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Related Experiment Videos

Ectonucleotide diphosphohydrolase activity in Crithidia deanei.

Adriana dos Passos Lemos1, Ana Acacia de Sá Pinheiro, Márcia de Berrêdo-Pinho

  • 1Departamento de Bioquímica Médica, ICB, Universidade Federal do Rio de Janeiro, Cidade Universitária, Ilha do Fundão, 21941-590, Rio de Janeiro, RJ, Brazil.

Parasitology Research
|September 5, 2002
PubMed
Summary
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Living Crithidia deanei cells possess Mg(2+)-dependent ecto-ATPase activity, crucial for extracellular ATP hydrolysis. This enzyme is specific for ATP and located on the cell surface, unaffected by common inhibitors.

Area of Science:

  • Biochemistry
  • Cell Biology
  • Parasitology

Background:

  • Extracellular ATP (adenosine triphosphate) serves as a signaling molecule.
  • Ecto-ATPases are enzymes located on the cell surface that hydrolyze extracellular ATP.
  • Understanding ecto-ATPases is important for various biological processes, including cell signaling and parasite-host interactions.

Purpose of the Study:

  • To investigate the presence and characteristics of ecto-ATPase activity in the protozoan parasite Crithidia deanei.
  • To determine the substrate specificity and kinetic properties of the identified ecto-ATPase.
  • To confirm the cell surface localization and distinguish it from other ATPases and phosphatases.

Main Methods:

  • Measurement of ATP hydrolysis in intact Crithidia deanei cells under varying conditions (pH, divalent metal ions, substrate concentration).

Related Experiment Videos

  • Enzyme inhibition studies using specific ecto-ATPase inhibitors and general ATPase/phosphatase inhibitors.
  • Cytochemical analysis to confirm the cell surface localization of the ATP-hydrolyzing activity.

    • Main Results:

    • Crithidia deanei cells exhibit Mg(2+)-dependent ecto-ATPase activity, with optimal activity observed in the presence of MgCl(2).
    • ATP was the preferred substrate, with significantly lower hydrolysis rates for other nucleotides like ITP, GTP, UTP, and CTP.
    • The enzyme's activity was insensitive to common inhibitors of other ATPases and phosphatases but was inhibited by suramin and 4,4'-diisothiocyanostylbene 2,2'-disulfonic acid, confirming its ecto-nature and cell surface localization.

    Conclusions:

    • Crithidia deanei possesses a distinct Mg(2+)-dependent ecto-ATPase located on its cell surface.
    • This ecto-ATPase plays a role in the hydrolysis of extracellular ATP, potentially influencing the parasite's environment and interactions.
    • The enzyme's specificity and localization provide insights into its function in the biology of Crithidia deanei.