Table of Contents Author Guidelines Submit a Manuscript
Journal of Parasitology Research
Volume 2011, Article ID 479146, 7 pages
http://dx.doi.org/10.1155/2011/479146
Review Article

Possible Roles of Ectophosphatases in Host-Parasite Interactions

1Instituto de Bioquímica Médica, Universidade Federal do Rio de Janeiro, CCS, Bloco H, Cidade Universitária, Ilha do Fundão, 21941-902 Rio de Janeiro, RJ, Brazil
2Instituto Nacional de Ciência e Tecnologia de Biologia Estrutural e Bioimagem (INCTBEB), CCS, Bloco H, Cidade Universitária, 21941-902 Rio de Janeiro, RJ, Brazil
3Instituto de Microbiologia Professor Paulo de Góes, Universidade Federal do Rio de Janeiro, CCS, Bloco H, Cidade Universitária, Ilha do Fundão, 21941-902 Rio de Janeiro, RJ, Brazil

Received 22 November 2010; Revised 7 February 2011; Accepted 1 March 2011

Academic Editor: Barbara Papadopoulou

Copyright © 2011 Marta T. Gomes et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. C. J. Oliver and S. Shenolikar, “Physiologic importance of protein phosphatase inhibitors,” Frontiers in Bioscience, vol. 3, pp. D961–D972, 1998. View at Google Scholar · View at Scopus
  2. P. Cohen, “The origins of protein phosphorylation,” Nature Cell Biology, vol. 4, no. 5, pp. E127–E130, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  3. T. Hunter, “Protein kinases and phosphatases: the yin and yang of protein phosphorylation and signaling,” Cell, vol. 80, no. 2, pp. 225–236, 1995. View at Google Scholar · View at Scopus
  4. M. Parsons, E. A. Worthey, P. N. Ward, and J. C. Mottram, “Comparative analysis of the kinomes of three pathogenic trypanosomatids: Leishmania major, Trypanosoma brucei and Trypanosoma cruzi,” BMC Genomics, vol. 6, pp. 127–145, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  5. R. Brenchley, H. Tariq, H. McElhinney et al., “The TriTryp phosphatome: analysis of the protein phosphatase catalytic domains,” BMC Genomics, vol. 8, pp. 434–455, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  6. M. J. M. Alves and W. Colli, “Trypanosoma cruzi: adhesion to the host cell and intracellular survival,” IUBMB Life, vol. 59, no. 4-5, pp. 274–279, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  7. J. R. Meyer-Fernandes, “Ecto-ATPases in protozoa parasites: looking for a function,” Parasitology International, vol. 51, no. 3, pp. 299–303, 2002. View at Publisher · View at Google Scholar · View at Scopus
  8. J. R. Meyer-Fernandes, D. Cosentino-Gomes, D. P. Vieira, and A. H. Lopes, “Ecto-nucleoside triphosphate diphosphohydrolase activities in trypanosomatids: possible roles in infection, virulence and purine recycling,” The Open Parasitology Journal, vol. 4, pp. 116–119, 2010. View at Google Scholar
  9. B. Szöör, “Trypanosomatid protein phosphatases,” Molecular and Biochemical Parasitology, vol. 173, pp. 53–63, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  10. A. V. Andreeva and M. A. Kutuzov, “Protozoan protein tyrosine phosphatases,” International Journal for Parasitology, vol. 38, no. 11, pp. 1279–1295, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  11. E. E. D. Almeida-Amaral, R. Belmont-Firpo, M. A. Vannier-Santos, and J. R. Meyer-Fernandes, “Leishmania amazonensis: characterization of an ecto-phosphatase activity,” Experimental Parasitology, vol. 114, no. 4, pp. 334–340, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  12. S. A. O. Gomes, A. L. Fonseca-de-Souza, B. A. Silva et al., “Trypanosoma rangeli: differential expression of cell surface polypeptides and ecto-phosphatase activity in short and long epimastigote