Endoplasmic reticulum stress and the inflammatory basis of metabolic disease
Open accessAbstract
The endoplasmic reticulum (ER) is the major site in the cell for protein folding and trafficking and is central to many cellular functions. Failure of the ER's adaptive capacity results in activation of the unfolded protein response (UPR), which intersects with many different inflammatory and stress signaling pathways. These pathways are also critical in chronic metabolic diseases such as obesity, insulin resistance, and type 2 diabetes. The ER and related signaling networks are emerging as a potential site for the intersection of inflammation and metabolic disease.
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Oxidative stress is an initiator and major contributor to ER stress and lysosome-mediated autophagy.
“Oxidative stress has been shown to be an initiator and major contributor to both endoplasmic reticulum (ER) stress (Hotamisligil 2010; Kaneto et al. 2005) and lysosome-mediated autophagy (Lee et al. 2012)”
From Particulate matter 2.5 damages skin cells by inducing oxidative stress, subcellular organelle dysfunction, and apoptosis (2018) · cites this paper as Hotamisligil 2010
The citation to Hotamisligil is attached to ER stress, not lysosome-mediated autophagy, which has a separate citation. In “Emergence of ER Stress in Metabolic Disease” (page unavailable), the paper says ROS can cause ER stress and may help propagate it, but it does not establish oxidative stress as an initiator and major contributor. (LLM, conf=0.88)
Experimental — accuracy not yet measuredOxidative stress can lead to ER stress, characterized by unfolded protein response causing dysfunction of proteasomal degradation and autophagy, which reduces protein levels and causes imbalance in calcium homeostasis that altogether favor decrease in muscle mass.
“Oxidative stress can also lead to ER stress, which is characterized by unfolded protein response (UPR) causing dysfunction of proteasomal degradation and autophagy, which reduces protein levels and causes an imbalance in calcium homeostasis that altogether favor a decrease in muscle mass (30, 31).”
From Sarcopenic obesity: epidemiology, pathophysiology, cardiovascular disease, mortality, and management (2023) · cites this paper as [30]
ROS alter mitochondrial function and mass, increase mitochondrial DNA damage, reduce ATP synthesis, and elicit apoptotic pathway activity, which altogether lead to reduction in muscle mass.
“ROS alter mitochondrial function and mass, increase mitochondrial DNA damage, reduce ATP synthesis, and elicit apoptotic pathway activity, which altogether, lead to a reduction in muscle mass.”
From Sarcopenic obesity: epidemiology, pathophysiology, cardiovascular disease, mortality, and management (2023) · cites this paper as [30]
In the early stages of metabolic dysregulation, insulin secretion is elevated to compensate for increased glycemia; the high amount of insulin produced by the pancreas requires the endoplasmic reticulum to guarantee correct folding, generating endoplasmic reticulum overload and dysfunction, unfolded protein response overactivation, oxidative stress, and inflammation.
“In the early stages of metabolic dysregulation, insulin secretion is elevated to compensate for increased glycemia (hyperinsulinemia). The high amount of insulin produced by the pancreas requires that the ER guarantee the correct folding of the hormone, which generates an ER overload and dysfunction, an unfolded protein response (UPR) overactivation, Os, and inflammation [83, 91–95].”
From The critical role of oxidative stress in sarcopenic obesity (2021) · cites this paper as [91]
Excess nutrients, chronic inflammatory state, high adiposity, insulin resistance, metabolic syndrome, and aging harm endoplasmic reticulum function in the liver, skeletal muscle, and adipose tissue, inducing oxidative stress.
“Excess nutrients (ingesting high fat and/or high glucose), chronic inflammatory state, high adiposity, IR, metabolic syndrome, and aging harm the ER function in the liver, skeletal muscle, and adipose tissue, inducing Os [83, 91–95].”
From The critical role of oxidative stress in sarcopenic obesity (2021) · cites this paper as [91]
Endoplasmic reticulum stress is induced by reactive oxygen species accumulation, promoting oxidative stress.
“ER stress is induced by ROS accumulation, promoting Os.”
From The critical role of oxidative stress in sarcopenic obesity (2021) · cites this paper as [91]
With aging and obesity, especially abdominal obesity, insulin sensitivity gradually decreases in skeletal muscle and adipocytes, increasing serum glucose levels and promoting endoplasmic reticulum overload and oxidative stress.
“Also, with aging and obesity (especially abdominal obesity), insulin sensitivity gradually decreases in skeletal muscle and adipocytes, increasing serum glucose levels and promoting ER overload and Os [83, 91–95].”
From The critical role of oxidative stress in sarcopenic obesity (2021) · cites this paper as [91]
In the liver, imbalance in insulin metabolism negatively affects protein synthesis, lipogenesis, lipid transportation, and gluconeogenesis, inducing endoplasmic reticulum dysfunction and consequently oxidative stress.
“In the liver, the imbalance in insulin metabolism negatively affects protein synthesis, lipogenesis, lipid transportation, and gluconeogenesis, inducing ER dysfunction and, consequently, Os.”
From The critical role of oxidative stress in sarcopenic obesity (2021) · cites this paper as [91]
Obesity, metabolic syndrome, and aging cause endoplasmic reticulum stress and oxidative stress.
“Obesity, metabolic syndrome, and aging cause ER stress and Os [90–93].”
From The critical role of oxidative stress in sarcopenic obesity (2021) · cites this paper as [91]
Adipocytes from obese and insulin-resistant subjects (humans and mice) present elevated lipid storage, lipogenesis, and adipokine synthesis, all of which induce endoplasmic reticulum stress and oxidative stress.
“Also, adipocytes from obese and insulin-resistant subjects (humans and mice) present elevated lipid storage, lipogenesis, and adipokine synthesis, all of which induce ER stress and Os [83, 91, 96].”
From The critical role of oxidative stress in sarcopenic obesity (2021) · cites this paper as [91]
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- Authors
- Hotamisligil, G. S.
- Venue
- Cell
- Publisher
- Elsevier BV
- Published
- 2010-03
- Volume
- 140
- Issue
- 6
- Pages
- 900-917
- ISSN
- 0092-8674 (ISSN-L)
- PMC
- PMC2887297
- OpenAlex
- W2090556647
- Cited by
- 2,802
- References
- 153
- Citations by year
- 2026: 116 · 2025: 126 · 2024: 130 · 2023: 117 · 2022: 175 · 2021: 174 · 2020: 180 · 2019: 167 · 2018: 187 · 2017: 194 · 2016: 193 · 2015: 215 · 2014: 209 · 2013: 215 · 2012: 193
- FWCI
- 17.38
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cell (publishedVersion)
- PubMed (publishedVersion)
- PubMed Central (acceptedVersion)
- Funders
- National Institute of Diabetes and Digestive and Kidney Diseases (R01DK064360, R01DK052539, P30DK040561)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Endoplasmic Reticulum Stress and Disease
- Health Sciences › Medicine › Epidemiology › Adipokines, Inflammation, and Metabolic Diseases
- Life Sciences › Neuroscience › Sensory Systems › Ion Channels and Receptors
- Keywords
- endoplasmic reticulum stress, unfolded protein response, inflammation, metabolic disorders, obesity, insulin resistance, type 2 diabetes, protein folding, stress signaling pathways
- MeSH terms
- Animals, Endoplasmic Reticulum, Humans, Inflammation, Metabolic Diseases, Stress, Physiological, Protein Folding, Unfolded Protein Response
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