Research

Hormonal

Endoplasmic Reticulum (ER) stress, triggered by nutrient excess, activates the Unfolded Protein Response (UPR), which intersects with inflammatory pathways (via IRE-1, PERK, and ATF6) to inhibit insulin signaling and promote metabolic dysfunction.

Excess nutrients can overwhelm the cell's ability to process proteins, causing 'ER stress.' This stress activates specific cellular pathways (UPR) that interfere with insulin signaling. Managing caloric intake and reducing metabolic load can help alleviate this cellular stress.

GoodSupportsHIGH confidence
The UPR consists of 3 main branches controlled by the ER membrane proteins inositol-requiring enzyme (IRE)-1, protein kinase-like ER kinase (PERK), and activating transcription factor (ATF)-6. In response to changes in the protein-folding status within the ER, these proteins activate distinct and sometimes overlapping pathways.
Sarah Hummasti et al. · Circulation Research · 2010

Why this rating

The paper reviews extensive evidence linking ER stress to metabolic disease, including genetic studies.

Source

Endoplasmic Reticulum Stress and Inflammation in Obesity and Diabetes

Sarah Hummasti et al. · Circulation Research · 2010

DOI 10.1161/circresaha.110.225698

narrative_reviewCited 428×
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DOI resolved against Crossref · corpus check 2026-06-10

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