The endoplasmic reticulum (ER) is a key organelle in eukaryotic cells, responsible for a wide range of vital functions, including the modification, folding, and trafficking of proteins, as well as the biosynthesis of lipids and the maintenance of intracellular calcium homeostasis. A variety of factors can disrupt the function of the ER, leading to the aggregation of unfolded and misfolded proteins within its confines and the induction of ER stress. A conserved cascade of signaling events known as the unfolded protein response (UPR) has evolved to relieve the burden within the ER and restore ER homeostasis. However, these processes can culminate in cell death while ER stress is sustained over an extended period and at elevated levels. This review summarizes the potential role of ER stress and the UPR in determining cell fate and function in various diseases, including cardiovascular diseases, neurodegenerative diseases, metabolic diseases, autoimmune diseases, fibrotic diseases, viral infections, and cancer. It also puts forward that the manipulation of this intricate signaling pathway may represent a novel target for drug discovery and innovative therapeutic strategies in the context of human diseases.
Keyphrases
- endoplasmic reticulum
- endoplasmic reticulum stress
- induced apoptosis
- signaling pathway
- cell death
- drug discovery
- cardiovascular disease
- estrogen receptor
- endothelial cells
- cell fate
- cell cycle arrest
- systemic sclerosis
- squamous cell carcinoma
- young adults
- single molecule
- metabolic syndrome
- binding protein
- idiopathic pulmonary fibrosis
- small molecule
- risk assessment
- papillary thyroid
- induced pluripotent stem cells