Analysis of proteasomal proteolysis during the in vitro metacyclogenesis of Trypanosoma cruzi
| Autor: | Josiane Cardoso, Renata Guerra Sá, Stenio Perdigão Fragoso, Marco Aurélio Krieger, Samuel Goldenberg, Tiago Ferreira Leal, Carla V. de Paula Lima, Daniela Fiori Gradia |
|---|---|
| Jazyk: | angličtina |
| Rok vydání: | 2011 |
| Předmět: |
Trypanosoma
Proteasome Endopeptidase Complex Proteases Trypanosoma cruzi Proteolysis Cellular differentiation Blotting Western 030231 tropical medicine Cell lcsh:Medicine Protozoology Microbiology 03 medical and health sciences 0302 clinical medicine Ubiquitin medicine Animals lcsh:Science Biology 030304 developmental biology 0303 health sciences Multidisciplinary medicine.diagnostic_test biology Hydrolysis lcsh:R Parasite Physiology Ubiquitination biology.organism_classification In vitro Cell biology medicine.anatomical_structure Biochemistry Proteasome biology.protein Parastic Protozoans Parasitology lcsh:Q Research Article |
| Zdroj: | Repositório Institucional da UFOP Universidade Federal de Ouro Preto (UFOP) instacron:UFOP PLoS ONE, Vol 6, Iss 6, p e21027 (2011) PLoS ONE |
| Popis: | Proteasomes are large protein complexes, whose main function is to degrade unnecessary or damaged proteins. The inhibition of proteasome activity in Trypanosoma cruzi blocks parasite replication and cellular differentiation. We demonstrate that proteasome-dependent proteolysis occurs during the cellular differentiation of T. cruzi from replicative non-infectious epimastigotes to non-replicative and infectious trypomastigotes (metacyclogenesis). No peaks of ubiquitin-mediated degradation were observed and the profile of ubiquitinated conjugates was similar at all stages of differentiation. However, an analysis of carbonylated proteins showed significant variation in oxidized protein levels at the various stages of differentiation and the proteasome inhibition also increased oxidized protein levels. Our data suggest that different proteasome complexes coexist during metacyclogenesis. The 20S proteasome may be free or linked to regulatory particles (PA700, PA26 and PA200), at specific cell sites and the coordinated action of these complexes would make it possible for proteolysis of ubiquitin-tagged proteins and oxidized proteins, to coexist in the cell. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|