S-Nitrosylation links obesity-associated inflammation to endoplasmic reticulum dysfunction
| Autor: | Steven P. Gygi, Ryan C. Kunz, Gökhan S. Hotamisligil, Alessandro Arduini, Ediz S. Calay, Suneng Fu, Jason Fan, Ling Yang, Abdullah Yalcin |
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| Jazyk: | angličtina |
| Rok vydání: | 2015 |
| Předmět: |
X-Box Binding Protein 1
medicine.medical_specialty XBP1 RNA Splicing Mice Obese Nitric Oxide Synthase Type II Inflammation Context (language use) Regulatory Factor X Transcription Factors Biology Protein Serine-Threonine Kinases Diet High-Fat Endoplasmic Reticulum Article Mice Internal medicine Endoribonucleases medicine Glucose homeostasis Animals Homeostasis Obesity RNA Messenger Multidisciplinary Endoplasmic reticulum S-Nitrosylation Endoplasmic Reticulum Stress DNA-Binding Proteins Disease Models Animal Endocrinology Glucose Liver Unfolded protein response Unfolded Protein Response Nitrogen Oxides medicine.symptom Transcription Factors |
| Popis: | S-nitrosylation links obesity and cell stress Obesity and other diseases are somehow linked to malfunction of the protein-protecting functions of the endoplasmic reticulum (ER). Yang et al. propose a mechanism by which obesity and associated chronic inflammation may be linked to the accumulation of unfolded proteins in the ER. Such stress would normally trigger the process known as the unfolded protein response (UPR). However, obese mice had increased S-nitrosylation of inositol-requiring protein-1 (IRE1α), a ribonuclease that regulates the UPR. The modified IRE1α had decreased RNAse activity. The authors expressed an IRE1α mutant protein that could not be nitrosylated in the liver of obese mice. This approach improved the UPR and helped restore glucose homeostasis. Science , this issue p. 500 |
| Databáze: | OpenAIRE |
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