Proteasome dysfunction mediates high glucose-induced apoptosis in rodent beta cells and human islets.
PLoS One · 2014
Last updated 2026-05-28In lab tests, high blood sugar reduced the activity of a cell-cleanup system called the proteasome by 20% in rodent and human insulin-producing cells, leading to cell stress and a form of programmed cell death. Blocking the same cleanup system by 20% also triggered the same stress and death pathway. Treating the cells with Exendin-4, a GLP-1 drug, restored proteasome activity and protected the cells from high-glucose damage.
AI summary of the abstract below.
| Journal | PLoS One, 2014 |
|---|---|
| Citations | 43 |
| Relative citation ratio | 1.38 |
| NIH percentile | 61 |
| Molecules | — |
| Conditions studied | Type 2 Diabetes |
Abstract
The ubiquitin/proteasome system (UPS), a major cellular protein degradation machinery, plays key roles in the regulation of many cell functions. Glucotoxicity mediated by chronic hyperglycaemia is detrimental to the function and survival of pancreatic beta cells. The aim of our study was to determine whether proteasome dysfunction could be involved in beta cell apoptosis in glucotoxic conditions, and to evaluate whether such a dysfunction might be pharmacologically corrected. Therefore, UPS activity was measured in GK rats islets, INS-1E beta cells or human islets after high glucose and/or UPS inhibitor exposure. Immunoblotting was used to quantify polyubiquitinated proteins, endoplasmic reticulum (ER) stress through CHOP expression, and apoptosis through the cleavage of PARP and caspase-3, whereas total cell death was detected through histone-associated DNA fragments measurement. In vitro, we found that chronic exposure of INS-1E cells to high glucose concentrations significantly decreases the three proteasome activities by 20% and leads to caspase-3-dependent apoptosis. We showed that pharmacological blockade of UPS activity by 20% leads to apoptosis in a same way. Indeed, ER stress was involved in both conditions. These results were confirmed in human islets, and proteasome activities were also decreased in hyperglycemic GK rats islets. Moreover, we observed that a high glucose treatment hypersensitized beta cells to the apoptotic effect of proteasome inhibitors. Noteworthily, the decreased proteasome activity can be corrected with Exendin-4, which also protected against glucotoxicity-induced apoptosis. Taken together, our findings reveal an important role of proteasome activity in high glucose-induced beta cell apoptosis, potentially linking ER stress and glucotoxicity. These proteasome dysfunctions can be reversed by a GLP-1 analog. Thus, UPS may be a potent target to treat deleterious metabolic conditions leading to type 2 diabetes.
Verbatim abstract via PubMed 24642635 ↗