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Changes in HSP gene and protein expression in natural scrapie with brain damage.

Serrano C, Bolea R, Lyahyai J, Filali H, Varona L, Marcos-Carcavilla A, Acín C, Calvo JH, Serrano M, Badiola JJ, Zaragoza P, Martín-Burriel I - Vet. Res. (2011)

Bottom Line: 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.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.

View Article: PubMed Central - HTML - PubMed

Affiliation: Laboratorio de Genética Bioquímica (LAGENBIO), Facultad de Veterinaria, Universidad de Zaragoza, Miguel Servet 177, 50013 Zaragoza, Spain. minma@unizar.es.

ABSTRACT
Heat 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 over-expressed 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.

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Gene expression profiles of four chaperone genes (HSP27, HSP72, HSP73, and HSP90) in four CNS areas of control (grey bars) and scrapie (black bars) sheep in the medulla oblongata (a), diencephalon (b), prefrontal cortex (c), and cerebellum (d). Differences between groups were analysed using the Student's t-test (*p < 0.05, **p < 0.01).
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Figure 1: Gene expression profiles of four chaperone genes (HSP27, HSP72, HSP73, and HSP90) in four CNS areas of control (grey bars) and scrapie (black bars) sheep in the medulla oblongata (a), diencephalon (b), prefrontal cortex (c), and cerebellum (d). Differences between groups were analysed using the Student's t-test (*p < 0.05, **p < 0.01).

Mentions: The expression of the four HSP genes was analysed in four different areas of the central nervous system of scrapie-infected and control sheep. As Figure 1 shows, different gene expression profiles were observed in the analysed areas. Whereas changes in transcript levels were not observed in the cerebellum and medulla oblongata, significant decreases in HSP27 (p < 0.05) and HSP90 (p < 0.01) were detected in the prefrontal cortices of scrapie animals. In contrast, HSP73 was significantly over-expressed (p < 0.05) in infected diencephalons.


Changes in HSP gene and protein expression in natural scrapie with brain damage.

Serrano C, Bolea R, Lyahyai J, Filali H, Varona L, Marcos-Carcavilla A, Acín C, Calvo JH, Serrano M, Badiola JJ, Zaragoza P, Martín-Burriel I - Vet. Res. (2011)

Gene expression profiles of four chaperone genes (HSP27, HSP72, HSP73, and HSP90) in four CNS areas of control (grey bars) and scrapie (black bars) sheep in the medulla oblongata (a), diencephalon (b), prefrontal cortex (c), and cerebellum (d). Differences between groups were analysed using the Student's t-test (*p < 0.05, **p < 0.01).
© Copyright Policy - open-access
Related In: Results  -  Collection

License
Show All Figures
getmorefigures.php?uid=PMC3037893&req=5

Figure 1: Gene expression profiles of four chaperone genes (HSP27, HSP72, HSP73, and HSP90) in four CNS areas of control (grey bars) and scrapie (black bars) sheep in the medulla oblongata (a), diencephalon (b), prefrontal cortex (c), and cerebellum (d). Differences between groups were analysed using the Student's t-test (*p < 0.05, **p < 0.01).
Mentions: The expression of the four HSP genes was analysed in four different areas of the central nervous system of scrapie-infected and control sheep. As Figure 1 shows, different gene expression profiles were observed in the analysed areas. Whereas changes in transcript levels were not observed in the cerebellum and medulla oblongata, significant decreases in HSP27 (p < 0.05) and HSP90 (p < 0.01) were detected in the prefrontal cortices of scrapie animals. In contrast, HSP73 was significantly over-expressed (p < 0.05) in infected diencephalons.

Bottom Line: 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.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.

View Article: PubMed Central - HTML - PubMed

Affiliation: Laboratorio de Genética Bioquímica (LAGENBIO), Facultad de Veterinaria, Universidad de Zaragoza, Miguel Servet 177, 50013 Zaragoza, Spain. minma@unizar.es.

ABSTRACT
Heat 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 over-expressed 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.

Show MeSH
Related in: MedlinePlus