Unfolded protein response‐mediated modulation of mesenchymal stem cells

作者：Fataneh Tavasolian, Ahmad Zavaran Hosseini, Ali Mirzaei, Elham Abdollahi, Pouria Jandaghi, Sara Soudi, Mahmood Naderi, Ehsan Saburi, Amir Abbas Momtazi‐Borojeni, Thomas P. Johnston, Amirhossein Sahebkar · 发表于：IUBMB Life · 年份：2019 · DOI：10.1002/iub.2154 · 被引用次数：19 · 研究领域：Endoplasmic Reticulum Stress and Disease、Autophagy in Disease and Therapy、Pancreatic function and diabetes

The endoplasmic reticulum (ER) receives unfolded proteins predestined for the secretory pathway or to be incorporated as transmembrane proteins. The ER has to accommodate the proper folding and glycosylation of these proteins and also to properly incorporate transmembrane proteins. However, under various circumstances, the proteins shuttling through the ER can be misfolded and undergo aggregation, which causes activation of the unfolded protein response (UPR). The UPR is mediated through three primary pathways: activating transcription factor-6, inositol-requiring enzyme-1 (IRE1), and PKR-like endoplasmic reticulum kinase, which up-regulate ER folding chaperones and temporarily suppress protein translation. The UPR can be both cytoprotective and/or cytotoxic depending on the duration of UPR activation and the type of host cell. Proteostasis controls stem cell function, while stress responses affect stem cell identity and differentiation. The present review aimed to explore and discuss the effects of the UPR pathways on mesenchymal stem cells.