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Sestrin2 Overexpression Ameliorates Endoplasmic Reticulum Stress-Induced Apoptosis via Inhibiting mTOR Pathway in
Huiling Hu1,2, Zhijun Luo3, Xiuli Liu1,2
1Department of Clinical Laboratory, Sun Yat-Sen Memorial Hospital, Sun Yat-Sen University, Guangzhou, China.
International Journal of Endocrinology
|December 20, 2022
Summary
Sestrin2 protein alleviates endoplasmic reticulum (ER) stress and apoptosis in HepG2 cells. Overexpression of Sestrin2 inhibits the mTOR pathway, reducing cell death under ER stress conditions.
Area of Science:
- Cell Biology
- Molecular Biology
- Biochemistry
Background:
- Sestrin2 is a stress-inducible protein vital for cellular homeostasis.
- The role of Sestrin2 in endoplasmic reticulum (ER) stress-induced apoptosis remains unclear.
Purpose of the Study:
- To investigate Sestrin2's effect on tunicamycin (TM)-induced ER stress and apoptosis in HepG2 cells.
- To elucidate the molecular mechanisms underlying Sestrin2's role in ER stress response.
Main Methods:
- HepG2 cells were treated with tunicamycin (TM) to induce ER stress.
- Sestrin2 expression levels were analyzed.
- ER stress and apoptosis markers were assessed.
- Western blotting and TUNEL assays were performed.
- The mTOR pathway activation was investigated.
Main Results:
- Sestrin2 expression was upregulated by TM, correlating with ER stress.
- Sestrin2 overexpression reduced ER stress and inhibited apoptosis.
- Sestrin2 knockdown exacerbated TM-induced apoptosis.
- Sestrin2 overexpression suppressed TM-induced mTOR pathway activation.
Conclusions:
- Sestrin2 plays a protective role against ER stress-induced apoptosis in HepG2 cells.
- Sestrin2 ameliorates ER stress and apoptosis by inhibiting the mTOR pathway.
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