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- W2161108553 endingPage "262" @default.
- W2161108553 startingPage "235" @default.
- W2161108553 abstract "The proper folding, assembly, and maintenance of cellular proteins is a highly regulated process and is critical for cellular homeostasis. Multiple cellular compartments have adapted their own systems to ensure proper protein folding, and quality control mechanisms are in place to manage stress due to the accumulation of unfolded proteins. When the accumulation of unfolded proteins exceeds the capacity to restore homeostasis, these systems can result in a cell death response. Unfolded protein accumulation in the endoplasmic reticulum (ER) leads to ER stress with activation of the unfolded protein response (UPR) governed by the activating transcription factor 6 (ATF6), inositol requiring enzyme-1 (IRE1), and PKR-like endoplasmic reticulum kinase (PERK) signaling pathways. Many xenobiotics have been shown to influence ER stress and UPR signaling with either pro-survival or pro-death features. The ultimate outcome is dependent on many factors including the mechanism of action of the xenobiotic, concentration of xenobiotic, duration of exposure (acute vs. chronic), cell type affected, nutrient levels, oxidative stress, state of differentiation, and others. Assessing perturbations in activation or inhibition of ER stress and UPR signaling pathways are likely to be informative parameters to measure when analyzing mechanisms of action of xenobiotic-induced toxicity." @default.
- W2161108553 created "2016-06-24" @default.
- W2161108553 creator A5015505628 @default.
- W2161108553 creator A5040038736 @default.
- W2161108553 creator A5067269768 @default.
- W2161108553 date "2013-01-18" @default.
- W2161108553 modified "2023-10-16" @default.
- W2161108553 title "Xenobiotic Perturbation of ER Stress and the Unfolded Protein Response" @default.
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