Proteasome inhibitors induce a terminal unfolded protein response in multiple myeloma cells.

By Esther A Obeng, L. Carlson, D. Gutman, W. Harrington, Kelvin P. Lee, L. Boise. Blood, 2006

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Systematic Functional Annotation and Visualization of Biological Networks (2016, background): “…that proteasome inactivation may cause endoplasmic reticulum (ER) stress, due to an accumulation of misfolded proteins in the ER (Lee et al., 2003; Obeng et al., 2006), it has not been anticipated that loss-of-function mutations in ER-or other vesicle-related functions could alleviate this or…”
Tumorigenic and Immunosuppressive Effects of Endoplasmic Reticulum Stress in Cancer (2017, positive): “Consequently, highly secretory cancers such as the B cell malignancy multiple myeloma, which produces extremely high levels of immunoglobulins, often undergo persistent ER stress (Obeng et al., 2006).”
Antitumor activity of PR-171, a novel irreversible inhibitor of the proteasome. (2007, background): “9, 10). The cellular mechanism(s) responsible for the clinical efficacy of bortezomib remain unclear, but may include disruption of cell adhesion– and cytokine-dependent survival pathways, in part through suppression of NF-nB activity (11, 12), inhibition of angiogenesis (13), and/or activation of a”
NF-κB in biology and targeted therapy: new insights and translational implications (2024, background): “544 FDA-approved proteasome inhibitors include bortezomib, car ﬁ lzomib, and ixazomib, which have been mainly used for the treatment of multiple myeloma, diffuse large B cell lymphoma (DLBCL), and other solid tumors.”