Misfolded proteins, endoplasmic reticulum stress and neurodegeneration

Curr Opin Cell Biol. 2004 Dec;16(6):653-62. doi: 10.1016/j.ceb.2004.09.012.

Abstract

The accumulation of misfolded proteins (e.g. mutant or damaged proteins) triggers cellular stress responses that protect cells against the toxic buildup of such proteins. However, prolonged stress due to the buildup of these toxic proteins induces specific death pathways. Dissecting these pathways should be valuable in understanding the pathogenesis of, and ultimately in designing therapy for, neurodegenerative diseases that feature misfolded proteins.

Publication types

  • Research Support, Non-U.S. Gov't
  • Research Support, U.S. Gov't, P.H.S.
  • Review

MeSH terms

  • Animals
  • Endoplasmic Reticulum / metabolism
  • Endoplasmic Reticulum / pathology*
  • Heat-Shock Proteins / metabolism
  • Humans
  • Models, Biological
  • Molecular Chaperones / metabolism
  • Neurodegenerative Diseases / pathology
  • Oxidative Stress
  • Protein Denaturation
  • Protein Folding
  • Proteins / chemistry*
  • Signal Transduction

Substances

  • Heat-Shock Proteins
  • Molecular Chaperones
  • Proteins
  • molecular chaperone GRP78