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dc.contributor.authorSerrano, Carmenes_ES
dc.contributor.authorBolea, Rosaes_ES
dc.contributor.authorLyahyai, Jaberes_ES
dc.contributor.authorFilali, Hichames_ES
dc.contributor.authorVarona, Luises_ES
dc.contributor.authorMarcos Carcavilla, Anees_ES
dc.contributor.authorAcín, Cristinaes_ES
dc.contributor.authorCalvo Lacosta, Jorge Hugoes_ES
dc.contributor.authorSerrano, Mª Magdalenaes_ES
dc.contributor.authorBadiola, Juan J.es_ES
dc.contributor.authorZaragoza Fernández, María Pilares_ES
dc.contributor.authorMartín Burriel, Inmaculadaes_ES
dc.date.accessioned2011-03-31T08:45:18Zes_ES
dc.date.available2011-03-31T08:45:18Zes_ES
dc.date.issued2011es_ES
dc.identifier.citationSerrano, C. [et al.]. Changes in HSP gene and protein expression in natural scrapie with brain damage. Veterinary Research 2011, 42:13, 12 p.es_ES
dc.identifier.urihttp://hdl.handle.net/10532/1557es_ES
dc.description.abstractHeat shock proteins (Hsp) perform cytoprotective functions such as apoptosis regulation and inflammatory response control. These proteins can also be secreted to the extracellular medium, acting as inflammatory mediators, and their chaperone activity permits correct folding of proteins and avoids the aggregation of anomalous isoforms. Several studies have proposed the implication of Hsp in prion diseases. We analysed the gene expression and protein distribution of different members of the Hsp27, Hsp70, and Hsp90 families in the central nervous system of sheep naturally infected with scrapie. Different expression profiles were observed in the areas analysed. Whereas changes in transcript levels were not observed in the cerebellum or medulla oblongata, a significant decrease in HSP27 and HSP90 was detected in the prefrontal cortex. In contrast, HSP73 was overexpressed in diencephalons of scrapie animals. Western blotting did not reveal significant differences in Hsp90 and Hsp70 protein expression between scrapie and control animals. Expression rates identified by real-time RT-PCR and western blotting were compared with the extent of classical scrapie lesions using stepwise regression. Changes in Hsp gene and protein expression were associated with prion protein deposition, gliosis and spongiosis rather than with apoptosis. Finally, immunohistochemistry revealed intense Hsp70 and Hsp90 immunolabelling in Purkinje cells of scrapie sheep. In contrast, controls displayed little or no staining in these cells. The observed differences in gene expression and protein distribution suggest that the heat shock proteins analysed play a role in the natural form of the disease.es_ES
dc.language.isoenes_ES
dc.subject.otherEnfermedades de los animaleses_ES
dc.subject.otherVariación genéticaes_ES
dc.subject.otherEncefalopatía espongiformees_ES
dc.subject.otherProteínas de shock térmicoes_ES
dc.subject.otherEnfermedades de prioneses_ES
dc.subject.otherOvinoses_ES
dc.subject.otherApoptosises_ES
dc.subject.otherSistema nervioso centrales_ES
dc.subject.otherScrapiees_ES
dc.subject.otherRespuesta inmunológicaes_ES
dc.subject.otherProducción y sanidad animales_ES
dc.titleChanges in HSP gene and protein expression in natural scrapie with brain damagees_ES
dc.typeArticlees_ES
dc.relation.publisherversionhttp://www.veterinaryresearch.org/content/42/1/13es_ES
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