The Emerging Role of Electrophiles as a Key Regulator for Endoplasmic Reticulum (ER) Stress.
4-hydroxynonenal
ER stress
UPR
methylmercury
nitric oxide
reactive electrophiles
Journal
International journal of molecular sciences
ISSN: 1422-0067
Titre abrégé: Int J Mol Sci
Pays: Switzerland
ID NLM: 101092791
Informations de publication
Date de publication:
10 Apr 2019
10 Apr 2019
Historique:
received:
08
03
2019
revised:
28
03
2019
accepted:
08
04
2019
entrez:
13
4
2019
pubmed:
13
4
2019
medline:
31
7
2019
Statut:
epublish
Résumé
The unfolded protein response (UPR) is activated by the accumulation of misfolded proteins in the endoplasmic reticulum (ER), which is called ER stress. ER stress sensors PERK, IRE1, and ATF6 play a central role in the initiation and regulation of the UPR; they inhibit novel protein synthesis and upregulate ER chaperones, such as protein disulfide isomerase, to remove unfolded proteins. However, when recovery from ER stress is difficult, the UPR pathway is activated to eliminate unhealthy cells. This signaling transition is the key event of many human diseases. However, the precise mechanisms are largely unknown. Intriguingly, reactive electrophilic species (RES), which exist in the environment or are produced through cellular metabolism, have been identified as a key player of this transition. In this review, we focused on the function of representative RES: nitric oxide (NO) as a gaseous RES, 4-hydroxynonenal (HNE) as a lipid RES, and methylmercury (MeHg) as an environmental organic compound RES, to outline the relationship between ER stress and RES. Modulation by RES might be a target for the development of next-generation therapy for ER stress-associated diseases.
Identifiants
pubmed: 30974903
pii: ijms20071783
doi: 10.3390/ijms20071783
pmc: PMC6480251
pii:
doi:
Substances chimiques
Molecular Chaperones
0
Types de publication
Journal Article
Review
Langues
eng
Déclaration de conflit d'intérêts
The authors declare no conflict of interest.
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