Proteasome inhibitors disrupt the unfolded protein response in myeloma cells

By Ann-Hwee Lee, N. Iwakoshi, K. Anderson, Laurie H. Glimcher. Proceedings of the National Academy of Sciences of the United States of America, 2003

642 citations recorded by the source corpus.

Subfields: Cell Biology, Epidemiology, Molecular Biology

View Paper: https://www.semanticscholar.org/paper/420f748a444e46ea4af8f42557d479828e41149e

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Citations in the corpus

The endoplasmic reticulum stress response in immunity and autoimmunity (2008, background): “Of note, unspliced XBP1 mRNA encodes the short-lived protein XBP1u, which has only 261 amino acids and is rapidly degraded by both ubiquitin -dependent and ubiquitin-independent mechanism”
Tumorigenic and Immunosuppressive Effects of Endoplasmic Reticulum Stress in Cancer (2017, positive): “Additionally, the proteasome inhibitor Bortezomib induces ER stress and CHOP expression, but paradoxically reduces XBP1 protein accumulation by diminishing IRE1α-mediated XBP1 mRNA splicing and stabilizing the dominant negative unspliced XBP1 protein (Lee et al., 2003).”
Competence and competition: the challenge of becoming a long-lived plasma cell (2006, background): “The inhibition of XBP1 in plasmacytoma cells leads to ER-stress-induced apoptosi”
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”
Regulation of plasma-cell development (2005, background): “Proteasome inhibitors suppress the activity of IRE1α, thereby impairing generation of active, processed XBP1 (Ref”
XBP1 links ER stress to intestinal inflammation and confers genetic risk for human inflammatory bowel disease (2008, positive): “Quantitative PCR was performed as in Lee et al. (2003b).”
Cell death and endoplasmic reticulum stress: disease relevance and therapeutic opportunities (2008, background): “ER stress is probably particularly relevant to the clinical activity of the proteasome inhibitor bortezomib (Velcade; Millennium/Janssen-Cilag) in multiple myelom”
Linking of autophagy to ubiquitin-proteasome system is important for the regulation of endoplasmic reticulum stress and cell viability. (2007, result): “On the other hand, we found that proteasome inhibitors could not induce XBP-1 alternative splicing (data not shown), consistent with an earlier study.(32) Furthermore, deletion of XBP-1 did not affect the punctation of GFPLC3B (Figure 8, C and D) or LC3B-II formation (Figure 8E) induced by these age”
ER Stress Sensor XBP1 Controls Anti-tumor Immunity by Disrupting Dendritic Cell Homeostasis (2015, background): “Multiple known XBP1 and UPR target genes (Acosta-Alvear et al., 2007; Lee et al., 2003b) were markedly repressed in XBP1-deficient tDCs (Figure 4A), confirming sustained ER stress in DCs infiltrating OvCa.”
DEPTOR is an mTOR Inhibitor Whose Frequent Overexpression in Multiple Myeloma Cells Promotes their Survival (2009, background): “For example, the high demand that MM cells place on the protein synthesis machinery to produce large amounts of immunoglobulins (reviewed in Shapiro-Shelef and Calame, 2004), causes a significant ER stress, which renders these cells susceptible to apoptosis induction via agents that induce further E”
Systematic Functional Annotation and Visualization of Biological Networks (2016, background): “…have suggested 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…”
The role of the unfolded protein response in tumour development: friend or foe? (2004, positive): “In vitro studies have demonstrated that when cells already experiencing ER stress are further treated with protease inhibitors, some of the protective branches of the UPR are significantly dampened because of a blockage in the IRE1-dependent splicing of XBP1 mRN”