A metallo phosphatase activity present on the surface of Trypanosoma brucei procyclic forms

dc.creatorFernandes, EC
dc.creatorGranjeiro, JM
dc.creatorAoyama, H
dc.creatorFonseca, FV
dc.creatorMeyer-Fernandes, JR
dc.creatorVercesi, AE
dc.date2003
dc.dateDEC 1
dc.date2014-11-13T15:13:07Z
dc.date2015-11-26T17:10:10Z
dc.date2014-11-13T15:13:07Z
dc.date2015-11-26T17:10:10Z
dc.date.accessioned2018-03-28T23:58:45Z
dc.date.available2018-03-28T23:58:45Z
dc.identifierVeterinary Parasitology. Elsevier Science Bv, v. 118, n. 41671, n. 19, n. 28, 2003.
dc.identifier0304-4017
dc.identifierWOS:000187397900003
dc.identifier10.1016/j.vetpar.2003.09.012
dc.identifierhttp://www.repositorio.unicamp.br/jspui/handle/REPOSIP/76046
dc.identifierhttp://www.repositorio.unicamp.br/handle/REPOSIP/76046
dc.identifierhttp://repositorio.unicamp.br/jspui/handle/REPOSIP/76046
dc.identifier.urihttp://repositorioslatinoamericanos.uchile.cl/handle/2250/1280797
dc.descriptionIn this work, we describe how living cells of Trypanosoma brucei procyclic forms were able to hydrolyze extracellular p-nitrophenylphosphate (pNPP). These intact parasites, which had their viability determined by motility and the Trypan blue method, presented a low level of pNPP hydrolysis in the absence of any divalent metal (0.72 +/- 0.07 nmol pNP/mg min). Interestingly, in the presence of 5 mM MgCl2, ectophosphatase activity of 1.91 +/- 0.21 nmol pNP/mg min was observed. The ectophosphatase activity was also stimulated by MnCl2, CoCl2 and CuCl2 but not by CaCl2 and CdCl2? and was inhibited by ZnCl2. The addition of Mg2+, Mn2+, Co2+ and Cu2+ to extracellular medium increased the ectophosphatase activity in a dose-dependent manner. At 5 mM pNPP, half-maximal stimulation of pNPP hydrolysis was obtained with 0.39 +/- 0.05 MM MgCl2, 0.33 +/- 0.03 mM MnCl2, 1.63 +/- 0.12 mM CoCl2, and 2.04 +/- +/- 0.33 MM CuCl2. In the absence of any divalent metal (basal activity) the apparent K-m for pNPP was 0.66 +/- 0.09 mM, while at saturating MgCl2 concentrations the corresponding apparent K-m for pNPP for Mg2+ -stimulated phosphatase activity (difference between total minus basal phosphatase activity) was 0.27 +/- 0.03 mM. The Mg2+-stimulated pNPP hydrolysis was strongly inhibited by ZnCl2 and vanadate, while the metal-independent basal phosphatase activity was less inhibited by these phosphotyrosyl phosphatase inhibitors. (C) 2003 Elsevier B.V. All rights reserved.
dc.description118
dc.description41671
dc.description19
dc.description28
dc.languageen
dc.publisherElsevier Science Bv
dc.publisherAmsterdam
dc.publisherHolanda
dc.relationVeterinary Parasitology
dc.relationVet. Parasitol.
dc.rightsfechado
dc.rightshttp://www.elsevier.com/about/open-access/open-access-policies/article-posting-policy
dc.sourceWeb of Science
dc.subjectTrypanosoma brucei
dc.subjectectophosphatase
dc.subjectphosphotyrosine
dc.subjectProtein-tyrosine-phosphatase
dc.subjectPlatelet-activating-factor
dc.subjectBlood-stream Forms
dc.subjectEcto-atpase Activity
dc.subjectAcid-phosphatase
dc.subjectLeishmania-donovani
dc.subjectCell-surface
dc.subjectPhosphorylation
dc.subjectKinase
dc.subjectCruzi
dc.titleA metallo phosphatase activity present on the surface of Trypanosoma brucei procyclic forms
dc.typeArtículos de revistas


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