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Campo DC | Valor | Lengua/Idioma |
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dc.contributor.author | Berciano, María T. | - |
dc.contributor.author | Baltrons, María Antonia | - |
dc.contributor.author | Pifarré, Paula | - |
dc.contributor.author | Lafarga, Miguel | - |
dc.contributor.author | García, Agustina | - |
dc.date.accessioned | 2008-06-20T10:07:20Z | - |
dc.date.available | 2008-06-20T10:07:20Z | - |
dc.date.issued | 2007-07-25 | - |
dc.identifier.citation | BMC Pharmacology 2007, 7(Suppl 1):P3 | en_US |
dc.identifier.issn | 1471-2210 | - |
dc.identifier.uri | http://hdl.handle.net/10261/5211 | - |
dc.description | From 3rd International Conference on cGMP Generators, Effectors and Therapeutic Implications.-- This abstract is available from: http://www.biomedcentral.com/1471-2210/7/S1/P3 | en_US |
dc.description.abstract | [Background] We have previously shown that inflammatory agents (LPS, IL-1β, β-amyloid peptides) that induce reactivity and NOS-2 expression in glial cells down-regulate astroglial soluble guanylyl cyclase (sGC) in vitro and in vivo. | en_US |
dc.description.abstract | [Results] Here we show that the decrease in sGC activity and β1 subunit protein induced by LPS (10 ng/ml, 24 h) in cultured rat cerebellar astrocytes is prevented by inhibitors of proteasome activity (MG132 5 μM; lactacystin 10 μM) whereas other protease inhibitors (calpain inhibitor 25 μM; ICE inhibitor II 100 μM and leupeptin 5 μM) were not effective. Furthermore, immunocytochemistry and confocal laser microscopy revealed that in LPS-treated cells a strong sGC β1 immunorreactivity is evident in aggregates in the cell nuclei where it co-localizes with 20S proteasomes and ubiquitin in clastosomes, nucleoplasmic substructures involved in ubiquitin-proteasome-dependent nuclear proteolysis, but do not colocalize with others proteasome-enriched structures include promyelocytic leukaemia bodies and splicing speckles. In contrast, in untreated astrocytes clastosomes are scarce and sGC β1 immunorectivity shows a diffuse cytoplasmic pattern, while in the nucleus it is very weak. A similar distribution is observed when cells are treated with LPS and the proteasome inhibitor MG132 or the protein synthesis inhibitor cycloheximide. | en_US |
dc.description.abstract | [Conclusion] LPS orchestrates the recruitment of sGC-β1 protein and components of the ubiquitin-proteasome system to specialized nuclear bodies, clastosomes, suggesting a mechanism for inflammation-induced down-regulation of sGC in astrocytes. | en_US |
dc.description.sponsorship | This work was supported by a SAF2004-01717 grant (Spain). | en_US |
dc.format.extent | 151184 bytes | - |
dc.format.mimetype | application/pdf | - |
dc.language.iso | eng | en_US |
dc.publisher | BioMed Central | en_US |
dc.relation.isversionof | Publisher's version | - |
dc.rights | openAccess | en_US |
dc.title | LPS-induced down-regulation of NO-sensitive guanylyl cyclase in astrocytes occurs by proteasomal degradation in nuclear bodies | en_US |
dc.type | artículo | en_US |
dc.identifier.doi | 10.1186/1471-2210-7-S1-P3 | - |
dc.description.peerreviewed | Peer reviewed | en_US |
dc.type.coar | http://purl.org/coar/resource_type/c_6501 | es_ES |
item.openairetype | artículo | - |
item.grantfulltext | open | - |
item.cerifentitytype | Publications | - |
item.openairecristype | http://purl.org/coar/resource_type/c_18cf | - |
item.fulltext | With Fulltext | - |
item.languageiso639-1 | en | - |
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