ArticleParasitology research2004
A Mg-dependent ecto-ATPase is increased in the infective stages of Trypanosoma cruzi.
Article in Parasitology research, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.
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21 citing papers in PubMed, 58 citations in OpenAlex.
- Synthesis of new non-natural L-glycosidic flavonoid derivatives and their evaluation as inhibitors of Trypanosoma cruzi ecto-nucleoside triphosphate diphosphohydrolase 1 (TcNTPDase1).Purinergic signalling · 2024Article
- The Role of Inorganic Phosphate Transporters in Highly Proliferative Cells: From Protozoan Parasites to Cancer Cells.Membranes · 2022Review
- Overexpression ofInternational journal of molecular sciences · 2022Article
- E-NTPDases: Possible Roles on Host-Parasite Interactions and Therapeutic Opportunities.Frontiers in cellular and infection microbiology · 2021Review
- The Functioning of NaCells · 2020Review
- Knocking Down TcNTPDase-1 Gene ReducesFrontiers in microbiology · 2020Article
- Dependence ofJournal of parasitic diseases : official organ of the Indian Society for Parasitology · 2019Review
- Purinergic Antagonist Suramin Aggravates Myocarditis and Increases Mortality by Enhancing Parasitism, Inflammation, and Reactive Tissue Damage inOxidative medicine and cellular longevity · 2018Article
- Magnesium-Dependent Ecto-ATP Diphosphohydrolase Activity in Leishmania donovani.Current microbiology · 2016Article
- Purinergic signaling during Porphyromonas gingivalis infection.Biomedical journal · 2016Review
- Golgi-located NTPDase1 of Leishmania major is required for lipophosphoglycan elongation and normal lesion development whereas secreted NTPDase2 is dispensable for virulence.PLoS neglected tropical diseases · 2014Article
- Leishmania infantum ecto-nucleoside triphosphate diphosphohydrolase-2 is an apyrase involved in macrophage infection and expressed in infected dogs.PLoS neglected tropical diseases · 2014Article
- Nucleoside triphosphate diphosphohydrolase1 (TcNTPDase-1) gene expression is increased due to heat shock and in infective forms of Trypanosoma cruzi.Parasites & vectors · 2014Article
- Extracellular ATP acts as a damage-associated molecular pattern (DAMP) signal in plants.Frontiers in plant science · 2014Review
- Ecto-nucleotidase activities of promastigotes from Leishmania (Viannia) braziliensis relates to parasite infectivity and disease clinical outcome.PLoS neglected tropical diseases · 2012Article
- The P2X(7) receptor and intracellular pathogens: a continuing struggle.Purinergic signalling · 2009Article
- Influence of Ecto-nucleoside triphosphate diphosphohydrolase activity on Trypanosoma cruzi infectivity and virulence.PLoS neglected tropical diseases · 2009Article
- Possible effects of microbial ecto-nucleoside triphosphate diphosphohydrolases on host-pathogen interactions.Microbiology and molecular biology reviews : MMBR · 2008Review
- Enzymatic properties of an ecto-nucleoside triphosphate diphosphohydrolase from Legionella pneumophila: substrate specificity and requirement for virulence.The Journal of biological chemistry · 2008Article
- OppA, the ecto-ATPase of Mycoplasma hominis induces ATP release and cell death in HeLa cells.BMC microbiology · 2008Article
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9 authors at 1 institution in 1 country.
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Abstract
In this work, we describe the ability of living epimastigotes of Trypanosoma cruzi to hydrolyze extracellular ATP. In these intact parasites, there was a low level of ATP hydrolysis in the absence of any divalent metal (2.42 +/- 0.31 nmol Pi/h x 10(8) cells). ATP hydrolysis was stimulated by MgCl2, and the Mg-dependent ecto-ATPase activity was 27.15 +/- 2.91 nmol Pi/h x 10(8) cells. The addition of MgCl2 to the extracellular medium increased the ecto-ATPase activity in a dose-dependent manner. This stimulatory activity was also observed when MgCl2 was replaced by MnCl2, but not by CaCl2 or SrCl2. The apparent Km for Mg-ATP2- was 0.61 mM, and free Mg2+ did not increase the ecto-ATPase activity. This ecto-ATPase activity was insensitive to the inhibitors of other ATPase and phosphatase activities. To confirm that this Mg-dependent ATPase was an ecto-ATPase, we used an impermeant inhibitor, DIDS (4, 4'.diisothiocyanostylbene 2'-2'-disulfonic acid) as well as suramin, an antagonist of P2 purinoreceptors and inhibitor of some ecto-ATPases. These two reagents inhibited the Mg2+-dependent ATPase activity in a dose-dependent manner. A comparison among the Mg2+-ecto-ATPase activities of the three forms of T. cruzi showed that the noninfective epimastigotes were less efficient at hydrolyzing ATP than the infective trypomastigote and amastigote stages.
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