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Unfolded protein response to autophagy as a promising druggable target for anticancer therapy
Article first published online: 10 OCT 2012
© 2012 New York Academy of Sciences.
Annals of the New York Academy of Sciences
Volume 1271, Nutrition and Physical Activity in Aging, Obesity, and Cancer pages 20–32, October 2012
How to Cite
Suh, D. H., Kim, M.-K., Kim, H. S., Chung, H. H. and Song, Y. S. (2012), Unfolded protein response to autophagy as a promising druggable target for anticancer therapy. Annals of the New York Academy of Sciences, 1271: 20–32. doi: 10.1111/j.1749-6632.2012.06739.x
- Issue published online: 10 OCT 2012
- Article first published online: 10 OCT 2012
- endoplasmic reticulum stress;
- unfolded protein response;
- molecular targeted therapies
The endoplasmic reticulum (ER) is responsible for protein processing. In rapidly proliferating tumor cells, the ER tends to be overloaded with unfolded and misfolded proteins due to high metabolic demand. With the limited protein-folding capacity of the ER, tumor cells often suffer from more ER stress than do normal cells. Thus, cellular stress responses to cope with ER stress, such as the unfolded protein response (UPR) and autophagy, might be more activated in cancer cells than in normal cells. The complex signaling pathways from the UPR to autophagy provide promising druggable targets; a number of UPR/autophagy-targeted anticancer agents are currently in development in preclinical and clinical studies. In this short review we will discuss the potential anticancer efficacy of modulators of cellular stress responses, especially UPR and autophagy, on the basis of their signaling pathways. In addition, the current developmental status of the UPR/autophagy-targeted agents will be discussed.