دورية أكاديمية

mTORC1‐mediated amino acid signaling is critical for cell fate determination under transplant‐induced stress.

التفاصيل البيبلوغرافية
العنوان: mTORC1‐mediated amino acid signaling is critical for cell fate determination under transplant‐induced stress.
المؤلفون: Cheng, Xiaoyan, Ge, Maolin, Zhu, Shouhai, Li, Dan, Wang, Ruiheng, Xu, Qiongyu, Chen, Zhihong, Xie, Shufeng, Liu, Han
المصدر: FEBS Letters; Feb2021, Vol. 595 Issue 4, p462-475, 14p
مصطلحات موضوعية: CELL determination, AMINO acids, PROTEIN synthesis, CELL death, CELL cycle
مستخلص: Transplantation of in vitro‐manipulated cells is widely used in hematology. While transplantation is well recognized to impose severe stress on transplanted cells, the nature of transplant‐induced stress remains elusive. Here, we propose that the lack of amino acids in serum is the major cause of transplant‐induced stress. Mechanistically, amino acid deficiency decreases protein synthesis and nutrient consummation. However, in cells with overactive AKT and ERK, mTORC1 is not inhibited and protein synthesis remains relatively high. This impaired signaling causes nutrient depletion, cell cycle block, and eventually autophagy and cell death, which can be inhibited by cycloheximide or mTORC1 inhibitors. Thus, mTORC1‐mediated amino acid signaling is critical in cell fate determination under transplant‐induced stress, and protein synthesis inhibition can improve transplantation efficiency. [ABSTRACT FROM AUTHOR]
Copyright of FEBS Letters is the property of Wiley-Blackwell and its content may not be copied or emailed to multiple sites or posted to a listserv without the copyright holder's express written permission. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
قاعدة البيانات: Complementary Index
الوصف
تدمد:00145793
DOI:10.1002/1873-3468.14008