Please use this identifier to cite or link to this item: http://ricaxcan.uaz.edu.mx/jspui/handle/20.500.11845/2189
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dc.contributor84378es_ES
dc.contributor4495es_ES
dc.contributor4494es_ES
dc.contributor.otherhttps://orcid.org/0000-0002-3403-9849-
dc.coverage.spatialGlobales_ES
dc.creatorMeza Lamas, Esteban-
dc.creatorBollain y Goytia, Juan José-
dc.creatorRamírez Sandoval, Roxana-
dc.creatorSánchez Rodríguez, Sergio-
dc.creatorLópez Robles, Erendira-
dc.creatorAvalos Díaz, Esperanza del Refugio-
dc.creatorHerrera Esparza, Rafael-
dc.date.accessioned2020-12-10T05:28:47Z-
dc.date.available2020-12-10T05:28:47Z-
dc.date.issued2006-04-19-
dc.identifierinfo:eu-repo/semantics/publishedVersiones_ES
dc.identifier.issn1425-8153es_ES
dc.identifier.issn1689-1392es_ES
dc.identifier.urihttp://ricaxcan.uaz.edu.mx/jspui/handle/20.500.11845/2189-
dc.identifier.urihttps://doi.org/10.48779/54wd-vt90-
dc.description.abstractFas ligand (L) is a membrane protein from the tumor necrosis factor (TNF) family. It induces apoptosis upon contact with its Fas/CD95/APO1 receptor. Trimerization of FasL on the surface of effector cells is essential in the binding of the Fas trimer of the target cells. The receptor then recruits an adaptor and caspase-like proteins which lead apoptosis. This paper reports on the fate of FasL in HEp-2 cells committed to apoptosis by induction with campthotecin. Our main results demonstrated that in non-apoptotic cells, FasL aggregates in the cytoplasm forming trimers of 120 kDa. Apoptosis increases the trimeric FasL species, but also induces its dissociation into monomers of 35 kDa. In conclusion, camptothecin appears to perturb the Fas and FasL segregation in the cytoplasm by promoting the transit of FasL to the cell surface, thus fostering a process of autocrine or paracrine apoptosis. FasL is trimerized prior to Fas/FasL complex formation, and after apoptosis, FasL undergoes an intense turnover.es_ES
dc.language.isoenges_ES
dc.publisherSpringer Naturees_ES
dc.relationhttp://www.cmbl.org.pl/es_ES
dc.relation.urigeneralPublices_ES
dc.rightsAtribución-NoComercial-CompartirIgual 3.0 Estados Unidos de América*
dc.rights.urihttp://creativecommons.org/licenses/by-nc-sa/3.0/us/*
dc.sourceCellular & Molecular Biology Letters Vol. 11, pp. 299 - 311es_ES
dc.subject.classificationMEDICINA Y CIENCIAS DE LA SALUD [3]es_ES
dc.subject.otherFasLes_ES
dc.subject.otherApoptosises_ES
dc.subject.otherOligomerizationes_ES
dc.subject.otherCamptothecines_ES
dc.subject.otherTUNELes_ES
dc.titleCamptothecin induces the transit of fASl trimers to the cell surface in apoptotic heP-2 cellses_ES
dc.typeinfo:eu-repo/semantics/articlees_ES
Appears in Collections:*Documentos Académicos*-- UA Medicina

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