forms,” Experimental Parasitology, vol. 112, no. 4, pp. 253–262, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  13. A. L. Fonseca-de-Souza, C. F. Dick, A. L. A. dos Santos, and J. R. Meyer-Fernandes, “A Mg2+-dependent ecto-phosphatase activity on the external surface of Trypanosoma rangeli modulated by exogenous inorganic phosphate,” Acta Tropica, vol. 107, no. 2, pp. 153–158, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  14. A. L. Fonseca-de-Souza, C. F. Dick, A. L. A. dos Santos, F. V. Fonseca, and J. R. Meyer-Fernandes, “Trypanosoma rangeli: a possible role for ecto-phosphatase activity on cell proliferation,” Experimental Parasitology, vol. 122, no. 3, pp. 242–246, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  15. C. F. Dick, A. L. A. dos-Santos, A. L. Fonseca-de-Souza, J. Rocha-Ferreira, and J. R. Meyer-Fernandes, “Trypanosoma rangeli: differential expression of ecto-phosphatase activities in response to inorganic phosphate starvation,” Experimental Parasitology, vol. 124, no. 4, pp. 386–393, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  16. A. T. Remaley, D. B. Kuhns, and R. E. Basford, “Leishmanial phosphatase blocks neutrophil O-2 production,” The Journal of Biological Chemistry, vol. 259, no. 18, pp. 11173–11175, 1984. View at Google Scholar · View at Scopus
  17. D. S. Alviano, L. F. Kneipp, A. H. Lopes et al., “Differentiation of Fonsecaea pedrosoi mycelial forms into sclerotic cells is induced by platelet-activating factor,” Research in Microbiology, vol. 154, no. 10, pp. 689–695, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  18. T. Furuya, L. I. Zhong, J. R. Meyer-Fernandes, H. G. Lu, S. N. J. Moreno, and R. Docampo, “Ecto-protein tyrosine phosphatase activity in Trypanosoma cruzi infective stages,” Molecular and Biochemical Parasitology, vol. 92, no. 2, pp. 339–348, 1998. View at Publisher · View at Google Scholar · View at Scopus
  19. T. Kiffer-Moreira, A. A. D. S. Pinheiro, W. S. Alviano et al., “An ectophosphatase activity in Candida parapsilosis influences the interaction of fungi with epithelial cells,” FEMS Yeast Research, vol. 7, no. 4, pp. 621–628, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  20. M. B. Portela, L. F. Kneipp, I. P. Ribeiro De Souza et al., “Ectophosphatase activity in Candida albicans influences fungal adhesion: study between HIV-positive and HIV-negative isolates,” Oral Diseases, vol. 16, no. 5, pp. 431–437, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  21. E. Touati, E. Dassa, J. Dassa, and P. L. Boquet, “Acid phosphatase (pH2.5) of Escherichia coli: regulatory characteristics,” in Microorganisms, A. Torriani- Gorini, F. G. Rothman, S. Silver, A. Wright, and E. Yagil, Eds., pp. 31–40, ASM Press, Washington, DC, USA, 1987. View at Google Scholar
  22. L. F. Kneipp, M. L. Rodrigues, C. Holandino et al., “Ectophosphatase activity in conidial forms of Fonsecaea pedrosoi is modulated by exogenous phosphate and mediates fungal adhesion to epithelial cells,” Microbiology, vol. 150, pp. 3355–3362, 2004. View at Google Scholar
  23. I. Collopy-Junior, F. F. Esteves, L. Nimrichter, M. L. Rodrigues, C. S. Alviano, and J. R. Meyer-Fernandes, “An ectophosphatase activity in Cryptococcus neoformans,” FEMS Yeast Research, vol. 6, no. 7, pp. 1010–1017, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  24. A. Martiny, M. A. Vannier-Santos, V. M. Borges et al., “Leishmania-induced tyrosine phosphorylation in the host macrophage and its implication to infection,” European Journal of Cell Biology, vol. 71, no. 2, pp. 206–215, 1996. View at Google Scholar · View at Scopus
