Assessment of HDAC Inhibitor-Induced Endoplasmic Reticulum (ER) Stress.
Electron microscopy
Endoplasmic reticulum (ER) stress
Fluorescence microscopy
HDAC inhibitor
HDACi
Unfolded protein response (UPR)
Western blot
qPCR
Journal
Methods in molecular biology (Clifton, N.J.)
ISSN: 1940-6029
Titre abrégé: Methods Mol Biol
Pays: United States
ID NLM: 9214969
Informations de publication
Date de publication:
2023
2023
Historique:
entrez:
18
10
2022
pubmed:
19
10
2022
medline:
21
10
2022
Statut:
ppublish
Résumé
The endoplasmic reticulum (ER) is a multifunctional cell organelle which is important for the folding and processing of proteins. Different endogenous and exogenous factors can disturb the ER homeostasis, causing ER stress and activating the unfolded protein response (UPR) to remove misfolded proteins and aggregates. ER stress and the UPR are associated with several human diseases, such as diabetes, Alzheimer's or Parkinson's disease, and cancer. Histone deacetylase inhibitors (HDACi) are used to treat cancer and were shown to induce ER stress/to modulate the UPR, although the exact mechanism is not fully understood and needs further research. Several approaches to monitoring ER stress exist. Here we describe methods including qPCR, Western blot, transmission electron microscopy, and fluorescence microscopy to analyze changes in mRNA and protein expression levels as well as defects in ER structures after HDAC inhibitor-induced ER stress.
Identifiants
pubmed: 36255630
doi: 10.1007/978-1-0716-2788-4_17
doi:
Substances chimiques
Histone Deacetylase Inhibitors
0
RNA, Messenger
0
Types de publication
Journal Article
Research Support, Non-U.S. Gov't
Langues
eng
Sous-ensembles de citation
IM
Pagination
253-268Informations de copyright
© 2023. The Author(s), under exclusive license to Springer Science+Business Media, LLC, part of Springer Nature.
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