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AutorFerrão, Patrícia M.
AutorOliveira, Fabiane L. de
AutorDegrave, Wim M.
AutorAraujo-Jorge, Tania C.
AutorLima, Leila Mendonça
AutorWaghabi, Mariana C.
Fecha de acceso2017-04-11T16:08:08Z
Fecha de disponibilización2017-04-11T16:08:08Z
Fecha de publicación2012
ReferenciaFERRÃO, Patrícia M. et al. A Phosphoproteomic Approach towards the Understanding of the Role of TGF-b in Trypanosoma cruzi Biology. Plos One, v.7, n.6, e38736, 16p, June 2012.pt_BR
ISSN1932-6203pt_BR
URIhttps://www.arca.fiocruz.br/handle/icict/18381
Idiomaporpt_BR
EditorPublic Library of Sciencept_BR
Derechos de autoropen access
Palabras clave en PortuguésTrypanosoma cruzipt_BR
Palabras clave en PortuguésDoença de Chagaspt_BR
Palabras clave en PortuguésAbordagem Fosfoproteómicapt_BR
Palabras clave en PortuguésFator de crescimento de transformação beta (TGF-b)pt_BR
TítuloA phosphoproteomic approach towards the understanding of the role of TGF-β in Trypanosoma cruzi biologypt_BR
Tipo del documentoArticle
DOI10.1371/journal.pone.0038736
Resumen en InglésTransforming growth factor beta (TGF-β) plays a pivotal role in Chagas disease, not only in the development of chagasic cardiomyopathy, but also in many stages of the T. cruzi life cycle and survival in the host cell environment. The intracellular signaling pathways utilized by T. cruzi to regulate these mechanisms remain unknown. To identify parasite proteins involved in the TGF-β response, we utilized a combined approach of two-dimensional gel electrophoresis (2DE) analysis and mass spectrometry (MS) protein identification. Signaling via TGF-β is dependent on events of phosphorylation, which is one of the most relevant and ubiquitous post-translational modifications for the regulation of gene expression, and especially in trypanosomatids, since they lack several transcriptional control mechanisms. Here we show a kinetic view of T. cruzi epimastigotes (Y strain) incubated with TGF-β for 1, 5, 30 and 60 minutes, which promoted a remodeling of the parasite phosphorylation network and protein expression pattern. The altered molecules are involved in a variety of cellular processes, such as proteolysis, metabolism, heat shock response, cytoskeleton arrangement, oxidative stress regulation, translation and signal transduction. A total of 75 protein spots were up- or down-regulated more than twofold after TGF-β treatment, and from these, 42 were identified by mass spectrometry, including cruzipain-the major T. cruzi papain-like cysteine proteinase that plays an important role in invasion and participates in the escape mechanisms used by the parasite to evade the host immune system. In our study, we observed that TGF-β addition favored epimastigote proliferation, corroborating 2DE data in which proteins previously described to be involved in this process were positively stimulated by TGF-β.pt_BR
AfiliaciónFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil.pt_BR
AfiliaciónFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil.pt_BR
AfiliaciónFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil.pt_BR
AfiliaciónFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Inovações em Terapias, Ensino e Bioprodutos. Rio de Janeiro, RJ. Brasil.pt_BR
AfiliaciónFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil.pt_BR
AfiliaciónFundação Oswaldo Cruz. Instituto Oswaldo Cruz. Laboratório de Genômica Funcional e Bioinformática. Rio de Janeiro, RJ, Brasil.pt_BR
Palavras clave en InglêsTrypanosoma cruzipt_BR
Palavras clave en InglêsChagas diseasept_BR
Palavras clave en InglêsPhosphoproteomic Approachpt_BR
Palavras clave en InglêsTGF-bpt_BR
xmlui.metadata.dc.subject.ods03 Saúde e Bem-Estar


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