Please use this identifier to cite or link to this item: http://repositorio.unicamp.br/jspui/handle/REPOSIP/198334
Type: Artigo de periódico
Title: Distinct Phosphatase Activity Profiles In Two Strains Of Trypanosoma Cruzi.
Author: Morales-Neto, R
Hulshof, L
Ferreira, C V
Gadelha, F R
Abstract: Phosphorylation of parasite proteins plays a key role in the process of cell invasion by Trypanosoma 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 I) showed higher phosphatase activities and specificity constants when compared to the Y strain (Lineage II). 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 Mg2+. 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.
Subject: Culture Media
Hydrogen-ion Concentration
Kinetics
Nitrophenols
Organophosphorus Compounds
Phosphates
Phosphoric Monoester Hydrolases
Phosphorylation
Protozoan Proteins
Trypanosoma Cruzi
Citation: The Journal Of Parasitology. v. 95, n. 6, p. 1525-31, 2009-Dec.
Rights: fechado
Identifier DOI: 10.1645/GE-1899.1
Address: http://www.ncbi.nlm.nih.gov/pubmed/19476404
Date Issue: 2009
Appears in Collections:Unicamp - Artigos e Outros Documentos

Files in This Item:
File SizeFormat 
pmed_19476404.pdf283.87 kBAdobe PDFView/Open


Items in DSpace are protected by copyright, with all rights reserved, unless otherwise indicated.