Metabolic Aspects of Glycosomes in Trypanosomatidae – New Data and Views

Michels, Paul A.M.; Hannaert, Véronique; Bringaud, Frédéric

doi:10.1016/s0169-4758(00)01810-x

Cited by 135 publications

(123 citation statements)

References 47 publications

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“…In Kinetoplastida, a taxonomic order of protozoan organisms that includes important pathogens, the first nine enzymes of the glycolytic pathway are included in an organelle called the glycosome (Opperdoes & Borst 1977, Michels et al 2000. Unlike human PFKs, the PFKs of kinetoplastids show the highest degree of sequence similarity with inorganic pyrophosphate (PP i )-dependent enzymes, despite being themselves ATP-dependent.…”

mentioning

confidence: 99%

Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase

Rodriguez

Lander

Ramı́rez

2009

Mem. Inst. Oswaldo Cruz

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mentioning

confidence: 99%

Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase

Rodriguez

Lander

Ramı́rez

2009

Mem. Inst. Oswaldo Cruz

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“…the long slender form in blood, lymphatic fluid, and cerebrospinal fluid of its mammalian host and the procyclic form in the mid-gut of the tsetse fly. Due to the lack of a functional Krebs cycle and oxidative phosphorylation capabilities, the bloodstream forms depend on glycolysis for ATP production, with glycerol as an alternative substrate (1,2). Glycolysis in trypanosomes differs markedly from the corresponding pathway in higher eukaryotes.…”

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confidence: 99%

“…4,72076T. brucei (TbAQP1, TbAQP2, and TbAQP3) 1 and describe their functional expression and their biochemical characterization in Saccharomyces cerevisiae and in Xenopus laevis oocytes.…”

mentioning

confidence: 99%

Cloning, Heterologous Expression, and Characterization of Three Aquaglyceroporins from Trypanosoma brucei

Uzcátegui

Szallies

Pavlovic-Djuranovic³

et al. 2004

Journal of Biological Chemistry

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Trypanosoma brucei, causative for African sleeping sickness, relies exclusively on glycolysis for ATP production. Under anaerobic conditions, glucose is converted to equimolar amounts of glycerol and pyruvate, which are both secreted from the parasite. As we have shown previously, glycerol transport in T. brucei occurs via specific membrane proteins (Wille, U., Schade, B., and Duszenko, M. (1998) Eur. J. Biochem. 256, 245-250). Here, we describe cloning and biochemical characterization of the three trypanosomal aquaglyceroporins (AQP; TbAQP1-3), which show a 40 -45% identity to mammalian AQP3 and -9. AQPs belong to the major intrinsic protein family and represent channels for small non-ionic molecules. Both TbAQP1 and TbAQP3 contain two highly conserved NPA motifs within the pore-forming region, whereas TbAQP2 contains NSA and NPS motifs instead, which are only occasionally found in AQPs. For functional characterization, all three proteins were heterologously expressed in yeast and Xenopus oocytes. In the yeast fps1⌬ mutant, TbAQPs suppressed hypoosmosensitivity and rendered cells to a hyper-osmosensitive phenotype, as expected for unregulated glycerol channels. Under iso-and hyperosmotic conditions, these cells constitutively released glycerol, consistent with a glycerol efflux function of TbAQP proteins. TbAQP expression in Xenopus oocytes increased permeability for water, glycerol and, interestingly, dihydroxyacetone. Except for urea, TbAQPs were virtually impermeable for other polyols; only TbAQP3 transported erythritol and ribitol. Thus, TbAQPs represent mainly water/glycerol/dihydroxyacetone channels involved in osmoregulation and glycerol metabolism in T. brucei. This function and especially the so far not investigated transport of dihydroxyacetone may be pivotal for the survival of the parasite survival under non-aerobic or osmotic stress conditions.

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“…The compartmentalization of glycolysis, first described in Trypanosoma brucei , was observed in all members of the Trypanosomatidae family (Cannata et al 1982, Coombs et al 1982, Taylor et al 1979) and the organelle was thus called a glycosome. Biochemical studies carried out on isolated fractions have shown that the glycosomes of trypanosomatids are involved in other metabolic pathways such as carbon dioxide fixation (Opperdoes & Cottem 1982), purine salvage and de novo pyrimidine biosynthesis (reviewed in Opperdoes 1987, Shih et al 1998, Michels et al 2000, Parsons et al 2001). Opperdoes and co-workers obtained a highly purified subcellular fraction containing glycosomes from bloodstream-form trypomastigotes of T. brucei: grinding with silicon carbide disrupted the parasites and a glycosomeenriched fraction was recovered from a Percoll gradient.…”

Section: Isolation Of the Glycosome (Peroxisome)mentioning

confidence: 99%

Cell fractionation of parasitic protozoa: a review

Souza

Cunha-e-Silva

2003

Mem. Inst. Oswaldo Cruz

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Cell fractionation, a methodological strategy for obtaining purified organelle preparations, has been applied successfully to parasitic protozoa by a number of investigators. Here we present and discuss the work of several groups that have obtained highly purified subcellular fractions from trypanosomatids, Apicomplexa and trichomonads, and whose work have added substantially to our knowledge of the cell biology of these parasites.

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Metabolic Aspects of Glycosomes in Trypanosomatidae – New Data and Views

Cited by 135 publications

References 47 publications

Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase

Molecular and biochemical characterisation of Trypanosoma cruzi phosphofructokinase

Cloning, Heterologous Expression, and Characterization of Three Aquaglyceroporins from Trypanosoma brucei

Cell fractionation of parasitic protozoa: a review

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