Unfolded protein stress in the endoplasmic reticulum and mitochondria: A role in neurodegeneration
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Fecha
2012
Autores
Profesor/a Guía
Facultad/escuela
Idioma
en
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Título del volumen
Editor
Frontiers Media S.A.
Nombre de Curso
Licencia CC
Attribution-NonCommercial 3.0 Unported (CC BY-NC 3.0)
Licencia CC
Resumen
Protein-folding occurs in several intracellular locations including the endoplasmic reticulum and mitochondria. In normal conditions there is a balance between the levels of unfolded proteins and protein folding machinery. Disruption of homeostasis and an accumulation of unfolded proteins trigger stress responses, or unfolded protein responses (UPR), in these organelles. These pathways signal to increase the folding capacity, inhibit protein import or expression, increase protein degradation, and potentially trigger cell death. Many aging-related neurodegenerative diseases involve the accumulation of misfolded proteins in both the endoplasmic reticulum and mitochondria. The exact participation of the UPRs in the onset of neurodegeneration is unclear, but there is significant evidence for the alteration of these pathways in the endoplasmic reticulum and mitochondria. Here we will discuss the involvement of endoplasmic reticulum and mitochondrial stress and the possible contributions of the UPR in these organelles to the development of two neurodegenerative diseases, Parkinson's disease (PD) and Alzheimer's disease (AD).
Notas
Indexación: Scopus.
Palabras clave
Alzheimer's disease, Endoplasmic reticulum, Mitochondria, Neurodegeneration, Parkinson's disease, Unfolded protein response
Citación
Frontiers in Aging Neuroscience, Volume 4, Issue APR, Pages 1 - 13, 2012
DOI
10.3389/fnagi.2012.00005