Startseite Medizin Trehalose protects against spinal cord injury through regulating heat shock proteins 27 and 70 and caspase-3 genes expression
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Trehalose protects against spinal cord injury through regulating heat shock proteins 27 and 70 and caspase-3 genes expression

  • Roya Nasouti , Mohammad Khaksari , Moghaddameh Mirzaee und Mahdieh Nazari-Robati EMAIL logo
Veröffentlicht/Copyright: 7. Oktober 2019

Abstract

Background

Heat shock proteins (HSPs) are a class of highly conserved proteins responsible for various functions critical to cell survival. Pharmacological induction of HSPs has been implicated in the regulation of neuronal loss and functional deficits in peripheral and central nervous system injuries. Accordingly, the present study was conducted to investigate the effect of trehalose on spinal expression of HSP27, HSP70 and caspase-3 genes following traumatic spinal cord injury (SCI) in rats.

Methods

Male rats weighing 250–300 g underwent laminectomy and were divided into four groups including sham, SCI (received SCI), vehicle (received SCI and phosphate buffer saline intrathecally) and trehalose (received 10 mM trehalose intrathecally following SCI). On days 1, 3 and 7 after injury, HSP27, HSP70 and caspase-3 genes transcripts were quantified in spinal cord tissues via a real-time PCR technique. In addition, locomotor function was assessed using the Basso, Beattie and Bresnahan (BBB) rating scale.

Results

SCI induced the expression of HSP27, HSP70 and caspase-3 genes and BBB score at all time points. Trehalose treatment upregulated HSP27, HSP70 genes expression at 1 day after SCI. Interestingly, a significant reduction in the expression of HSP27 and HSP70 genes was observed on days 3 and 7 following trauma compared with the vehicle group (p < 0.01). Caspase-3 gene showed a decrease in expression in the trehalose-treated group at all times. In addition, neurological function revealed an improvement after treatment with trehalose.

Conclusion

This study suggests that the neuroprotective effect of trehalose is mediated via regulation of HSP27 and HSP70, which are involved in cytoprotection and functional recovery following SCI.

  1. Author contributions: All the authors have accepted responsibility for the entire content of this manuscript and approved its submission.

  2. Research funding: This work was supported by Kerman University of Medical Sciences, Funder Id: http://dx.doi.org/10.13039/501100004621, grant 96-961.

  3. Employment or Leadership: None declared.

  4. Honorarium: None declared.

  5. Competing interests: The authors state no conflicts of interest.

  6. Ethical approval: All experiments were approved by the Ethics Committee of Kerman University of Medical Sciences (IR.KMU.REC.1397.017) and were according to National Institutes of Health (NIH) guidelines for laboratory care and safety.

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Received: 2018-12-24
Accepted: 2019-08-11
Published Online: 2019-10-07

© 2020 Walter de Gruyter GmbH, Berlin/Boston

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