6533b7d0fe1ef96bd125adc2
RESEARCH PRODUCT
Myelin pathology: Involvement of molecular chaperones and the promise of chaperonotherapy
Federica ScaliaAlberto J. L. MacarioEverly Conway De MacarioFrancesco CappelloAntonella Marino Gammazzasubject
ChaperonotherapyMyelinopathiechaperonopathiescctlcsh:RC321-571Chaperonin03 medical and health sciencesMyelin0302 clinical medicinemedicineAxonlcsh:Neurosciences. Biological psychiatry. NeuropsychiatryGene030304 developmental biologyMyelinopathies0303 health sciencesbiologyGeneral NeuroscienceHsp60medicine.anatomical_structureMyelinChaperone (protein)PerspectiveProteinopathiesbiology.proteinChaperonopathiemyelinopathiesHSP60Neuroscience030217 neurology & neurosurgeryMyelin pathologydescription
The 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.
| year | journal | country | edition | language |
|---|---|---|---|---|
| 2019-09-26 |