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dc.contributor.authorGallardo-Vara, Eunate
dc.contributor.authorRuiz-Llorente, Lidia
dc.contributor.authorCasado-Vela, Juan
dc.contributor.authorRuiz-Rodriguez, Maria J 
dc.contributor.authorLópez-Andrés, Natalia
dc.contributor.authorPattnaik, Asit K
dc.contributor.authorQuintanilla, Miguel
dc.contributor.authorBernabeu, Carmelo
dc.date.accessioned2019-09-24T12:02:25Z
dc.date.available2019-09-24T12:02:25Z
dc.date.issued2019-09
dc.identifier.citationCells. 2019; 8(9):E1082es_ES
dc.identifier.issn2073-4409es_ES
dc.identifier.urihttp://hdl.handle.net/20.500.12105/8373
dc.description.abstractEndoglin is a 180-kDa glycoprotein receptor primarily expressed by the vascular endothelium and involved in cardiovascular disease and cancer. Heterozygous mutations in the endoglin gene (ENG) cause hereditary hemorrhagic telangiectasia type 1, a vascular disease that presents with nasal and gastrointestinal bleeding, skin and mucosa telangiectases, and arteriovenous malformations in internal organs. A circulating form of endoglin (alias soluble endoglin, sEng), proteolytically released from the membrane-bound protein, has been observed in several inflammation-related pathological conditions and appears to contribute to endothelial dysfunction and cancer development through unknown mechanisms. Membrane-bound endoglin is an auxiliary component of the TGF-β receptor complex and the extracellular region of endoglin has been shown to interact with types I and II TGF-β receptors, as well as with BMP9 and BMP10 ligands, both members of the TGF-β family. To search for novel protein interactors, we screened a microarray containing over 9000 unique human proteins using recombinant sEng as bait. We find that sEng binds with high affinity, at least, to 22 new proteins. Among these, we validated the interaction of endoglin with galectin-3, a secreted member of the lectin family with capacity to bind membrane glycoproteins, and with tripartite motif-containing protein 21 (TRIM21), an E3 ubiquitin-protein ligase. Using human endothelial cells and Chinese hamster ovary cells, we showed that endoglin co-immunoprecipitates and co-localizes with galectin-3 or TRIM21. These results open new research avenues on endoglin function and regulation.es_ES
dc.language.isoenges_ES
dc.publisherMultidisciplinary Digital Publishing Institute (MDPI) es_ES
dc.type.hasVersionVoRes_ES
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/*
dc.subjectBMPes_ES
dc.subjectHHTes_ES
dc.subjectTGF-βes_ES
dc.subjectTRIM familyes_ES
dc.subjectCanceres_ES
dc.subjectEndoglines_ES
dc.subjectEndothelial cellses_ES
dc.subjectGalectin familyes_ES
dc.subjectPreeclampsiaes_ES
dc.subjectProtein–protein interactionses_ES
dc.titleEndoglin Protein Interactome Profiling Identifies TRIM21 and Galectin-3 as New Binding Partnerses_ES
dc.typejournal articlees_ES
dc.rights.licenseAtribución 4.0 Internacional*
dc.identifier.pubmedID31540324es_ES
dc.format.volume8es_ES
dc.format.number9es_ES
dc.format.page1082es_ES
dc.identifier.doi10.3390/cells8091082es_ES
dc.description.peerreviewedes_ES
dc.identifier.e-issn2073-4409es_ES
dc.relation.publisherversionhttps://doi.org/10.3390/cells8091082es_ES
dc.identifier.journalCellses_ES
dc.repisalud.orgCNICCNIC::Grupos de investigación::Regulación Génica en Remodelado Vascular e Inflamaciónes_ES
dc.repisalud.institucionCNICes_ES
dc.rights.accessRightsopen accesses_ES


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Atribución 4.0 Internacional
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