Protein misfolding, amyloid formation, and neurodegeneration: a critical role for molecular chaperones?

Neuron. 2002 Jul 3;35(1):9-12. doi: 10.1016/s0896-6273(02)00761-4.

Abstract

The most conspicuous feature of many neurodegenerative disorders, including Alzheimer's, Parkinson's, and Huntington's disease, is the occurrence of protein aggregates in ordered fibrillar structures known as amyloid found inside and outside of brain cells. The appearance of aggregates in diseased brains implies an underlying incapacity in the cellular machinery of molecular chaperones that normally functions to prevent the accumulation of misfolded proteins. Here we review recent studies that have revealed a critical role for molecular chaperones in several neurodegenerative disorders.

Publication types

  • Review

MeSH terms

  • Amyloid / genetics
  • Amyloid / metabolism*
  • Animals
  • Brain / metabolism*
  • Brain / pathology
  • Brain / physiopathology
  • Disease Models, Animal
  • Humans
  • Molecular Chaperones / genetics
  • Molecular Chaperones / metabolism*
  • Neurodegenerative Diseases / genetics*
  • Neurodegenerative Diseases / metabolism*
  • Neurodegenerative Diseases / pathology
  • Neurofibrillary Tangles / genetics
  • Neurofibrillary Tangles / metabolism
  • Neurofibrillary Tangles / pathology
  • Neurons / metabolism*
  • Neurons / pathology
  • Peptides / genetics
  • Peptides / metabolism
  • Protein Folding*

Substances

  • Amyloid
  • Molecular Chaperones
  • Peptides
  • polyglutamine