Characterization of bortezomib-adapted I-45 mesothelioma cells

Zhang, Youmin; Littlejohn, James; Cui, Yu; Cao, Xuanye; Peddaboina, Chander; Smythe, W. Roy

doi:10.1186/1476-4598-9-110

Cited by 28 publications

(20 citation statements)

References 24 publications

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“…Flavonoids such as (−)-epigallocatechin-3-gallate (EGCG), apigenin, quercetin, kaempferol, myricetin have been reported to inhibit the proteasomal activity in a dose-and time-dependent manner both in vitro and in cultured leukemia cells with apigenin being among the most potent inhibitors [12]. This inhibition is associated with apoptosis induction in tumor cells, but not in normal, non-transformed cells [5]. Apigenin (4,5,7-trihydroxyflavone), a dietary phytochemical, is widely distributed in many fruits and vegetables, including parsley, onions, oranges, tea, chamomile, wheat sprouts and in some seasonings.…”

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confidence: 97%

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Apigenin manipulates the ubiquitin–proteasome system to rescue estrogen receptor-β from degradation and induce apoptosis in prostate cancer cells

et al. 2014

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Apigenin selectively inhibits proteasomal degradation of tumor suppressor ER-β by specifically inhibiting chymotrypsin-like activity of proteasome, preventing its assembly via PSMA5 and inhibiting USP14 enzyme activity in prostate cancer cells, resulting in cancer cell apoptosis. Unlike bortezomib, apigenin's actions are subtle, precise, mechanistically distinct and capable of abstaining drug resistance.

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confidence: 97%

“…the chymotrypsin-like (β-5 subunit), the trypsin-like (β-2 subunit) and the caspase-like (β-1 subunit) activities [5]. Chymotrypsin-like activity is the rate-limiting step of protein degradation [6].…”

mentioning

confidence: 99%

Apigenin manipulates the ubiquitin–proteasome system to rescue estrogen receptor-β from degradation and induce apoptosis in prostate cancer cells

et al. 2014

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“…It has been previously reported that Noxa expresses in colorectal cancers, malignant melanomas and ameloblastomas [36,37,38,39], and that it is involved in the mechanism of action of the anticancer agents bortezomib and pemetrexed [40,41,42,43,44,45,46,47]. However, the expression of Noxa in mesothelioma cells has so far not been reported.…”

Section: Discussionmentioning

confidence: 98%

Use of Anti-Noxa Antibody for Differential Diagnosis between Epithelioid Mesothelioma and Reactive Mesothelial Hyperplasia

Kushitani

Amatya²,

Mawas³

et al. 2016

Pathobiology

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Objectives: The histological differential diagnosis between epithelioid mesothelioma (EM) and reactive mesothelial hyperplasia (RMH) is not always straightforward. The aim of the present study was to search for new immunohistochemical markers to distinguish EM from RMH. Methods: We evaluated and compared the expression of apoptosis-related genes in EM and RMH by real-time RT-PCR array analysis followed by clustering of significant gene expression. Immunohistochemical staining and statistical analysis of Noxa expression in 81 cases of EM and 55 cases of RMH were performed and compared with the utility of other previously reported antibodies such as Desmin, EMA, GLUT-1, IMP-3 and CD146. Results: Noxa mRNA expression levels were found to be increased in EM when compared to RMH by RT-PCR array analysis. In the immunohistochemical analysis, Noxa showed sensitivity of 69.0%, specificity of 93.6% and positive predictive value of 93.0% as a positive marker of EM in distinguishing it from RMH, and these values were almost similar to IMP-3. Conclusion: Noxa is a marker with relatively high specificity, and can be used to distinguish EM from RMH. It would be a valuable addition to the current antibody panel used for the differential diagnosis of EM and RMH.

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“…59,60 Differences in underlying resistance mechanisms have not been convincingly elucidated. 2,[61][62][63][64][65][66][67] Recently, upregulation of P-glycoprotein could be demonstrated after CFZ, suggesting that drug transport may contribute to resistance. 68,69 …”

Section: Cfz Resistancementioning

confidence: 99%

Carfilzomib

Kortuem

Stewart

2013

Blood

185

141

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IntroductionProteasome inhibition is highly effective treatment for multiple myeloma (MM), Waldenström macroglobulinemia, low-grade nonHodgkin lymphomas, and primary amyloidosis. 1 Almost 10 years ago, the US Food and Drug Administration (FDA) approved the dipeptidyl boronic acid derivative proteasome inhibitor bortezomib (BTZ) for the treatment of refractory MM and subsequently frontline therapy for MM, thus opening the door to a new era of improved MM therapy. Indeed, disease-free and overall survival for most MM patients has been significantly extended. Nevertheless primary or secondary BTZ resistance 2 is common, and treatment is often limited by BTZ-induced, dose-limiting side effects, mostly consequent to peripheral neuropathy. 3 Although less frequent BTZ administration at lower doses and using subcutaneous delivery 4,5 may contribute to a lowered BTZ neuropathy incidence and severity without seemingly compromising efficacy, new proteasome inhibitors-the "second generation"-have now been developed and are aimed at being potentially more efficacious and less toxic. The FDA recently granted accelerated approval for carfilzomib (CFZ) injection for the treatment of patients with MM who have received at least 2 prior therapies, including BTZ and an immunomodulatory agent, and who have demonstrated disease progression on or within 60 days of the completion of last therapy. This spotlight review focuses on the data leading to drug approval and provides helpful management tips for treating physicians. Ubiquitin-proteasome pathway inhibition in MM treatmentProteasomes are present in all eukaryotic cells. 6,7 They degrade proteins 8,9 and influence a multitude of cellular processes, [10][11][12][13][14][15][16] including proliferation and DNA repair. [17][18][19] Proteasome inhibition leads to an unfolded protein stress response by accumulation of misfolded proteins in the cell, 20-22 inhibits NF-B, 23 and thus induces cell-cycle arrest 24,25 and apoptosis. [26][27][28] The (malignant) plasma cell in particular is susceptible to proteasome inhibition, even to small changes, 29 because of its inherent function in Ab production. 22,[30][31][32] The proteasomeThe constitutive 26S proteasome consists of protein-recognizing 19S regulatory particles and a 20S proteolytic core 33 that carries 3 protein-specific 29 catalytic sites: the chymotrypsin, trypsin, and caspase-like sites. 34,35 Blocking the chymotrypsin-like site is most effective in cellular growth inhibition in vitro, but coinhibition of other proteasome subunits further increases overall growth retardation. [35][36][37][38] Unique immunoproteasomes exist in cells of immune or hematopoietic origin, where the catalytic sites differ from the constitutive proteasomes. 36 These play an important role in generating antigens for MHC class I presentation. 39 Both constitutive and immunoproteasomes are expressed in MM cells and are targeted by the available inhibitors BTZ and CFZ. It has not been fully elucidated whether the anticancer effects depend on inhibition o...

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Characterization of bortezomib-adapted I-45 mesothelioma cells

Cited by 28 publications

References 24 publications

Apigenin manipulates the ubiquitin–proteasome system to rescue estrogen receptor-β from degradation and induce apoptosis in prostate cancer cells

Apigenin manipulates the ubiquitin–proteasome system to rescue estrogen receptor-β from degradation and induce apoptosis in prostate cancer cells

Use of Anti-Noxa Antibody for Differential Diagnosis between Epithelioid Mesothelioma and Reactive Mesothelial Hyperplasia

Carfilzomib

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