Abstract
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.
Highlights
Normal physiological functioning of the nervous system depends on the presence of healthy myelin
Since most proteins need chaperone assistance for maturation into a functional molecule, and as the chaperoning system is present in all tissues, it is likely that some chaperonopathies may contribute to diseases characterized by myelin pathology, with one or more myelin proteins qualitatively and/or quantitatively abnormal
There might be myelinopathies that are directly associated with mutation of a chaperone gene, whose protein might be myelinopathies that are directly associated with mutation of a chaperone gene, whose product is defective and unable to assist in the production and transport protein product is defective and unable to assist in the production and of one or more myelin proteins (Figure 1, left panel)
Summary
Normal physiological functioning of the nervous system depends on the presence of healthy myelin. In principle, be due to a mutation in a gene encoding a myelin protein, in which case we have a proteinopathy, and the involvement of molecular chaperones in the protein, in which case we have a proteinopathy, and the involvement of molecular chaperones in the mechanism of disease may not be the most determinant (Figure 1, right panel). There might be myelinopathies that are directly associated with mutation of a chaperone gene, whose protein might be myelinopathies that are directly associated with mutation of a chaperone gene, whose product (i.e., the molecular chaperone) is defective and unable to assist in the production and transport protein product (i.e., the molecular chaperone) is defective and unable to assist in the production and of one or more myelin proteins (Figure 1, left panel).
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