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dc.contributor.authorTahir, Muhammad-
dc.contributor.authorArshid, Samina-
dc.contributor.authorFontes, Belchor-
dc.contributor.authorCastro, Mariana S.-
dc.contributor.authorSidoli, Simone-
dc.contributor.authorSchwämmle, Veit-
dc.contributor.authorLuz, Isabelle Souza-
dc.contributor.authorRoepstorff, Peter-
dc.contributor.authorFontes, Wagner-
dc.date.accessioned2022-10-26T22:50:21Z-
dc.date.available2022-10-26T22:50:21Z-
dc.date.issued2020-08-14-
dc.identifier.citationTAHIR, Muhammad et al. Phosphoproteomic analysis of rat neutrophils shows the effect of intestinal ischemia/reperfusion and preconditioning on kinases and phosphatases. International Journal of Molecular Sciences, Basel, v. 21, n. 16, art. 5799, 2020. DOI 10.3390/ijms21165799. Disponível em: https://www.mdpi.com/1422-0067/21/16/5799. Acesso em: 26 out. 2022.pt_BR
dc.identifier.urihttps://repositorio.unb.br/handle/10482/45070-
dc.language.isoInglêspt_BR
dc.publisherMDPIpt_BR
dc.rightsAcesso Abertopt_BR
dc.titlePhosphoproteomic analysis of rat neutrophils shows the effect of intestinal ischemia/reperfusion and preconditioning on kinases and phosphatasespt_BR
dc.typeArtigopt_BR
dc.subject.keywordIsquemiapt_BR
dc.subject.keywordReperfusão (Fisiologia)pt_BR
dc.subject.keywordFosforilaçãopt_BR
dc.subject.keywordNeutrófilospt_BR
dc.rights.licenseInternational Journal of Molecular Sciences - This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (https:// creativecommons.org/licenses/by/ 4.0/). Fonte: https://www.mdpi.com/openaccess. Acesso em: 26 out. 2022.pt_BR
dc.identifier.doihttps://doi.org/10.3390/ijms21165799pt_BR
dc.description.abstract1Intestinal ischemia reperfusion injury (iIRI) is a severe clinical condition presenting high morbidity and mortality worldwide. Some of the systemic consequences of IRI can be prevented by applying ischemic preconditioning (IPC), a series of short ischemia/reperfusion events preceding the major ischemia. Although neutrophils are key players in the pathophysiology of ischemic injuries, neither the dysregulation presented by these cells in iIRI nor the protective effect of iIPC have their regulation mechanisms fully understood. Protein phosphorylation, as well as the regulation of the respective phosphatases and kinases are responsible for regulating a large number of cellular functions in the inflammatory response. Moreover, in previous work we found hydrolases and transferases to be modulated in iIR and iIPC, suggesting the possible involvement of phosphatases and kinases in the process. Therefore, in the present study, we analyzed the phosphoproteome of neutrophils from rats submitted to mesenteric ischemia and reperfusion, either submitted or not to IPC, compared to quiescent controls and sham laparotomy. Proteomic analysis was performed by multi-step enrichment of phosphopeptides, isobaric labeling, and LC-MS/MS analysis. Bioinformatics was used to determine phosphosite and phosphopeptide abundance and clustering, as well as kinases and phosphatases sites and domains. We found that most of the phosphorylation-regulated proteins are involved in apoptosis and migration, and most of the regulatory kinases belong to CAMK and CMGC families. An interesting finding revealed groups of proteins that are modulated by iIR, but such modulation can be prevented by iIPC. Among the regulated proteins related to the iIPC protective effect, Vamp8 and Inpp5d/Ship are discussed as possible candidates for control of the iIR damage.pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-8722-5103pt_BR
dc.identifier.orcidhttps://orcid.org/0000-0001-5140-8573pt_BR
dc.contributor.emailmailto:tahir.bio@gmail.compt_BR
dc.contributor.emailmailto:saminatahir83@yahoo.compt_BR
dc.contributor.emailmailto:belchor@uol.com.brpt_BR
dc.contributor.emailmailto:mscastro69@gmail.compt_BR
dc.contributor.emailmailto:simone.sidoli@gmail.compt_BR
dc.contributor.emailmailto:veits@bmb.sdu.dkpt_BR
dc.contributor.emailmailto:isabelle.sluz@gmail.compt_BR
dc.contributor.emailmailto:roe@bmb.sdu.dkpt_BR
dc.contributor.emailmailto:wagnerf@unb.brpt_BR
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