Myelin pathology: Involvement of molecular chaperones and the promise of chaperonotherapy
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AbstractThe process of axon myelination involves various proteins including molecular chaperones. Myelin alteration is a common feature in neurological diseases due to structural and functional abnormalities of one or more myelin proteins. Genetic proteinopathies may occur either in the presence of a normal chaperoning system, which is unable to assist the defective myelin protein in its folding and migration, or due to mutations in chaperone genes, leading to functional defects in assisting myelin maturation/migration. The latter are a subgroup of genetic chaperonopathies causing demyelination. In this brief review, we describe some paradigmatic examples pertaining to the chaperonins Hsp60 (HSPD1, or HSP60, or Cpn60) and CCT (chaperonin-containing TCP-1). Our aim is to make scientists and physicians aware of the possibility and advantages of classifying patients depending on the presence or absence of a chaperonopathy. In turn, this subclassification will allow the development of novel therapeutic strategies (chaperonotherapy) by using molecular chaperones as agents or targets for treatment. Copyright 2019 by the authors.
SponsorsPart of this work was supported by the Italian National Operational Programme for Research and Competitiveness grant awarded to the project titled ?Cyber Brain - Polo di innovazione? (Project code: PONa3_00210, European Regional Development Fund). AJLM and ECdeM were partially supported by IMET and IEMEST. This is IMET contribution number IMET 19-017.
Identifier to cite or link to this itemhttps://www.scopus.com/inward/record.uri?eid=2-s2.0-85074424260&doi=10.3390%2fbrainsci9110297&partnerID=40&md5=60ea5f41b112ddbe53aea1389a53a345; http://hdl.handle.net/10713/11389