Endoplasmic reticulum stress unfolded protein response

Endoplasmic reticulum stress or unfolded protein response. A response to an accumulation of unfolded or misfolded proteins in the lumen of the endoplasmic reticulum. The unfolded protein response (UPR) has two primary aims initially to restore normal function of the cell by halting protein translation and to activate the signaling pathways that lead to increasing the production of molecular chaperones involved in protein folding. If these objectives are not achieved within a certain time lapse or the disruption is prolonged, the UPR aims to apoptosis. 

Kawahara, T., Yanagi, H., Yura, T., and Mori, K., 1997, Endoplasmic reticulum stress-induced mRNA splicing permits synthesis of transcription factor Haclp/Ern4p that activates the unfolded protein response. Mol. Biol. Cell 8 1845-1862. 

Takayanagi S, Fukuda R, Takeuchi Y, Tsukada S, Yoshida K (2013) Gene regulatory network of unfolded protein response genes in endoplasmic reticulum stress. Cell Stress Chaperones 18(1) 11-23. doi l0.1007/sl2192-012-0351-5... 

Jager, R., Bertrand, M.J.M., Gorman, A.M., Vandenabeele, P., and Samali, A. 2012. The unfolded protein response at the crossroads of cellular life and death during endoplasmic reticulum stress. Biology of the CelPunder the Auspices of the European Cell Biology Organization, 104(5), 259-270. doi 10.1111/boc.201100055. 

Samali, A., Fitzgerald, U., Deegan, S., and Gupta, S. 2010. Methods for monitoring endoplasmic reticulum stress and the unfolded protein response. International Journal of Cell Biology. 2010, 830307. doi 10.1155/2010/830307. 

Vattemi G, Engel WK, McFerrin J et al. (2004) Endoplasmic reticulum stress and unfolded protein response in inclusion body myositis muscle. Am J Pathol 164, 1-7. 

Shen X, Zhang K, Kaufman RJ. (2004) The unfolded protein response-a stress signaling pathway of the endoplasmic reticulum. J Chem Neuroanat 28( 1-2) 79-92. 

TD alters protein processing and induces endoplasmic reticulum (ER) stress which is a response to unfolded proteins. The microsomal fractions contain 20-24% of the thiamine in the cells (Balaghi and Pearson, 1966). TD up-regulates several markers... 

Nelfinavir inhibits experimentally induced tissue degeneration and cell damage by preventing loss of the mitochondrial membrane potential and even protects mitochondria in cancer cells. However, conversely, it selectively induces a mitochondria-independent cell death mechanism in cancer cells by the so-called endoplasmic reticulum unfolded protein stress response, allowing it to act on otherwise chemoresistant cancer cells [127 ]. 

---