Proteasome activator subunit 3 promotes pancreatic cancer growth via c-Myc-glycolysis signaling axis

Guo, Jiefang; Hao, Jun; Jiang, Hongbin; Jin, Jing; H, Wu; Jin, Zhendong; Li, Zhao‐Shen

doi:10.1016/j.canlet.2016.08.018

Cited by 47 publications

(38 citation statements)

References 29 publications

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“…PA28γ physically binds to SIRT1 and then promotes its ubiquitin‐independent degradation. Furthermore, PA28γ is upregulated in many cancers, including thyroid (Okamura et al, ), colorectal (Roessler et al, ), pancreatic (Guo et al, ), breast (Wang et al, ; Chai et al, ) and ovarian cancer (Wang et al, ). Upregulation of circulating PA28γ is detected in the sera of patients with rheumatoid arthritis, Sjögren's syndrome, connective‐tissue diseases, and adult‐onset Still's disease (Gruner et al, ).…”

Section: Substrate‐recognizing Receptors On Proteasomesmentioning

confidence: 99%

Substrate receptors of proteasomes

2018

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Proteasomes are responsible for the turnover of most cellular proteins, and thus are critical to almost all cellular activities. A substrate entering the proteasome must first bind to a substrate receptor. Substrate receptors can be classified as ubiquitin receptors and non-ubiquitin receptors. The intrinsic ubiquitin receptors, including proteasome regulatory particle base subunits 1, 10 and 13 (Rpn1, Rpn10, and Rpn13), determine the capability of the proteasome to recognize a ubiquitin chain, and thus provide selectivity for the 26S proteasome. However, the non-ubiquitin receptors, including proteasome activator 200 (PA200) and PA28γ, have received great attention due to their remarkable compensatory roles relative to canonical ubiquitin-mediated proteasomal degradation. Herein we review recent advances in understanding the contributions of these substrate receptors to proteasomal degradation, and introduce their substrates and interacting factors. We also provide insights into their biological functions related to spermatogenesis, immune responses, cellular homeostasis, and tumour development. Finally, we summarize advances in developing small-molecule inhibitors of these substrate receptors and discuss their potential as drug targets.

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Section: Substrate‐recognizing Receptors On Proteasomesmentioning

confidence: 99%

Substrate receptors of proteasomes

2018

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“…HIF1α stimulates aerobic glycolysis by inducing the expression of glucose transporters (such as glucose transporter 1, GLUT1) and directly targeting enzymes that regulate glycolysis, such as hexokinase 2 (HK2), phosphoglycerate kinase 1 (PGK1), lactate dehydrogenase A (LDHA), monocarboxylate transporter 4, and pyruvate dehydrogenase lipoamide kinase isozyme 1 (PDK1) [12]. A number of studies have revealed the importance of this metabolic reprogramming in cancer cells [13-17]. …”

Section: Introductionmentioning

confidence: 99%

Propofol Disrupts Aerobic Glycolysis in Colorectal Cancer Cells via Inactivation of the NMDAR-CAMKII-ERK Pathway

Chen

Sun

et al. 2018

Cell Physiol Biochem

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Background/Aims: To investigate the effect of propofol on glucose metabolism in colorectal cancer cells and in an in vivo xenograft model. Methods: Glucose metabolism was assessed by measuring the extracellular acidification rate in HT29 and SW480 colorectal cancer cells. Quantitative real-time PCR and western blot analyses were used to detect mRNA and protein levels, respectively. Intracellular calcium was assessed by using a Fluo-3 AM fluorescence kit. Micro-positron emission tomography/computed tomography (microPET/CT) imaging was used to analyze glucose metabolism in the tumors of the xenograft model. Results: Propofol exposure induced a dose-dependent decrease of aerobic glycolysis in HT29 and SW480 colorectal cancer cells. MicroPET/CT indicated that propofol also inhibited ¹⁸F-FDG uptake in the xenograft model. In addition, hypoxia-inducible factor 1α (HIF1α) was also reduced by propofol dose-dependently. Propofol repressed the NMDAR-CAMKII-ERK pathway to inactivate HIF1α and therefore reduced glycolysis. Conclusion: Propofol inhibited aerobic glycolysis in colorectal cancer cells through the inactivation of the NMDAR-CAMKII-ERK pathway, which may facilitate a better understanding of the use of propofol in the clinical setting.

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“…A total of 2 mL of cell suspension with a density of 5.5 × 10 4 cells/mL was incubated in a 6-well, flat-bottom plate in 5% CO 2 at 37°C for 48 h. Cells were then treated with 3 different fractions at different concentrations and incubated for another 24 h. Cells were lysed in RIPA lysate buffer containing 1 mM PMSF, which had been used in many other reports [16–18]. The cell lysates were centrifuged, the supernatants were collected and protein concentration was quantified using a BCA assay kit.…”

Section: Methodsmentioning

confidence: 99%

The comparative study among different fractions of muscadine grape ‘Noble’ pomace extracts regarding anti-oxidative activities, cell cycle arrest and apoptosis in breast cancer

Luo

Song

et al. 2017

Food & Nutrition Research

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As a by-product of wine making, pomace contains rich amounts of phenolic compounds that can be potentially utilized as raw materials to make beneficial products especially for the anti-cancer agents including the breast cancer. Muscadinia rotundifolia ‘Noble’ is a wine-making grape cultivar, and to better use ‘Noble’ pomace, the most effective phenolic fractions in cancer inhibition must be identified. In this study, anti-oxidative activities of three separated fractions of ‘Noble’ pomace (F1, F2 and F3) were compared in 2,2-diphenyl-1-picrylhydrazyl and 2,2ʹ-azino-bis-(3-ethylbenzothiazoline-6-sulphonic acid) radical scavenging (DPPH and ABTS) assays as well as the ferric-reducing antioxidant power (FRAP) assay. The ability of different fractions to induce cell cycle arrest and apoptosis in MDA-MB-231 breast cancer cells was also evaluated by flow cytometry and Western blot analysis. Fraction F3, which contained a mixture of anthocyanidins and ellagic acids, exhibited the strongest anti-oxidative activity, as determined at both low and high concentrations in the DPPH and FRAP assays. F3 also demonstrated the greatest ability to induce apoptosis via caspase activation and cell cycle arrest by downregulating cyclin A and upregulating p21. F3 was thus the most effective bioactive fraction among those prepared from muscadine grape ‘Noble’ pomace.

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Proteasome activator subunit 3 promotes pancreatic cancer growth via c-Myc-glycolysis signaling axis

Cited by 47 publications

References 29 publications

Substrate receptors of proteasomes

Substrate receptors of proteasomes

Propofol Disrupts Aerobic Glycolysis in Colorectal Cancer Cells via Inactivation of the NMDAR-CAMKII-ERK Pathway

The comparative study among different fractions of muscadine grape ‘Noble’ pomace extracts regarding anti-oxidative activities, cell cycle arrest and apoptosis in breast cancer

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