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Endoplasmic Reticulum Stress: Triggers Microenvironmental Regulation and Drives Tumor Evolution.
Chaosheng Peng1,2, Juan Wang1,2, Shu Wang1,2
1Department of Digestive Surgery, Xijing Hospital of Digestive Diseases, Fourth Military Medical University, Xi'an, China.
Endoplasmic reticulum (ER) stress, triggered by cellular imbalances, activates the unfolded protein response (UPR). This UPR significantly impacts tumor growth, microenvironment, and treatment resistance, offering potential therapeutic targets.
Area of Science:
- Cellular Biology
- Oncology
- Molecular Medicine
Background:
- The endoplasmic reticulum (ER) is vital for protein homeostasis.
- ER stress arises from disruptions like hypoxia and oxidative stress, leading to misfolded protein accumulation.
- The unfolded protein response (UPR) is a cellular defense mechanism involving IRE1, PERK, and ATF6 sensors.
Purpose of the Study:
- To review the factors inducing ER stress.
- To elucidate the UPR signaling pathway mechanism.
- To analyze ER stress effects on the tumor microenvironment and immune cells.
Main Methods:
- Literature review of scientific papers on ER stress in the tumor microenvironment.
Main Results:
- ER stress influences tumor angiogenesis, migration, metabolism, and treatment resistance.
- Tumors leverage ER stress to modulate their evolution and the tumor microenvironment.
- ER stress impacts immune-infiltrating cells within the tumor microenvironment.
Conclusions:
- ER stress plays a critical role in tumor development and progression.
- Understanding ER stress offers novel therapeutic strategies for precision cancer treatment.
- Further research into ER stress mechanisms can yield clinical diagnostic and therapeutic applications.
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