Glycosome
Mostrando 1-12 de 17 artigos, teses e dissertações.
-
1. The relationship between the cellular location of Leishmania (Leishmania) amazonensis arginase and its role during murine macrophage infection / Relação entre a localização celular da enzima arginase de Leishmania (Leishmania) amazonensis e seu papel na infecção de macrófagos murinos
In the mammal host, Leishmania parasites live inside macrophages escaping from their microbicidal mechanisms, such as the nitric oxide (NO) production. The macrophage NO production by inducible nitric oxide synthase (iNOS) requires L-arginine as substrate, the same amino acid required by arginase to generate ornithine and urea. So, arginase may play a dual r
Publicado em: 2010
-
2. Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase
The characterisation of the gene encoding Trypanosoma cruzi CL Brener phosphofructokinase (PFK) and the biochemical properties of the expressed enzyme are reported here. In contradiction with previous reports, the PFK genes of CL Brener and YBM strain T. cruzi were found to be similar to their Leishmania mexicana and Trypanosoma brucei homologs in terms of b
Memórias do Instituto Oswaldo Cruz. Publicado em: 2009-08
-
3. Structural organization of Trypanosoma cruzi
Since the initial description of Trypanosoma cruzi by Carlos Chagas in 1909, several research groups have used different microscopic techniques to obtain detailed information about the various developmental stages found in the life cycle of this intracellular parasite. This review describes the present knowledge on the organization of the most important stru
Memórias do Instituto Oswaldo Cruz. Publicado em: 2009-07
-
4. A α-glycerophosphate dehydrogenase is present in Trypanosoma cruzi glycosomes
α-glycerophosphate dehydrogenase (α-GPDH-EC.1.1.1.8) has been considered absent in Trypanosoma cruzi in contradiction with all other studied trypanosomatids. After observing that the sole malate dehydrogenase can not maintain the intraglycosomal redox balance, GPDH activity was looked for and found, although in very variable levels, in epimastigotes extrac
Memórias do Instituto Oswaldo Cruz. Publicado em: 2001-07
-
5. Compartmentation protects trypanosomes from the dangerous design of glycolysis
Unlike in other organisms, in trypanosomes and other Kinetoplastida the larger part of glycolysis takes place in a specialized organelle, called the glycosome. At present it is impossible to remove the glycosome without changing much of the rest of the cell. It would seem impossible, therefore, to assess the metabolic consequences of this compartmentation. T
The National Academy of Sciences.
-
6. Characterization of an in vitro assay for import of 3-phosphoglycerate kinase into the glycosomes of Trypanosoma brucei.
Glycosomes are microbody organelles found in kinetoplastida, where they serve to compartmentalize the enzymes of the glycolytic pathway. In order to identify the mechanism by which these enzymes are targeted to the glycosome, we have modified the in vitro import assay developed by Dovey et al. (Proc. Natl. Acad. Sci. USA 85:2598-2602, 1988). This assay measu
-
7. Compartmentation of phosphoglycerate kinase in Trypanosoma brucei plays a critical role in parasite energy metabolism
African trypanosomes compartmentalize glycolysis in a microbody, the glycosome. When growing in the mammalian bloodstream, trypanosomes contain only a rudimentary mitochondrion, and the first seven glycolytic enzymes, including phosphoglycerate kinase, are located in the glycosome. Procyclic trypanosomes, growing in the gut of tsetse flies, possess a fully d
The National Academy of Sciences.
-
8. Glucose is toxic to glycosome-deficient trypanosomes
Trypanosomatids, the etiologic agents of sleeping sickness, leishmaniasis, and Chagas' disease, compartmentalize glycolysis within glycosomes, metabolic organelles related to peroxisomes. Here, we identify a trypanosome homologue of PEX14, one of the components of the peroxisomal protein import docking complex. We have used double-stranded RNA interference t
National Academy of Sciences.
-
9. Biogenesis of glycosomes of Trypanosoma brucei: an in vitro model of 3-phosphoglycerate kinase import.
Glycosomes are intracellular, membrane-bound microbody organelles of trypanosomes and leishmania. Nine glycolytic enzymes are the major protein components of the glycosomes of Trypanosoma brucei long-slender bloodstream forms. Glycosomal proteins are believed to be synthesized in the cytoplasm and inserted across the glycosomal membrane posttranslationally.
-
10. Functional identification of a Leishmania gene related to the peroxin 2 gene reveals common ancestry of glycosomes and peroxisomes.
Glycosomes are membrane-bounded microbody organelles that compartmentalize glycolysis as well as other important metabolic processes in trypanosomatids. The compartmentalization of these enzymatic reactions is hypothesized to play a crucial role in parasite physiology. Although the metabolic role of glycosomes differs substantially from that of the peroxisom
-
11. Vitamin C biosynthesis in trypanosomes: A role for the glycosome
The capacity to synthesize vitamin C (ascorbate) is widespread in eukaryotes but is absent from humans. The last step in the biosynthetic pathway involves the conversion of an aldonolactone substrate to ascorbate, a reaction catalyzed by members of an FAD-dependent family of oxidoreductases. Here we demonstrate that both the African trypanosome, Trypanosoma
National Academy of Sciences.
-
12. Modulation of the Leishmania donovani Peroxin 5 Quaternary Structure by Peroxisomal Targeting Signal 1 Ligands
The import of proteins containing the peroxisomal targeting signal 1 (PTS1) into the Leishmania glycosome is dependent on the docking of the PTS1-loaded LdPEX5 cytosolic receptor with LdPEX14 on the glycosome surface. Here we show that, in the absence of PTS1, LdPEX5 is a tetramer that is stabilized by two distinct interaction domains; the first is a coiled-
American Society for Microbiology.