Premium
Unfolded protein response‐mediated modulation of mesenchymal stem cells
Author(s) -
Tavasolian Fataneh,
Hosseini Ahmad Z.,
Mirzaei Ali,
Abdollahi Elham,
Jandaghi Pouria,
Soudi Sara,
Naderi Mahmood,
Saburi Ehsan,
MomtaziBorojeni Amir Abbas,
Johnston Thomas P.,
Sahebkar Amirhossein
Publication year - 2020
Publication title -
iubmb life
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.132
H-Index - 113
eISSN - 1521-6551
pISSN - 1521-6543
DOI - 10.1002/iub.2154
Subject(s) - unfolded protein response , endoplasmic reticulum , proteostasis , microbiology and biotechnology , transmembrane protein , tunicamycin , protein kinase a , eif 2 kinase , chemistry , endoplasmic reticulum associated protein degradation , biology , kinase , biochemistry , receptor , cyclin dependent kinase 2
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.