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dc.contributor.authorAlberti, Giusi
dc.contributor.authorPaladino, Letizia
dc.contributor.authorVitale, Alessandra Maria
dc.contributor.authorCaruso Bavisotto, Celeste
dc.contributor.authorConway de Macario, Everly
dc.contributor.authorCampanella, Claudia
dc.contributor.authorMacario, Alberto J.L.
dc.contributor.authorMarino Gammazza, Antonella
dc.date.accessioned2021-01-26T15:28:53Z
dc.date.available2021-01-26T15:28:53Z
dc.date.issued2021-01-02
dc.identifier.urihttp://hdl.handle.net/10713/14416
dc.description.abstractNeuroinflammation is implicated in central nervous system (CNS) diseases, but the molecular mechanisms involved are poorly understood. Progress may be accelerated by developing a comprehensive view of the pathogenesis of CNS disorders, including the immune and the chaperone systems (IS and CS). The latter consists of the molecular chaperones; cochaperones; and chaperone cofactors, interactors, and receptors of an organism and its main collaborators in maintaining protein homeostasis (canonical function) are the ubiquitin–proteasome system and chaperone-mediated autophagy. The CS has also noncanonical functions, for instance, modulation of the IS with induction of proinflammatory cytokines. This deserves investigation because it may be at the core of neu-roinflammation, and elucidation of its mechanism will open roads toward developing efficacious treatments centered on molecular chaperones (i.e., chaperonotherapy). Here, we discuss information available on the role of three members of the CS—heat shock protein (Hsp)60, Hsp70, and Hsp90—in IS modulation and neuroinflammation. These three chaperones occur intra-and extracellularly, with the latter being the most likely involved in neuroinflammation because they can interact with the IS. We discuss some of the interactions, their consequences, and the molecules involved but many aspects are still incompletely elucidated, and we hope that this review will encourage research based on the data presented to pave the way for the development of chaperonotherapy. This may consist of blocking a chaperone that promotes destructive neuroinflammation or replacing or boosting a defective chaperone with cytoprotective activity against neurodegeneration. © 2021 by the authors.en_US
dc.description.urihttps://doi.org/10.3390/app11020736en_US
dc.language.isoenen_US
dc.publisherMDPI AGen_US
dc.relation.ispartofApplied Sciences (Switzerland)en_US
dc.subjectAlzheimer’s diseaseen_US
dc.subjectAmyotrophic lateral sclerosisen_US
dc.subjectChaperone systemen_US
dc.subjectChaperonopathiesen_US
dc.subjectChaperonotherapyen_US
dc.subjectMolecular chaperonesen_US
dc.subjectMultiple sclerosisen_US
dc.subjectParkinson’s diseaseen_US
dc.subjectHuntington’s diseaseen_US
dc.titleFunctions and therapeutic potential of extracellular hsp60, hsp70, and hsp90 in neuroinflammatory disordersen_US
dc.typeArticleen_US
dc.identifier.doi10.3390/app11020736
dc.source.volume11
dc.source.issue2
dc.source.beginpage1
dc.source.endpage13


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