CNRS UMR 5203, INSERM U661, and Montpellier 1 & 2 University, Institute of Functional Genomics, Montpellier, France; Laboratory for Diabetes Cell Therapy, Institute for Research in Biotherapy, University Hospital St-Eloi, Montpellier, France.
Laboratory for Diabetes Cell Therapy, Institute for Research in Biotherapy, University Hospital St-Eloi, Montpellier, France.
PLoS One. 2014 Mar 18;9(3):e92066. doi: 10.1371/journal.pone.0092066. eCollection 2014.
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.
泛素-蛋白酶体系统(UPS)是一种主要的细胞蛋白降解机制,在调节许多细胞功能方面发挥着关键作用。慢性高血糖介导的糖毒性对胰岛β细胞的功能和存活有害。我们的研究目的是确定蛋白酶体功能障碍是否与葡萄糖毒性条件下的β细胞凋亡有关,并评估这种功能障碍是否可以通过药理学方法纠正。因此,我们在高血糖和/或 UPS 抑制剂暴露后,测量了 GK 大鼠胰岛、INS-1E 细胞或人胰岛中的 UPS 活性。免疫印迹用于定量多泛素化蛋白,通过 CHOP 表达检测内质网(ER)应激,通过 PARP 和 caspase-3 的切割检测细胞凋亡,而通过组蛋白相关 DNA 片段测量检测总细胞死亡。在体外,我们发现慢性暴露于高葡萄糖浓度的 INS-1E 细胞显著降低了三种蛋白酶体活性 20%,并导致 caspase-3 依赖性凋亡。我们表明,通过 20%的 UPS 活性药理学阻断以同样的方式导致凋亡。事实上,两种情况下都涉及 ER 应激。这些结果在人胰岛中得到了证实,并且在高血糖 GK 大鼠胰岛中也观察到蛋白酶体活性降低。此外,我们观察到高葡萄糖处理使β细胞对蛋白酶体抑制剂的凋亡作用更加敏感。值得注意的是,高葡萄糖处理可以通过 Exendin-4 纠正蛋白酶体活性的降低,Exendin-4 也可以防止葡萄糖毒性诱导的细胞凋亡。总之,我们的研究结果揭示了蛋白酶体活性在高葡萄糖诱导的β细胞凋亡中的重要作用,可能将 ER 应激和糖毒性联系起来。这些蛋白酶体功能障碍可以通过 GLP-1 类似物逆转。因此,UPS 可能是治疗导致 2 型糖尿病的有害代谢状况的有效靶点。