  25. J. M. Jadin and J. Creemers, “The role of excretion of acid phosphatase in Trypanosoma brucei and T. cruzi,” Transactions of the Royal Society of Tropical Medicine and Hygiene, vol. 66, no. 1, pp. 8–9, 1972. View at Google Scholar · View at Scopus
  26. L. O. Andrade and N. W. Andrews, “Opinion: the Trypanosoma cruzi-host-cell interplay: location, invasion, retention,” Nature Reviews Microbiology, vol. 3, no. 10, pp. 819–823, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  27. J. A. Atwood, D. B. Weatherly, T. A. Minning et al., “Microbiology: the Trypanosoma cruzi proteome,” Science, vol. 309, no. 5733, pp. 473–476, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  28. J. McLaughlin, “The association of distinct acid phosphatases with the flagella pocket and surface membrane fractions obtained from bloodstream forms of Trypanosoma rhodesiense,” Molecular and Cellular Biochemistry, vol. 70, no. 2, pp. 177–184, 1986. View at Publisher · View at Google Scholar · View at Scopus
  29. O. M. Tosomba, T. H. T. Coetzer, and J. D. Lonsdale-Eccles, “Localisation of acid phosphatase activity on the surface of bloodstream forms of Trypanosoma congolense,” Experimental Parasitology, vol. 84, no. 3, pp. 429–438, 1996. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  30. E. C. Fernandes, J. R. Meyer-Fernandes, M. A. C. Silva-Neto, and A. E. Vercesi, “Trypanosoma brucei: ecto-phosphatase activity present on the surface of intact procyclic forms,” Zeitschrift fur Naturforschung Section C—Journal of Biosciences, vol. 52, no. 5-6, pp. 351–358, 1997. View at Google Scholar · View at Scopus
  31. N. Bakalara, X. Santarelli, C. Davis, and T. Baltz, “Purification, cloning, and characterization of an acidic ectoprotein phosphatase differentially expressed in the infectious bloodstream form of Trypanosoma brucei,” The Journal of Biological Chemistry, vol. 275, no. 12, pp. 8863–8871, 2000. View at Publisher · View at Google Scholar · View at Scopus
  32. J. R. Meyer-Fernandes, M. A. Da Silva-Neto, M. Dos Santos Soares, E. Fernandas, A. E. Vercesi, and M. M. de Oliveira, “Ecto-phosphatase activities on the cell surface of the amastigote forms of Trypanosoma cruzi,” Zeitschrift fur Naturforschung—Section C Journal of Biosciences, vol. 54, no. 11, pp. 977–984, 1999. View at Google Scholar · View at Scopus
  33. D. Cosentino-Gomes, T. Russo-Abrahão, A. L. Fonseca-de-Souza, C. R. Ferreira, A. Galina, and J. R. Meyer-Fernandes, “Modulation of Trypanosoma rangeli ecto-phosphatase activity by hydrogen peroxide,” Free Radical Biology and Medicine, vol. 47, no. 2, pp. 152–158, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  34. N. Bakalara, A. Seyfang, C. Davis, and T. Baltz, “Characterization of a life-cycle-stage-regulated membrane protein tyrosine phosphatase in Trypanosoma brucei,” European Journal of Biochemistry, vol. 234, no. 3, pp. 871–877, 1995. View at Google Scholar · View at Scopus
  35. P. M. L. Dutra, C. O. Rodrigues, J. B. Jesus, A. H. C. S. Lopes, T. Souto-Padrón, and J. R. Meyer-Fernandes, “A novel ecto-phosphatase activity of herpetomonas muscarum muscarum inhibited by platelet-activating factor,” Biochemical and Biophysical Research Communications, vol. 253, no. 1, pp. 164–169, 1998. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  36. P. M. L. Dutra, C. O. Rodrigues, A. Romeiro et al., “Characterization of ectophosphatase activities in trypanosomatid parasites of plants,” Phytopathology, vol. 90, no. 9, pp. 1032–1038, 2000. View at Google Scholar · View at Scopus
