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Review ARTICLE Provisionally accepted The full-text will be published soon. Notify me

Front. Pharmacol. | doi: 10.3389/fphar.2019.00920

Heat Shock Proteins in Neuroinflammation

Brigitta Dukay1, Bálint Csoboz1 and  Melinda E. Tóth1*
  • 1Institute of Biochemistry, Biological Research Centre (MTA), Hungarian Academy of Sciences, Hungary

The heat shock response, one of the main pro-survival mechanisms of a living organism, has evolved as the biochemical response of cells to cope with heat stress. The most well-characterized aspect of the heat shock response is the accumulation of a conserved set of proteins termed heat shock proteins (HSPs). HSPs are key players in protein homeostasis acting as chaperones by aiding the folding and assembly of nascent proteins and protecting against protein aggregation. HSPs have been associated with neurological diseases in the context of their chaperone activity, as they were found to suppress the aggregation of misfolded toxic proteins. In recent times, HSPs have proven to have functions apart from the classical molecular chaperoning in that they play a role in a wider scale of neurological disorders by modulating neuronal survival, inflammation, and disease-specific signaling processes. Heat shock proteins are gaining importance based on their ability to fine-tune inflammation and act as immune modulators in various bodily fluids. However, their effect on neuroinflammation processes is not yet fully understood. In this review, we summarize the role of neuroinflammation in acute and chronic pathological conditions affecting the brain. Moreover, we seek to explore the existing literature on HSP mediated inflammatory function within the central nervous system and compare the function of these proteins when they are localized intracellularly compared to being present in the extracellular milieu.

Keywords: Neuroinflammation, Heat shock proteins, heat shock response, Diseases of the central nervous system, extracellular heat shock proteins, inflammation modulation

Received: 25 Apr 2019; Accepted: 22 Jul 2019.

Copyright: © 2019 Dukay, Csoboz and Tóth. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms.

* Correspondence: Dr. Melinda E. Tóth, Institute of Biochemistry, Biological Research Centre (MTA), Hungarian Academy of Sciences, Szeged, H-6726, Hungary,