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dc.contributor.author
Díaz Viraqué, Florencia
dc.contributor.author
Chiribao, María Laura
dc.contributor.author
Paes Vieira, Lisvane
dc.contributor.author
Machado, Matias R.
dc.contributor.author
Faral Tello, Paula
dc.contributor.author
Tomasina, Ramiro
dc.contributor.author
Trochine, Andrea
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dc.contributor.author
Robello, Carlos
dc.date.available
2024-04-22T15:18:43Z
dc.date.issued
2023-01
dc.identifier.citation
Díaz Viraqué, Florencia; Chiribao, María Laura; Paes Vieira, Lisvane; Machado, Matias R.; Faral Tello, Paula; et al.; New Insights into the Role of the Trypanosoma cruzi Aldo-Keto Reductase TcAKR; MDPI; Pathogens; 12; 1; 1-2023; 1-16
dc.identifier.issn
2076-0817
dc.identifier.uri
http://hdl.handle.net/11336/233785
dc.description.abstract
Chagas disease is a zoonotic infectious disease caused by the protozoan parasite Trypanosoma cruzi. It is distributed worldwide, affecting around 7 million people; there is no effective treatment, and it constitutes a leading cause of disability and premature death in the Americas. Only two drugs are currently approved for the treatment, Benznidazole and Nifurtimox, and both have to be activated by reducing the nitro-group. The T. cruzi aldo-keto reductase (TcAKR) has been related to the metabolism of benznidazole. TcAKR has been extensively studied, being most efforts focused on characterizing its implication in trypanocidal drug metabolism; however, little is known regarding its biological role. Here, we found that TcAKR is confined, throughout the entire life cycle, into the parasite mitochondria providing new insights into its biological function. In particular, in epimastigotes, TcAKR is associated with the kinetoplast, which suggests additional roles of the protein. The upregulation of TcAKR, which does not affect TcOYE expression, was correlated with an increase in PGF2α, suggesting that this enzyme is related to PGF2α synthesis in T. cruzi. Structural analysis showed that TcAKR contains a catalytic tetrad conserved in the AKR superfamily. Finally, we found that TcAKR is also involved in Nfx metabolization.
dc.format
application/pdf
dc.language.iso
eng
dc.publisher
MDPI
dc.rights
info:eu-repo/semantics/openAccess
dc.rights.uri
https://creativecommons.org/licenses/by/2.5/ar/
dc.subject
TRYPANOSOMA CRUZI
dc.subject
ALDO-KETO REDUCTASE
dc.subject
MITHOCONDRIAL ENZYME
dc.subject
KINETOPLAST
dc.subject.classification
Bioquímica y Biología Molecular
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dc.subject.classification
Ciencias Biológicas
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dc.subject.classification
CIENCIAS NATURALES Y EXACTAS
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dc.title
New Insights into the Role of the Trypanosoma cruzi Aldo-Keto Reductase TcAKR
dc.type
info:eu-repo/semantics/article
dc.type
info:ar-repo/semantics/artículo
dc.type
info:eu-repo/semantics/publishedVersion
dc.date.updated
2024-04-09T11:53:11Z
dc.journal.volume
12
dc.journal.number
1
dc.journal.pagination
1-16
dc.journal.pais
Suiza
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dc.journal.ciudad
Basel
dc.description.fil
Fil: Díaz Viraqué, Florencia. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Chiribao, María Laura. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Paes Vieira, Lisvane. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Machado, Matias R.. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Faral Tello, Paula. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Tomasina, Ramiro. Instituto Pasteur de Montevideo; Uruguay
dc.description.fil
Fil: Trochine, Andrea. Consejo Nacional de Investigaciones Científicas y Técnicas. Centro Científico Tecnológico Conicet - Patagonia Norte. Instituto Andino Patagónico de Tecnologías Biológicas y Geoambientales. Universidad Nacional del Comahue. Instituto Andino Patagónico de Tecnologías Biológicas y Geoambientales; Argentina
dc.description.fil
Fil: Robello, Carlos. Instituto Pasteur de Montevideo; Uruguay
dc.journal.title
Pathogens
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/url/https://www.mdpi.com/2076-0817/12/1/85
dc.relation.alternativeid
info:eu-repo/semantics/altIdentifier/doi/http://dx.doi.org/10.3390/pathogens12010085
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