  37. P. M. L. Dutra, F. A. Dias, M. A. A. Santos et al., “Secreted phosphatase activities in trypanosomatid parasites of plants modulated by platelet-activating factor,” Phytopathology, vol. 91, no. 4, pp. 408–414, 2001. View at Google Scholar · View at Scopus
  38. M. M. Aguirre-García, J. Cerbón, and P. Talamás-Rohana, “Purification and properties of an acid phosphatase from Entamoeba histolytica HM-1:IMSS,” International Journal for Parasitology, vol. 30, no. 5, pp. 585–591, 2000. View at Publisher · View at Google Scholar · View at Scopus
  39. J. N. Amazonas, D. Cosentino-Gomes, A. Werneck-Lacerda et al., “Giardia lamblia: characterization of ecto-phosphatase activities,” Experimental Parasitology, vol. 121, no. 1, pp. 15–21, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  40. J. De Jesus, T. Podlyska, A. Hampshire, C. Lopes, M. Vannier-Santos, and J. Meyer-Fernandes, “Characterization of an ecto-phosphatase activity in the human parasite Trichomonas vaginalis,” Parasitology Research, vol. 88, no. 11, pp. 991–997, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  41. A. M. Shakarian, M. B. Joshi, E. Ghedin, and D. M. Dwyer, “Molecular dissection of the functional domains of a unique, tartrate-resistant, surface membrane acid phosphatase in the primitive human pathogen Leishmania donovani,” The Journal of Biological Chemistry, vol. 277, no. 20, pp. 17994–18001, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  42. M. M. Aguirre-García, A. R. Escalona-Montaño, N. Bakalara, A. Pérez-Torres, L. Gutiérrez-Kobeh, and I. Becker, “Leishmania major: detection of membrane-bound protein tyrosine phosphatase,” Parasitology, vol. 132, no. 5, pp. 641–649, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  43. E. C. Fernandes, J. M. Granjeiro, E. M. Taga, J. R. Meyer-Fernandes, and H. Aoyama, “Phosphatase activity characterization on the surface of intact bloodstream forms of Trypanosoma brucei,” FEMS Microbiology Letters, vol. 220, no. 2, pp. 197–206, 2003. View at Publisher · View at Google Scholar · View at Scopus
  44. E. C. Fernandes, J. M. Granjeiro, H. Aoyama, F. V. Fonseca, J. R. Meyer-Fernandes, and A. E. Vercesi, “A metallo phosphatase activity present on the surface of Trypanosoma brucei procyclic forms,” Veterinary Parasitology, vol. 118, no. 1-2, pp. 19–28, 2003. View at Publisher · View at Google Scholar · View at Scopus
  45. B. Menz, G. Winter, T. Ilg, F. Lottspeich, and P. Overath, “Purification and characterization of a membrane-bound acid phosphatase of Leishmania mexicana,” Molecular and Biochemical Parasitology, vol. 47, no. 1, pp. 101–108, 1991. View at Publisher · View at Google Scholar · View at Scopus
  46. M. Wiese, O. Berger, Y. D. Stierhof, M. Wolfram, M. Fuchs, and P. Overath, “Gene cloning and cellular localization of a membrane-bound acid phosphatase of Leishmania mexicana,” Molecular and Biochemical Parasitology, vol. 82, no. 2, pp. 153–165, 1996. View at Publisher · View at Google Scholar · View at Scopus
  47. M. Engstler, F. Weise, K. Bopp et al., “The membrane-bound histidine acid phosphatase TbMBAP1 is essential for endocytosis and membrane recycling in Trypanosoma brucei,” Journal of Cell Science, vol. 118, no. 10, pp. 2105–2118, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  48. P. M. L. Dutra, L. C. Couto, A. H. C. S. Lopes, and J. R. Meyer-Fernandes, “Characterization of ecto-phosphatase activities of Trypanosoma cruzi: a comparative study between Colombiana and Y strains,” Acta Tropica, vol. 100, no. 1-2, pp. 88–95, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  49. T. C. A. Jorge, H. S. Barbosa, A. L. Moreira, W. De Souza, and M. N. L. Meirelles, “The interaction of myotropic and macrophagotropic strains of Trypanosoma cruzi with myoblasts and fibers of skeletal muscle,” Zeitschrift für Parasitenkunde Parasitology Research, vol. 72, no. 5, pp. 577–584, 1986. View at Publisher · View at Google Scholar · View at Scopus
