ArticleParasites & vectors2015
Identification and functional characterization of a novel arginine/ornithine transporter, a member of a cationic amino acid transporter subfamily in the Trypanosoma cruzi genome.
Article in Parasites & vectors, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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9 citing papers in PubMed, 12 citations in OpenAlex.
- The Glutamatergic System Regulates Feather Pecking Behaviors in Laying Hens Through the Gut-Brain Axis.Animals : an open access journal from MDPI · 2025Article
- Polyamine Metabolism for Drug Intervention in Trypanosomatids.Pathogens (Basel, Switzerland) · 2024Review
- Identification of transport systems involved in eflornithine delivery across the blood-brain barrier.Frontiers in drug delivery · 2023Article
- Polyamine Metabolism inMedical sciences (Basel, Switzerland) · 2022Review
- Sheltered in Stromal Tissue Cells,Pathogens (Basel, Switzerland) · 2022Article
- The Uptake and Metabolism of Amino Acids, and Their Unique Role in the Biology of Pathogenic Trypanosomatids.Pathogens (Basel, Switzerland) · 2018Review
- Ornithine uptake and the modulation of drug sensitivity inFASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2017Article
- Metabolomic profiling reveals a finely tuned, starvation-induced metabolic switch inThe Journal of biological chemistry · 2017Article
- Article
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Authors and funding
9 authors at 6 institutions in 3 countries.
Funding
Abstract
backgroundTrypanosoma cruzi, the etiological agent of Chagas disease, is auxotrophic for arginine. It obtains this amino acid from the host through transporters expressed on the plasma membrane and on the membranes of intracellular compartments. A few cationic amino acid transporters have been characterized at the molecular level, such as the novel intracellular arginine/ornithine transporter, TcCAT1.1, a member of the TcCAT subfamily that is composed of four almost identical open reading frames in the T. cruzi genome.
methodsThe functional characterization of the TcCAT1.1 isoform was performed in two heterologous expression systems. TcCAT subfamily expression was evaluated by real-time PCR in polysomal RNA fractions, and the cellular localization of TcCAT1.1 fused to EGFP was performed by confocal and immunoelectron microscopy.
resultsIn the S. cerevisiae expression system, TcCAT1.1 showed high affinity for arginine (K m = 0.085 ± 0.04 mM) and low affinity for ornithine (K m = 1.7 ± 0.2 mM). Xenopus laevis oocytes expressing TcCAT1.1 showed a 7-fold increase in arginine uptake when they were pre-loaded with arginine, indicating that transport is enhanced by substrates on the trans side of the membrane (trans-stimulation). Oocytes that were pre-loaded with [(3)H]-arginine displayed a 16-fold higher efflux of [(3)H]-arginine compared with that of the control. Analysis of polysomal RNA fractions demonstrated that the expression of members of the arginine transporter TcCAT subfamily is upregulated under nutritional stress and that this upregulation precedes metacyclogenesis. To investigate the cellular localization of the transporter, EGFP was fused to TcCAT1.1, and fluorescence microscopy and immunocytochemistry revealed the intracellular labeling of vesicles in the anterior region, in a network of tubules and vesicles.
conclusionsTcCAT1.1 is a novel arginine/ornithine transporter, an exchanger expressed in intracellular compartments that is physiologically involved in arginine homeostasis throughout the T. cruzi life cycle. The properties and estimated kinetic parameters of TcCAT1.1 can be extended to other members of the TcCAT subfamily.
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