Myelin Pathology: Involvement of Molecular Chaperones and the Promise of Chaperonotherapy.
Federica ScaliaAntonella Marino GammazzaEverly Conway de MacarioAlberto J L MacarioFrancesco CappelloPublished in: Brain sciences (2019)
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.
Keyphrases
- heat shock
- white matter
- heat shock protein
- genome wide
- single molecule
- end stage renal disease
- primary care
- newly diagnosed
- clinical trial
- prognostic factors
- multiple sclerosis
- copy number
- oxidative stress
- living cells
- brain injury
- gene expression
- big data
- combination therapy
- binding protein
- study protocol
- blood brain barrier
- patient reported outcomes
- fluorescent probe
- subarachnoid hemorrhage
- open label
- cerebral ischemia
- phase iii