The unfolded protein response during prostate cancer development.
Accumulation of misfolded proteins in the endoplasmic reticulum (ER) induces the unfolded protein response (UPR). The UPR promotes cell survival by adjusting ER protein folding capacity but if homeostasis cannot be re-established, apoptosis is induced. The execution of life/death decisions is regulated by the three UPR branches (IRE1, PERK, ATF6) and their downstream effectors. Events that offset the balance of the UPR branches can have devastating consequences, and UPR misregulation has been correlated with various diseases, including metabolic and neurodegenerative diseases and cancer. In cancer, upregulation of the UPR is thought to provide a growth advantage to tumor cells. In contrast to this prevailing view, we report here an analysis of data obtained by others indicating that all three UPR branches appear selectively down-regulated in mouse models of prostate tumorigenesis.
So
Alex Yick-Lun
AY
MIFAB, Universidad San Sebastián,Fundación Ciencia para la Vida, Av. Zañartu 1482, Nuñoa 7780272, Santiago, Chile.
de la Fuente
Erwin
E
Walter
Peter
P
Shuman
Marc
M
Bernales
Sebastián
S
D000818:Animals; D002462:Cell Membrane / Q000378:metabolism; D004195:Disease Models, Animal; D004721:Endoplasmic Reticulum / Q000378:metabolism; D015972:Gene Expression Regulation, Neoplastic; D006801:Humans; D008297:Male; D051379:Mice; D008822:Mice, Transgenic; D008954:Models, Biological; D020411:Oligonucleotide Array Sequence Analysis / Q000379:methods; D011471:Prostatic Neoplasms / Q000378:metabolism*; D011489:Protein Denaturation; D017510:Protein Folding; D015398:Signal Transduction