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Autophagy, mitochondria and 3‐nitropropionic acid joined in the same model
Author(s) -
GonzálezPolo Rosa A,
BravoSan Pedro José M,
GómezSánchez Rubén,
PizarroEstrella Elisa,
NisoSantano Mireia,
Fuentes José M
Publication year - 2013
Publication title -
british journal of pharmacology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 2.432
H-Index - 211
eISSN - 1476-5381
pISSN - 0007-1188
DOI - 10.1111/j.1476-5381.2012.02203.x
Subject(s) - autophagy , mitophagy , mitochondrial fission , mitochondrion , mitochondrial permeability transition pore , huntingtin , microbiology and biotechnology , mitochondrial fusion , mptp , programmed cell death , biology , huntingtin protein , mitochondrial dna , dnaja3 , apoptosis , gene , genetics , neuroscience , mutant , dopaminergic , dopamine
Huntington's disease (HD) is a neurodegenerative disorder caused by a mutation in the gene encoding the huntingtin protein. Although the precise mechanism by which neuronal degeneration occurs is still unclear, several elements are important to its development: (1) altered gene expression and protein synthesis, (2) mitochondrial damage and (3) improper regulation of the autophagy programme. In this issue of British Journal of Pharmacology, Galindo and co-workers provide the first evidence for a role of the mitochondrial permeability transition pore (mPTP) in mitochondrial fragmentation and autophagy activation. In a model of cell death induced by 3-nitropropionic acid (3-NP) in human neural cells, the authors describe clear functions for mPTP and Bax, but not the mitochondrial fusion/fission machinery, mitochondrial fragmentation and autophagy (mitophagy). This commentary summarises the significance of this relationship and suggests several points for future development.