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http://ru.facmed.unam.mx/jspui/handle/FACMED_UNAM/A108
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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Elia Torres-Gutiérrez | - |
dc.contributor.author | Perez Cervera, Yobana | - |
dc.contributor.author | Luc Camoin | - |
dc.contributor.author | Zenteno Galindo, Arturo Edgar | - |
dc.contributor.author | Aquino Gil, Moyira Osny | - |
dc.contributor.author | Lefebvre, Tony | - |
dc.contributor.author | Cabrera Bravo, Margarita | - |
dc.contributor.author | Reynoso Ducoing, Olivia Alicia | - |
dc.contributor.author | Bucio Torres, Martha Irene | - |
dc.contributor.author | Salazar Schettino, Paz Maria Silvia | - |
dc.coverage.spatial | CH | - |
dc.date.accessioned | 2019-06-17T17:23:07Z | - |
dc.date.available | 2019-06-17T17:23:07Z | - |
dc.date.issued | 2019 | - |
dc.identifier.uri | http://ru.facmed.unam.mx/jspui/handle/FACMED_UNAM/A108 | - |
dc.description.abstract | Originally an anthropozoonosis in the Americas, Chagas disease has spread from its previous borders through migration. It is caused by the protozoan Trypanosoma cruzi. Differences in disease severity have been attributed to a natural pleomorphism in T. cruzi. Several post-translational modifications (PTMs) have been studied in T. cruzi, but to date no work has focused on O-GlcNAcylation, a highly conserved monosaccharide-PTM of serine and threonine residues mainly found in nucleus, cytoplasm, and mitochondrion proteins. O-GlcNAcylation is thought to regulate protein function analogously to protein phosphorylation; indeed, crosstalk between both PTMs allows the cell to regulate its functions in response to nutrient levels and stress. Herein, we demonstrate O-GlcNAcylation in T. cruzi epimastigotes by three methods: by using specific antibodies against the modification in lysates and whole parasites, by click chemistry labelling, and by proteomics. In total, 1271 putative O-GlcNAcylated proteins and 6 modification sequences were identified by mass spectrometry (data available via ProteomeXchange, ID PXD010285). Most of these proteins have structural and metabolic functions that are essential for parasite survival and evolution. Furthermore, O-GlcNAcylation pattern variations were observed by antibody detection under glucose deprivation and heat stress conditions, supporting their possible role in the adaptive response. Given the numerous biological processes in which O-GlcNAcylated proteins participate, its identification in T. cruzi proteins opens a new research field in the biology of Trypanosomatids, improve our understanding of infection processes and may allow us to identify new therapeutic targets. | - |
dc.language.iso | en | - |
dc.publisher | Frontiers Media S.A. | - |
dc.rights | openAccess | - |
dc.rights.uri | http://creativecommons.org/licenses/by-nc-nd/4.0 | - |
dc.subject | Parasitología | - |
dc.subject | Trypanosoma cruzi | - |
dc.subject | O-Glicosilación de proteínas | - |
dc.subject | Epimastigote | - |
dc.subject.classification | Biología y Química | - |
dc.subject.other | Parasitology | - |
dc.subject.other | Trypanosoma cruzi | - |
dc.subject.other | O-GlcNAcylated proteins | - |
dc.subject.other | Post translational modification | - |
dc.subject.other | Epimastigote | - |
dc.title | Identification of O-Glcnacylated Proteins in Trypanosoma cruzi. | - |
dc.type | Artículo | - |
dc.type | publishedVersion | - |
dcterms.bibliographicCitation | Frontiers in Endocrinology (1664-2392) vol. 10(1), 1-13 (2019) | - |
dcterms.creator | Elia Torres-Gutiérrez::orcid::0000-0002-8829-9777 | - |
dcterms.creator | Perez Cervera, Yobana::cvu::219358 | - |
dcterms.creator | Luc Camoin::orcid::0000-0002-1230-4787 | - |
dcterms.creator | Zenteno Galindo, Arturo Edgar::cvu::5582 | - |
dcterms.creator | Aquino Gil, Moyira Osny::cvu::409244 | - |
dcterms.creator | Lefebvre, Tony::ca::1239389 | - |
dcterms.creator | Cabrera Martinez, Margarita::cvu::756855 | - |
dcterms.creator | Reynoso Ducoing, Olivia Alicia::cvu::56287 | - |
dcterms.creator | Bucio Torres, Martha Irene::cvu::254494 | - |
dcterms.creator | Salazar Schettino, Paz Maria Silvia::cvu::2511 | - |
dc.identifier.doi | 10.3389/fendo.2019.00199 | - |
dc.relation.ispartofjournal | https://www.ncbi.nlm.nih.gov/pmc/issues/328297/ | - |
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