addition, classical acid phosphatase inhibitors, including sodium orthovanadate, decreased enzymatic activity. Sodium orthovanadate was able to inhibit ectophosphatase activity while also inhibiting cell proliferation, adhesion, and migration, which are important processes in tumor progression, especially in metastatic breast cancer MDA‐MB‐231 cells that have higher ectophosphatase activity than MCF‐7 and MCF‐10 breast cells.

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Section: Discussionsupporting

confidence: 82%

Ectophosphatase activity in the triple‐negative breast cancer cell line MDA‐MB‐231

Lacerda-Abreu

Russo‐Abrahão

Aguiar

et al. 2020

Cell Biology International

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“…Several ecto-enzymatic activities involved in the hydrolysis of phosphorylated substrates have been described in T. rangeli , including a Mg 2+ -dependent ecto-ATPase activity [57], [58] and an ecto-phosphatase activity capable of hydrolyzing β-GP [50], [59]. Table 1 shows the influence of several inhibitors on these activities.…”

Section: Resultsmentioning

confidence: 99%

“…Other ecto-enzymes have been detected and characterized on the outer surface of the plasma membrane of this parasite, including a Mg 2+ -dependent ecto-ATPase [57], [58] and an ecto-phosphatase that uses β-GP as a substrate [50], [59]. To rule out the participation of these ecto-enzymes in the hydrolysis of PPi, we determined the sensitivity of each activity to classical phosphatase and pyrophosphatase inhibitors.…”

Section: Discussionmentioning

confidence: 99%

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

et al. 2014

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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 MgCl2. In the presence of MgCl2, this activity was inhibited by millimolar concentrations of CaCl2. 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.

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Ectonucleotidase activity driven by acid ectophosphatase in luminal A MCF‐7 breast cancer cells

Lacerda‐Abreu,

Mendonça,

Nestal de Moraes

et al. 2024

Cell Biology International

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Ectophosphatases catalyse the hydrolysis of phosphorylated molecules, such as phospho‐amino acids, in the extracellular environment. Nevertheless, the hydrolysis of nucleotides in the extracellular environment is typically catalysed by ectonucleotidases. Studies have shown that acid ectophosphatase, or transmembrane‐prostatic acid phosphatase (TM‐PAP), a membrane‐bound splice variant of prostatic acid phosphatase, has ecto‐5′‐nucleotidase activity. Furthermore, it was demonstrated that ectophosphatase cannot hydrolyse ATP, ADP, or AMP in triple‐negative breast cancer cells. In contrast to previous findings in MDA‐MB‐231 cells, the ectophosphatase studied in the present work displayed a remarkable capacity to hydrolyse AMP in luminal A breast cancer cells (MCF‐7). We showed that AMP dose‐dependently inhibited p‐nitrophenylphosphate (p‐NPP) hydrolysis. The p‐NPP and AMP hydrolysis showed similar biochemical behaviours, such as increased hydrolysis under acidic conditions and comparable inhibition by NiCl2, ammonium molybdate, and sodium orthovanadate. In addition, this ectophosphatase with ectonucleotidase activity was essential for the release of adenosine and inorganic phosphate from phosphorylated molecules available in the extracellular microenvironment. This is the first study to show that prostatic acid phosphatase on the membrane surface of breast cancer cells (MCF‐7) is correlated with cell adhesion and migration.

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Trypanosoma rangeli: An alkaline ecto-phosphatase activity is involved with survival and growth of the parasite

Cited by 7 publications

References 36 publications

Ectophosphatase activity in the triple‐negative breast cancer cell line MDA‐MB‐231

Ectophosphatase activity in the triple‐negative breast cancer cell line MDA‐MB‐231

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

Ectonucleotidase activity driven by acid ectophosphatase in luminal A MCF‐7 breast cancer cells

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