期刊
CRITICAL REVIEWS IN ONCOLOGY HEMATOLOGY
卷 127, 期 -, 页码 66-79出版社
ELSEVIER SCIENCE INC
DOI: 10.1016/j.critrevonc.2018.05.003
关键词
Therapeutics; Cancer; Endoplasmic Reticulum (ER) Stress; Unfolded Protein Response (UPR); SRP; ERAD; Proteostasis; Secretory Pathway
资金
- Office of the Assistant Secretary of Defense for Health Affairs through the Breast Cancer Research Program [W81XWH-15-1-0199, W81XWH-15-1-0200]
- Florida Department of Health Bankhead-Coley [4BF03]
- Collaboration of Scientists for Critical Research in Biomedicine (CSCRB, Inc.)
- UF-Health Cancer Center pilot grant
The endoplasmic reticulum (ER) is an essential organelle in eukaryotic cells, responsible for protein synthesis, folding, sorting, and transportation. ER stress is initiated when the unfolded or misfolded protein load exceeds the capacity of the ER to properly fold protein. Tumor microenvironmental conditions, such as nutrient deprivation, hypoxia, and oxidative stress perturb protein folding and trigger chronic ER stress. Cancer cells can tolerate mild ER stress, however, persistent and severe ER stress kills cancer cells by inducing their autophagy, apoptosis, necroptosis, or immunogenic cell death. Based on this rationale, many drugs have been developed for triggering irremediable ER stress in cancer cells by targeting various processes in the secretory pathway. This review discusses the mechanisms of protein targeting to the ER, the key signaling cassettes that are involved in the ER stress response, and their correlation with cancer formation and progression. Importantly, this review discusses current experimental and FDA approved anti-cancer drugs that induce ER stress, and emerging targets within the secretory pathway for the development of new anticancer drugs.
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