Dicarbonyl stress, protein glycation and the unfolded protein response

• Published in: Glycoconjugate journal Vol. 38; no. 3; pp. 331 - 340
• Main Authors: Rabbani, Naila, Xue, Mingzhan, Thornalley, Paul J.
• Format: Journal Article
• Language: English
• Published: New York Springer US 01.06.2021; Springer Nature B.V
• Subjects: Advances in Glycation: from food to human health and disease; Biochemistry; Biomedical and Life Sciences; Body weight; Diabetes; Diabetes mellitus (non-insulin dependent); Endothelial cells; Fibroblasts; Glucose - metabolism; Glycosylation; Heat shock proteins; Hesperidin; Humans; Hydrophobicity; Insulin; Insulin resistance; Life Sciences; Mini Review; Obesity; Overweight; Pathology; Physiology; Protein folding; Proteins; Proteins - chemistry; Pyruvaldehyde; Resveratrol; Signal Transduction; Ubiquitin; Unfolded Protein Response; Heat shock response; Methylglyoxal; Ubiquitin ligase; Glyoxalase; Insulin resistance; Low grade inflammation; Glycation; Unfolded protein response

The reactive dicarbonyl metabolite, methylglyoxal (MG), is increased in obesity and diabetes and is implicated in the development of insulin resistance, type 2 diabetes mellitus and vascular complications of diabetes. Dicarbonyl stress is the metabolic state of abnormal high MG concentration. MG is...