Key Laboratory of Straw Biology and Utilization, Ministry of Education Changchun City, Jilin Province 130118, China.
Jilin Agricultural University, College of Life Sciences Changchun City, Jilin Province 130118, China
Protein Pept Lett. 2020;27(9):831-840. doi: 10.2174/0929866527666200407113549.
The unfolded protein response (UPR) is a protective mechanism against endoplasmic reticulum (ER) stress that induces a series of signal transduction pathways to eliminate misfolded proteins. The UPR mechanism is highly conserved in fungi, higher organisms, plants and mammals. The UPR pathway is activated to stabilize ER functions when there are too many unfolded proteins or misfolded proteins in the ER. However, stress continues when ER proteins are stimulated by toxic substances that affect the balance of the UPR pathway, which causes changes in the structure and function of the ER and other organelles. These ultimately disrupt homeostasis in the body and cause pathological reactions that can be fatal. The UPR mechanism has clear effects on stabilizing the protein-folding environment. Dysfunction or disruption of the UPR mechanism is associated with numerous disorders, including neurodegenerative diseases, loss of control of protein secretion, cerebral ischemia and epilepsy, neuropsychiatric diseases, eye diseases, skin diseases, metabolic and inflammatory diseases, atherosclerosis, and heart disease. Thus, characterization of UPR function and its dysfunction has significant importance and has broad application prospects, which make research into the UPR a research hotspot.
未折叠蛋白反应（UPR）是一种针对内质网（ER）应激的保护机制，它诱导一系列信号转导途径来消除错误折叠的蛋白质。UPR 机制在真菌、高等生物、植物和哺乳动物中高度保守。当 ER 中存在过多的未折叠蛋白或错误折叠蛋白时，UPR 途径会被激活以稳定 ER 的功能。然而，当 ER 蛋白受到影响 UPR 途径平衡的有毒物质刺激时，应激会持续下去，这会导致 ER 和其他细胞器的结构和功能发生变化。这些最终会破坏体内的内稳态，并导致可能致命的病理性反应。UPR 机制对稳定蛋白质折叠环境有明显的作用。UPR 机制的功能障碍或破坏与许多疾病有关，包括神经退行性疾病、蛋白质分泌失控、脑缺血和癫痫、神经精神疾病、眼病、皮肤病、代谢和炎症性疾病、动脉粥样硬化和心脏病。因此，对 UPR 功能及其功能障碍的特征描述具有重要意义，具有广阔的应用前景，使 UPR 的研究成为一个研究热点。
