Unfolded Protein Response and Cancer

Lihua Wu; Mary Chou; Shudong Zhu

doi:10.15190/d.2014.2

Unfolded Protein Response and Cancer

Discoveries (Craiova). 2014 Mar 14;2(1):e10. doi: 10.15190/d.2014.2.

Authors

Lihua Wu¹, Mary Chou², Shudong Zhu¹

Affiliations

¹ School of Life Sciences, State Key Laboratory of Medical Genetics, Central South University, Changsha, China.
² Advanced Orthomolecular Research Inc., Calgary, Canada.

Abstract

Physiological stresses, such as hypoxia and oxidative stress, induce protein misfolding in the endoplasmic reticulum (ER). If proteasome degradation fails to remove the misfolded proteins, these proteins accumulate in the ER, triggering the unfolded protein response (UPR). UPR involves a series of responses, such as the suppression of global protein synthesis and the select expression of a set of proteins to reduce ER stress and restore the homeostasis of ER. In different stages of tumor development, hypoxia occurs and UPR is initiated. The roles of UPR in cancer development are complex, involving angiogenesis, cell survival and proliferation. The current knowledge of the molecular mechanisms involved in UPR, particularly its role in the development of cancer, is discussed.

Keywords: Cancer; ER stress; IRE1a; PERK; Unfolded Protein Response (UPR).

Publication types

Review