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dc.contributor.authorRosal-Vela, Antonio-
dc.contributor.authorGarcía-Rodríguez, Sonia-
dc.contributor.authorLongobardo, Victoria-
dc.contributor.authorPostigo, Jorge-
dc.contributor.authorIglesias, Marcos-
dc.contributor.authorLario, Antonio-
dc.contributor.authorMerino, Jesús-
dc.contributor.authorMerino, Ramón-
dc.contributor.authorZubiaur, Mercedes-
dc.contributor.authorSancho, Jaime-
dc.date.accessioned2018-05-08T10:29:31Z-
dc.date.available2018-05-08T10:29:31Z-
dc.date.issued2016-
dc.identifierdoi: 10.1016/j.jprot.2015.11.023-
dc.identifiere-issn: 1876-7737-
dc.identifierissn: 1874-3919-
dc.identifier.citationJournal of Proteomics 134: 127-137 (2016)-
dc.identifier.urihttp://hdl.handle.net/10261/164535-
dc.descriptionA. Rosal-Vela et al.-
dc.description.abstractCollagen type II-induced arthritis (CIA) is an inflammatory and autoimmune disease. Spleen protein extracts were subjected to 2D-DiGE and MS-MALDI-TOF/TOF analysis to identify protein species that differ in abundance in CD38-KO versus B6 WT mice either with arthritis or with inflammation. Using multivariate analyses, in Col-II-immunized mice, 23 distinct spleen protein species were able to discriminate between WT and CD38-KO mice. Among them, several citrullinated proteins and multiple serotransferrin (Tf) species were identified. In contrast, in CFA/IFA-treated mice, the distinct protein profile, which discriminates between CD38-KO and WT mice, was unrelated with Tf, but not with citrullination. Unexpectedly, non-immunized CD38-KO mice showed a distinct proteome profile as compared with that in non-immunized WT mice, and again multiple protein species were identified as Tf. By using a μLC-TOF-MS method to separate and detect Tf glycopeptide glycoforms, increases in fucosylation and glycan branching was observed in sera from mice CIA versus non-immunized, and between WT and CD38-KO with arthritis. Data on 2-DE Tf spots indicated differences in glycosylation related with NeuGc content. Thus, Tf changed significantly in its glycosylation pattern in arthritic mice. The MS data have been deposited to the ProteomeXchange Consortium with the dataset identifiers: PXD002644, PXD002643, PXD003183, and PXD003163. Significance: 2-DE followed by μLC-TOF-MS could be implemented to identify Tf glycoforms linked to specific protein species, and correlate a particular Tf species to a function. To gain insight into the relationship between transferrin glycoforms and its biological function it is particularly interesting to study putative differences in the glycosylation pattern of Tf in specific tissues associated with the disease (i.e.: joints), or in specific compartments such as exosomes/microvesicles, which are highly enriched in Tf receptors.-
dc.description.sponsorshipThis work was supported in part by the European Commission in collaboration with the following Funding Agencies: Ministerio de Economía y Competitividad (MINECO) del Gobierno de España grant number SAF2011-27261 (to J.S.), grant CTQ2011-27130, awarded to V. S-N; grant number SAF2011-22463 (to R.M.; cofunded by the European Regional Development Fund), and grant number SAF2012-34059 (to J.M.; cofunded by the European Regional Development Fund); Consejería de Innovación, Ciencia y Empresa de la Junta de Andalucía, grant number P08-CTS-04046 (to J.S.). From the MINECO del Gobierno de España, grant number IPT2011-1527-010000, associated to Fibrostatin SL, to J.M. A.R.V. was supported by a fellowship-contract from Consejería de Innovación, Ciencia y Empresa de la Junta de Andalucía. S.G.R. was supported by a JAEDoc contract from CSIC and a MINECO contract. A.B. was supported by a FPU fellowship from the Ministry of Education, Culture and Sport.-
dc.publisherElsevier-
dc.rightsclosedAccess-
dc.subjectGlycosylation-
dc.subjectCD38-
dc.subjectTransferrin-
dc.subjectProtein species-
dc.subjectInflammation-
dc.subjectArthritis-
dc.subjectCitrullination-
dc.titleIdentification of multiple transferrin species in the spleen and serum from mice with collagen-induced arthritis which may reflect changes in transferrin glycosylation associated with disease activity: The role of CD38-
dc.typeartículo-
dc.identifier.doi10.1016/j.jprot.2015.11.023-
dc.date.updated2018-05-08T10:29:32Z-
dc.description.versionPeer Reviewed-
dc.language.rfc3066eng-
dc.contributor.funderFibrostatin-
dc.contributor.funderJunta de Andalucía-
dc.contributor.funderConsejo Superior de Investigaciones Científicas (España)-
dc.contributor.funderMinisterio de Educación, Cultura y Deporte (España)-
dc.contributor.funderMinisterio de Economía y Competitividad (España)-
dc.contributor.funderEuropean Commission-
dc.relation.csic-
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003176es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003329es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100000780es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100003339es_ES
dc.identifier.funderhttp://dx.doi.org/10.13039/501100011011es_ES
dc.identifier.pmid26639305-
dc.type.coarhttp://purl.org/coar/resource_type/c_6501es_ES
item.openairetypeartículo-
item.grantfulltextnone-
item.cerifentitytypePublications-
item.openairecristypehttp://purl.org/coar/resource_type/c_18cf-
item.fulltextNo Fulltext-
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