Por favor, use este identificador para citar o enlazar a este item:
http://hdl.handle.net/10261/77814
COMPARTIR / EXPORTAR:
SHARE CORE BASE | |
Visualizar otros formatos: MARC | Dublin Core | RDF | ORE | MODS | METS | DIDL | DATACITE | |
Campo DC | Valor | Lengua/Idioma |
---|---|---|
dc.contributor.author | Cernuda-Morollón, Eva | - |
dc.contributor.author | Pineda-Molina, Estela | - |
dc.contributor.author | Cañada, F. Javier | - |
dc.contributor.author | Pérez-Sala, Dolores | - |
dc.date.accessioned | 2013-06-07T11:01:26Z | - |
dc.date.available | 2013-06-07T11:01:26Z | - |
dc.date.issued | 2001 | - |
dc.identifier.citation | Journal of Biological Chemistry 276(38): 35530- 35536 (2001) | - |
dc.identifier.issn | 0021-9258 | - |
dc.identifier.uri | http://hdl.handle.net/10261/77814 | - |
dc.description.abstract | Cyclopentenone prostaglandins display anti-inflammatory activities and interfere with the signaling pathway that leads to activation of transcription factor NF-ΚB. Here we explore the possibility that the NF-ΚB subunit p50 may be a target for the cyclopentenone 15-deoxy-Δ 12,14-prostaglandin J2 (15d-PGJ2). This prostaglandin inhibited the DNA binding ability of recombinant p50 in a dose-dependent manner. The inhibition required the cyclopentenone moiety and could be prevented but not reverted by glutathione and dithiothreitol. Moreover, a p50 mutant with a C62S mutation was resistant to inhibition, indicating that the effect of 15d-PGJ2 was probably due to its interaction with cysteine 62 in p50. The covalent modification of p50 by 15d-PGJ2 was demonstrated by reverse-phase high pressure liquid chromatography and mass spectrometry analysis that showed an increase in retention time and in the molecular mass of 15d-PGJ2-treated p50, respectively. The interaction between p50 and 15d-PGJ2 was relevant in intact cells. 15d-PGJ2 effectively inhibited cytokine-elicited NF-κB activity in HeLa without reducing IκBα degradation or nuclear translocation of NF-κB subunits. 15d-PGJ2 reduced NF-κB DNA binding activity in isolated nuclear extracts, suggesting a direct effect on NF-κB proteins. Finally, treatment of HeLa with biotinylated-15d-PGJ2 resulted in the formation of a 15d-PGJ 2-p50 adduct as demonstrated by neutravidin binding and immunoprecipitation. These results clearly show that p50 is a target for covalent modification by 15d-PGJ2 that results in inhibition of DNA binding. | - |
dc.language.iso | eng | - |
dc.publisher | American Society for Biochemistry and Molecular Biology | - |
dc.rights | openAccess | - |
dc.title | 15-deoxy-Δ12,14-prostaglandin J2 inhibition of NF-κB-DNA binding through covalent modification of the p50 subunit | - |
dc.type | artículo | - |
dc.identifier.doi | 10.1074/jbc.M104518200 | - |
dc.relation.publisherversion | http://dx.doi.org/10.1074/jbc.M104518200 | - |
dc.identifier.e-issn | 1083-351X | - |
dc.date.updated | 2013-06-07T11:01:26Z | - |
dc.description.version | Peer Reviewed | - |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.languageiso639-1 | en | - |
item.fulltext | With Fulltext | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.cerifentitytype | Publications | - |
item.grantfulltext | open | - |
item.openairetype | artículo | - |
Aparece en las colecciones: | (CIB) Artículos |
Ficheros en este ítem:
Fichero | Descripción | Tamaño | Formato | |
---|---|---|---|---|
J. Biol. Chem.-2001-Cernuda-Morollón-35530-6.pdf | 320,59 kB | Adobe PDF | Visualizar/Abrir |
CORE Recommender
SCOPUSTM
Citations
288
checked on 20-abr-2024
WEB OF SCIENCETM
Citations
278
checked on 24-feb-2024
Page view(s)
462
checked on 23-abr-2024
Download(s)
245
checked on 23-abr-2024
Google ScholarTM
Check
Altmetric
Altmetric
NOTA: Los ítems de Digital.CSIC están protegidos por copyright, con todos los derechos reservados, a menos que se indique lo contrario.