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Type: Artigo de periódico
Author: Morales-Neto, R
Hulshof, L
Ferreira, CV
Gadelha, FR
Abstract: Phosphorylation of parasite proteins plays a key role in the process of cell invasion by Trypanosonla cruzi, the etiologic agent of Chagas' disease. In this sense, characterization of parasite kinases and phosphatases could open new possibilities for the rational design of chemotherapeutic agents for the treatment of Chagas' disease. In this work, we analyzed phosphatase activities in T cruzi homogenates from 2 strains belonging to different lineages and with different resistance to oxidative stress. Tulahuen 2 cells (Lineage 1) showed higher phosphatase activities and specificity constants when compared to the Y strain (Lineage 11). Tulahuen 2 had an optimum phosphatase activity at pH 4.0 and the Y strain at pH 7.0. In both cases, neutral-basic, but not acid, phosphatase activities were increased in the presence of Mg(2+). Although calcium had an inhibitory effect at a pH of 7.0 and 8.0 in the Y strain, this inhibition was restricted to pH 8.0 in the other strain. Different substrates and acid phosphotyrosine and alkaline phosphatase inhibitors exhibited distinct effects on the phosphatase activity of both strains. Our results provide a better understanding of T cruzi phosphatases and reinforce the notion of heterogeneity among T. cruzi populations.
Country: EUA
Editor: Amer Soc Parasitologists
Rights: aberto
Identifier DOI: 10.1645/GE-1899
Date Issue: 2009
Appears in Collections:Unicamp - Artigos e Outros Documentos

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