  50. C. O. Rodrigues, P. M. L. Dutra, F. S. Barros, T. Souto-Padrón, J. R. Meyer-Fernandes, and A. H. C. S. Lopes, “Platelet-activating factor induction of secreted phosphatase activity in Trypanosoma cruzi,” Biochemical and Biophysical Research Communications, vol. 266, no. 1, pp. 36–42, 1999. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  51. A. Martiny, J. R. Meyer-Fernandes, W. De Souza, and M. A. Vannier-Santos, “Altered tyrosine phosphorylation of ERK1 MAP kinase and other macrophage molecules caused by Leishmania amastigotes,” Molecular and Biochemical Parasitology, vol. 102, no. 1, pp. 1–12, 1999. View at Publisher · View at Google Scholar · View at Scopus
  52. M. A. Vannier-Santos, A. Martiny, J. R. Meyer-Fernandes, and W. De Souza, “Leishmanial protein kinase C modulates host cell infection via secreted acid phosphatase,” European Journal of Cell Biology, vol. 67, no. 2, pp. 112–119, 1995. View at Google Scholar · View at Scopus
  53. D. Nandan, R. Lo, and N. E. Reiner, “Activation of phosphotyrosine phosphatase activity attenuates mitogen- activated protein kinase signaling and inhibits c-FOS and nitric oxide synthase expression in macrophages infected with Leishmania donovani,” Infection and Immunity, vol. 67, no. 8, pp. 4055–4063, 1999. View at Google Scholar · View at Scopus
  54. M. A. Gomez, I. Contreras, M. Hallé, M. L. Tremblay, R. W. McMaster, and M. Olivier, “Leishmania GP63 alters host signaling through cleavage-activated protein tyrosine phosphatases,” Science Signaling, vol. 2, no. 90, p. ra58, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  55. I. Abu-Dayyeh, K. Hassani, E. R. Westra, J. C. Mottram, and M. Olivier, “Comparative study of the ability of Leishmania mexicana promastigotes and amastigotes to alter macrophage signaling and functions,” Infection and Immunity, vol. 78, no. 6, pp. 2438–2445, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  56. D. E. Cool and J. J. Blum, “Protein tyrosine phosphatase activity in Leishmania donovani,” Molecular and Cellular Biochemistry, vol. 127-128, pp. 143–149, 1993. View at Google Scholar · View at Scopus
  57. M. Nascimento, W. W. Zhang, A. Ghosh et al., “Identification and characterization of a protein-tyrosine phosphatase in Leishmania: involvement in virulence,” The Journal of Biological Chemistry, vol. 281, no. 47, pp. 36257–36268, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  58. M. Anaya-Ruiz, J. L. Rosales-Encina, and P. Talamas-Rohana, “Membrane acid phosphatase (MAP) from Entamoeba histolytica,” Archives of Medical Research, vol. 28, pp. 182–183, 1997. View at Google Scholar · View at Scopus
  59. M. M. Aguirre-García, J. Cerbón, and P. Talamás-Rohana, “Purification and properties of an acid phosphatase from Entamoeba histolytica HM-1:IMSS,” International Journal for Parasitology, vol. 30, no. 5, pp. 585–591, 2000. View at Publisher · View at Google Scholar · View at Scopus
  60. M. M. Aguirre-Garcia, J. L. Rosales-Encina, and P. Talamas-Rohana, “Secreted Entamoeba histolytica acid phosphatase (SAP),” Archives of Medical Research, vol. 28, pp. 184–185, 1997. View at Google Scholar · View at Scopus
