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http://dspace.mediu.edu.my:8181/xmlui/handle/10261/5211Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.creator | Berciano, María T. | - |
| dc.creator | Baltrons, María Antonia | - |
| dc.creator | Pifarré, Paula | - |
| dc.creator | Lafarga, Miguel | - |
| dc.creator | García, Agustina | - |
| dc.date | 2008-06-20T10:07:20Z | - |
| dc.date | 2008-06-20T10:07:20Z | - |
| dc.date | 2007-07-25 | - |
| dc.date.accessioned | 2017-01-31T01:44:50Z | - |
| dc.date.available | 2017-01-31T01:44:50Z | - |
| dc.identifier | BMC Pharmacology 2007, 7(Suppl 1):P3 | - |
| dc.identifier | 1471-2210 | - |
| dc.identifier | http://hdl.handle.net/10261/5211 | - |
| dc.identifier | 10.1186/1471-2210-7-S1-P3 | - |
| dc.identifier.uri | http://dspace.mediu.edu.my:8181/xmlui/handle/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 | - |
| dc.description | [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. | - |
| dc.description | [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. | - |
| dc.description | [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. | - |
| dc.description | This work was supported by a SAF2004-01717 grant (Spain). | - |
| dc.description | Peer reviewed | - |
| dc.format | 151184 bytes | - |
| dc.format | application/pdf | - |
| dc.language | eng | - |
| dc.publisher | BioMed Central | - |
| dc.relation | Publisher’s version | - |
| dc.rights | openAccess | - |
| dc.title | LPS-induced down-regulation of NO-sensitive guanylyl cyclase in astrocytes occurs by proteasomal degradation in nuclear bodies | - |
| dc.type | Artículo | - |
| Appears in Collections: | Digital Csic | |
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