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Unfolded Protein Response and Cancer
Lihua Wu1, Mary Chou2, Shudong Zhu1
1School of Life Sciences, State Key Laboratory of Medical Genetics, Central South University, Changsha, China.
Discoveries (Craiova, Romania)
|April 21, 2020
Summary
Physiological stresses trigger the unfolded protein response (UPR) when misfolded proteins accumulate in the endoplasmic reticulum. This review discusses UPR
Area of Science:
- Molecular Biology
- Cellular Stress Response
- Oncology
Background:
- Physiological stresses like hypoxia and oxidative stress cause protein misfolding in the endoplasmic reticulum (ER).
- Failure of proteasome degradation leads to misfolded protein accumulation, initiating the unfolded protein response (UPR).
- UPR is a cellular defense mechanism involving suppressed protein synthesis and selective protein expression to restore ER homeostasis.
Purpose of the Study:
- To review the molecular mechanisms of the unfolded protein response (UPR).
- To discuss the complex roles of UPR in various stages of cancer development, including angiogenesis, cell survival, and proliferation.
Main Methods:
- Literature review of current knowledge on UPR and cancer.
- Discussion of molecular pathways involved in UPR.
- Analysis of UPR's role in tumor development.
Main Results:
- Hypoxia and UPR are initiated during tumor development.
- UPR plays multifaceted roles in cancer, influencing angiogenesis, cell survival, and proliferation.
Conclusions:
- UPR is a critical cellular process implicated in cancer development.
- Understanding UPR mechanisms is crucial for cancer research and therapy.
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