ArticleThe Biochemical journal2004
Identification, characterization and subcellular localization of TcPDE1, a novel cAMP-specific phosphodiesterase from Trypanosoma cruzi.
Article in The Biochemical journal, 2004. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.
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20 citing papers in PubMed, 41 citations in OpenAlex.
- Cyclic AMP compartmentalization drives signal specificity to control vector colonization and mammalian host infection by American trypanosomes.PLoS pathogens · 2026Article
- Cyclic AMP compartmentalization drives signal specificity to control vector colonization and mammalian host infection by American trypanosomes.bioRxiv : the preprint server for biology · 2025Article
- Outlining the structure of cAMP compartments in Trypanosoma cruzi.Trends in parasitology · 2025Review
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- A sticky situation: When trypanosomatids attach to insect tissues.PLoS pathogens · 2023Review
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- Signaling pathways involved in environmental sensing in Trypanosoma cruzi.Molecular microbiology · 2021Review
- Methods to Investigate Signal Transduction Pathways in Trypanosoma cruzi: Cyclic Nucleotide Phosphodiesterases Assay Protocols.Methods in molecular biology (Clifton, N.J.) · 2020Article
- The ever unfolding story of cAMP signaling in trypanosomatids: vive la difference!Frontiers in pharmacology · 2015Review
- Biological and structural characterization of Trypanosoma cruzi phosphodiesterase C and Implications for design of parasite selective inhibitors.The Journal of biological chemistry · 2012Article
- Phosphodiesterase inhibitors as a new generation of antiprotozoan drugs: exploiting the benefit of enzymes that are highly conserved between host and parasite.Future medicinal chemistry · 2011Article
- Article
- Defining the role of a FYVE domain in the localization and activity of a cAMP phosphodiesterase implicated in osmoregulation in Trypanosoma cruzi.Molecular microbiology · 2011Article
- The N terminus of phosphodiesterase TbrPDEB1 of Trypanosoma brucei contains the signal for integration into the flagellar skeleton.Eukaryotic cell · 2010Article
- Two phosphodiesterases from ustilago maydis share structural and biochemical properties with non-fungal phosphodiesterases.Frontiers in microbiology · 2010Article
- A contractile vacuole complex is involved in osmoregulation in Trypanosoma cruzi.Experimental parasitology · 2008Review
- Characterization of a novel cAMP-binding, cAMP-specific cyclic nucleotide phosphodiesterase (TcrPDEB1) from Trypanosoma cruzi.The Biochemical journal · 2006Article
- Cyclic nucleotide specific phosphodiesterases of Leishmania major.BMC microbiology · 2006Article
- Pde1 phosphodiesterase modulates cyclic AMP levels through a protein kinase A-mediated negative feedback loop in Cryptococcus neoformans.Eukaryotic cell · 2005Article
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Authors and funding
6 authors at 2 institutions in 1 country.
Funding
Abstract
Compartmentalization of cAMP phosphodiesterases plays a key role in the regulation of cAMP signalling in mammals. In the present paper, we report the characterization and subcellular localization of TcPDE1, the first cAMP-specific phosphodiesterase to be identified from Trypanosoma cruzi. TcPDE1 is part of a small gene family and encodes a 929-amino-acid protein that can complement a heat-shock-sensitive yeast mutant deficient in phospho-diesterase genes. Recombinant TcPDE1 strongly associates with membranes and cannot be released with NaCl or sodium cholate, suggesting that it is an integral membrane protein. This enzyme is specific for cAMP and its activity is not affected by cGMP, Ca2+, calmodulin or fenotiazinic inhibitors. TcPDE1 is sensitive to the phosphodiesterase inhibitor dipyridamole but is resistant to 3-isobutyl-1-methylxanthine, theophylline, rolipram and zaprinast. Papaverine, erythro-9-(2-hydroxy-3-nonyl)-adenine hydrochloride, and vinpocetine are poor inhibitors of this enzyme. Confocal laser scanning of T. cruzi epimastigotes showed that TcPDE1 is associated with the plasma membrane and concentrated in the flagellum of the parasite. The association of TcPDE1 with this organelle was confirmed by subcellular fractionation and cell-disruption treatments. The localization of this enzyme is a unique feature that distinguishes it from all the trypanosomatid phosphodiesterases described so far and indicates that compartmentalization of cAMP phosphodiesterases could also be important in these parasites.
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