  61. J. Ventura-Juarez, M. M. Aguirre-Garcia, and P. Talamas-Rohana, “Subcellular distribution and in situ localization of the acid phosphatase of Entamoeba histolytica,” Archives of Medical Research, vol. 31, no. 4, pp. S183–S184, 2000. View at Publisher · View at Google Scholar · View at Scopus
  62. A. A. de Sá Pinheiro, J. N. Amazonas, F. de Souza Barros et al., “Entamoeba histolytica: an ecto-phosphatase activity regulated by oxidation-reduction reactions,” Experimental Parasitology, vol. 115, no. 4, pp. 352–358, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  63. L. Nimrichter, M. L. Rodrigues, E. G. Rodrigues, and L. R. Travassos, “The multitude of targets for the immune system and drug therapy in the fungal cell wall,” Microbes and Infection, vol. 7, no. 4, pp. 789–798, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  64. P. Mildner, B. Ries, and S. Barbaric, “Acid phosphatase and adenosine triphosphatase activities in the cell wall of baker's yeast,” Biochimica et Biophysica Acta, vol. 391, no. 1, pp. 67–74, 1975. View at Google Scholar · View at Scopus
  65. P. H. Fernanado, G. J. Panagoda, and L. P. Samaranayake, “The relationship between the acid and alkaline phosphatase activity and the adherence of clinical isolates of Candida parapsilosis to human buccal epithelial cells,” APMIS, vol. 107, pp. 1034–1042, 1999. View at Google Scholar
  66. W. N. Arnold, L. C. Mann, and K. H. Sakai, “Acid phosphatases of Sporothrix schenckii,” Journal of General Microbiology, vol. 132, no. 12, pp. 3421–3432, 1986. View at Google Scholar · View at Scopus
  67. M. Bernard, I. Mouyna, G. Dubreucq et al., “Characterization of a cell-wall acid phosphatase (PhoAp) in Aspergillus fumigatus,” Microbiology, vol. 148, no. 9, pp. 2819–2829, 2002. View at Google Scholar · View at Scopus
  68. L. F. Kneipp, V. F. Palmeira, A. A. S. Pinheiro et al., “Phosphatase activity on the cell wall of Fonsecaea pedrosoi,” Medical Mycology, vol. 41, no. 6, pp. 469–477, 2003. View at Publisher · View at Google Scholar · View at Scopus
  69. T. Kiffer-Moreira, A. A. S. Pinheiro, M. R. Pinto et al., “Mycelial forms of Pseudallescheria boydii present ectophosphatase activities,” Archives of Microbiology, vol. 188, no. 2, pp. 159–166, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  70. I. Bose, A. J. Reese, J. J. Ory, G. Janbon, and T. L. Doering, “A yeast under cover: The capsule of Cryptococcus neoformans,” Eukaryotic Cell, vol. 2, no. 4, pp. 655–663, 2003. View at Publisher · View at Google Scholar · View at Scopus
  71. J. K. Klarlund, “Transformation of cells by an inhibitor of phosphatases acting on phosphotyrosine in proteins,” Cell, vol. 41, no. 3, pp. 707–717, 1985. View at Google Scholar · View at Scopus
  72. C. L. Sodré, B. L. M. Moreira, F. B. Nobrega et al., “Characterization of the intracellular Ca2+ pools involved in the calcium homeostasis in Herpetomonas sp. promastigotes,” Archives of Biochemistry and Biophysics, vol. 380, no. 1, pp. 85–91, 2000. View at Publisher · View at Google Scholar · View at PubMed
  73. E. E. de Almeida-Amaral, C. Caruso-Neves, V. M. P. Pires, and J. R. Meyer-Fernandes, “Leishmania amazonensis: characterization of an ouabain-insensitive Na+-ATPase activity,” Experimental Parasitology, vol. 118, no. 2, pp. 165–171, 2008. View at Publisher · View at Google Scholar · View at PubMed
  74. D. Cosentino-Gomes and J. R. Meyer-Fernandes, “Ecto-phosphatases in protozoan parasites: possible roles in nutrition, growth and ROS sensing,” Journal of Bioenergetics and Biomembranes, vol. 43, no. 1, pp. 89–92, 2011. View at Publisher · View at Google Scholar · View at PubMed