Department of Orthopaedics, The First Affiliated Hospital of Soochow University, Suzhou, China.
Department of Endocrinology and Metabolism, Shanghai Genenal Hospital, Shanghai Jiao Tong University, Shanghai, China.
Cell Biol Int. 2021 Jun;45(6):1316-1326. doi: 10.1002/cbin.11574. Epub 2021 Mar 3.
Hyperglycemia can drive advanced glycation end product (AGE) accumulation and associated nucleus pulposus cell (NPC) dysfunction, but the basis for this activity has not been elucidated. Hypoxia-inducible factor-1α (HIF-1α) is subject to cell-type-specific AGE-mediated regulation. In the current study, we assessed the mechanistic relationship between AGE accumulation and HIF-1α degradation in NPCs. Immunohistochemical staining of degenerated nucleus pulposus (NP) samples was used to assess AGE levels. AGE impact on NPC survival and glycolysis-related gene expression was assessed via 3-(4,5)-dimethylthiazol(-z-y1)-3,5-di-phenyltetrazolium bromide assay and quantitative reverse-transcription polymerase chain reaction (qRT-PCR), while HIF-1α expression in NPCs following AGE treatment was monitored via Western blot analysis and qRT-PCR. Additionally, a luciferase reporter assay was used to monitor HIF-1α transcriptional activity. The importance of the receptor for activated C-kinase 1 (RACK1) as a mediator of HIF-1α degradation was evaluated through gain- and loss-of-function experiments. Competitive binding of RACK1 and HSP90 to HIF-1α was evaluated via immunoprecipitation. Increased AGE accumulation was evident in NP samples from diabetic patients, and AGE treatment resulted in reduced HIF-1α protein levels in NPCs that coincided with reduced HIF-1α transcriptional activity. AGE treatment impaired the stability of HIF-1α, leading to its RACK1-mediated proteasomal degradation in a manner independent of the canonical PHD-mediated degradation pathway. Additionally, RACK1 competed with HSP90 for HIF-1α binding following AGE treatment. AGE treatment of NPCs leads to HIF-1α protein degradation. RACK1 competes with HSP90 for HIF-1α binding following AGE treatment, resulting in posttranslational HIF-1α degradation. These results suggest that AGE is an intervertebral disc degeneration risk factor, and highlight potential avenues for the treatment or prevention of this disease.
高血糖可导致晚期糖基化终产物(AGE)积累和相关核髓核细胞(NPC)功能障碍,但这种活性的基础尚未阐明。缺氧诱导因子-1α(HIF-1α)受到细胞类型特异性 AGE 介导的调节。在本研究中,我们评估了 NPC 中 AGE 积累与 HIF-1α降解之间的机制关系。通过免疫组织化学染色评估退变核髓核(NP)样本中的 AGE 水平。通过 3-(4,5)-二甲基噻唑(-z-y1)-3,5-二苯基四唑溴盐(MTT)测定和定量逆转录聚合酶链反应(qRT-PCR)评估 AGE 对 NPC 存活和糖酵解相关基因表达的影响,同时通过 Western blot 分析和 qRT-PCR 监测 NPC 中 AGE 处理后的 HIF-1α表达。此外,使用荧光素酶报告基因测定监测 HIF-1α转录活性。通过增益和失能实验评估激活 C 激酶 1(RACK1)受体作为 HIF-1α降解介质的重要性。通过免疫沉淀评估 RACK1 和 HSP90 与 HIF-1α 的竞争性结合。在糖尿病患者的 NP 样本中观察到 AGE 积累增加,AGE 处理导致 NPC 中 HIF-1α 蛋白水平降低,同时 HIF-1α 转录活性降低。AGE 处理损害了 HIF-1α 的稳定性,导致其在 RACK1 介导的蛋白酶体降解途径中独立于经典 PHD 介导的降解途径。此外,AGE 处理后,RACK1 与 HSP90 竞争与 HIF-1α 结合。AGE 处理 NPC 导致 HIF-1α 蛋白降解。AGE 处理后,RACK1 与 HSP90 竞争与 HIF-1α 结合,导致 HIF-1α 翻译后降解。这些结果表明 AGE 是椎间盘退变的危险因素,并强调了治疗或预防这种疾病的潜在途径。