Quercetin induces dual specificity phosphatase 5 via serum response factor
2
조회
0
다운로드
0
인용
0
참고문헌
키워드
초록
The phytochemical quercetin has gained attention for its antiinflammatoryand anti-tumorigenic properties in various typesof cancer. Tumorigenesis involves the aberrant regulation ofkinase/phosphatase, highlighting the importance of maintaininghomeostasis. Dual Specificity Phosphatase (DUSP) plays acrucial role in controlling the phosphorylation of ERK. The currentstudy aimed to clone the DUSP5 promoter, and investigateits transcriptional activity in the presence of quercetin. The results revealed that quercetin-induced DUSP5 expressionis associated with the serum response factor (SRF) binding sitelocated in the DUSP5 promoter. The deletion of this site abolishedthe luciferase activity induced by quercetin, indicating itsvital role in quercetin-induced DUSP5 expression. SRF proteinis a transcription factor that potentially contributes to quercetin-induced DUSP5 expression at the transcriptional level. Additionally, quercetin enhanced SRF binding activity withoutchanging its expression. These findings provide evidence ofhow quercetin affects anti-cancer activity in colorectal tumorigenesisby inducing SRF transcription factor activity, therebyincreasing DUSP5 expression at the transcriptional level. Thisstudy highlights the importance of investigating the molecularmechanisms underlying the anti-cancer properties of quercetin,and suggests its potential use in cancer therapy.
Abstract
The phytochemical quercetin has gained attention for its antiinflammatoryand anti-tumorigenic properties in various typesof cancer. Tumorigenesis involves the aberrant regulation ofkinase/phosphatase, highlighting the importance of maintaininghomeostasis. Dual Specificity Phosphatase (DUSP) plays acrucial role in controlling the phosphorylation of ERK. The currentstudy aimed to clone the DUSP5 promoter, and investigateits transcriptional activity in the presence of quercetin. The results revealed that quercetin-induced DUSP5 expressionis associated with the serum response factor (SRF) binding sitelocated in the DUSP5 promoter. The deletion of this site abolishedthe luciferase activity induced by quercetin, indicating itsvital role in quercetin-induced DUSP5 expression. SRF proteinis a transcription factor that potentially contributes to quercetin-induced DUSP5 expression at the transcriptional level. Additionally, quercetin enhanced SRF binding activity withoutchanging its expression. These findings provide evidence ofhow quercetin affects anti-cancer activity in colorectal tumorigenesisby inducing SRF transcription factor activity, therebyincreasing DUSP5 expression at the transcriptional level. Thisstudy highlights the importance of investigating the molecularmechanisms underlying the anti-cancer properties of quercetin,and suggests its potential use in cancer therapy.
참고문헌 (34)
- McFann SE, "Putting in the Erk : growth factor signaling and mesoderm morphogenesis", Curr Top Dev Biol, 149, pp.263~310 (2022)
- Caunt CJ, "Dual-specificity MAP kinase phosphatases(MKPs) : shaping the outcome of MAP kinase signalling", FEBS J, 280, pp.489~504 (2013)
- Huang CY, "DUSPs, to MAP kinases and beyond", Cell Biosci, 2, pp.24~ (2012)
- Kucharska A, "Regulation of the inducible nuclear dual-specificity phosphatase DUSP5 by ERK MAPK", Cell Signal, 21, pp.1794~1805 (2009)
- Buffet C, "Dual specificity phosphatase 5, a specific negative regulator of ERK signaling, is induced by serum response factor and Elk-1 transcription factor", PLoS One, 10, pp.e0145484~ (2015)
- Kidger AM, "Dualspecificity phosphatase 5 controls the localized inhibition, propagation, and transforming potential of ERK signaling", Proc Natl Acad Sci U S A, 114, pp.E317~E326 (2017)
- Liu T, "The suppression of DUSP5expression correlates with paclitaxel resistance and poor prognosis in basal-like breast cancer", Int J Med Sci, 15, pp.738~747 (2018)
- Cai C, "Down-regulation of dual-specificity phosphatase 5 predicts poor prognosis of patients with prostate cancer", Int J Clin Exp Med, 8, pp.4186~4194 (2015)
- Shin SH, "Down-regulation of dual-specificity phosphatase 5 in gastric cancer by promoter CpG island hypermethylation and its potential role in carcinogenesis", Am J Pathol, 182, pp.1275~1285 (2013)
- Nunes-Xavier CE, "Differential up-regulation of MAP kinase phosphatases MKP3", DUSP6 and DUSP5 by Ets2 and c-Jun converge in the control of the growth arrest versus proliferation response of MCF-7 breast cancer cells to phorbol ester, 2010, pp.285, 26417~26430
- Azam H, "Emerging role for the Serum Response Factor(SRF)as a potential therapeutic target in cancer", Expert Opin Ther Targets, 26, pp.155~169 (2022)
- Chai J, "Serum response factor : discovery, biochemistry, biological roles and implications for tissue injury healing", J Physiol Pharmacol, 53, pp.147~157 (2002)
- Choi HN, "Serum response factor enhances liver metastasis of colorectal carcinoma via alteration of the E-cadherin", beta-catenin complex, 2009, pp.21, 57~63
- Patten LC, "Serum response factor is alternatively spliced in human colon cancer", J Surg Res, 121, pp.92~100 (2004)
- Almatroodi SA, "Potential therapeutic targets of quercetin, a plant flavonol, and its role in the therapy of various types of cancer through the modulation of various cell signaling pathways", Molecules, 26, pp.1315~ (2021)
- Vafadar A, "Quercetin and cancer : new insights into its therapeutic effects on ovarian cancer cells", Cell Biosci, 10, pp.32~ (2020)
- Boots AW, "Health effects of quercetin : from antioxidant to nutraceutical", Eur J Pharmacol, 585, pp.325~337 (2008)
- Kim YH, "Quercetin augments TRAIL-induced apoptotic death : involvement of the ERK signal transduction pathway", Biochem Pharmacol, 75, pp.1946~1958 (2008)
- Huang CF, "Quercetin induces tongue squamous cell carcinoma cell apoptosis via the JNK activation-regulated ERK", GSK-3alpha, Oncol Lett, pp.2022, 23[DOI]
- Nguyen TT, "The role of activated MEK-ERK pathway in quercetin-induced growth inhibition and apoptosis in A549 lung cancer cells", Carcinogenesis, 25, pp.647~659 (2004)
- Sugiura R, "ERK : a doubleedged sword in cancer. ERK-dependent apoptosis as a potential therapeutic strategy for cancer", Cells, 10, pp.2509~ (2021)
- Chen HF, "Regulation of dual-specificity phosphatase(DUSP)ubiquitination and protein stability", Int J Mol Sci, 20, pp.2668~ (2019)
- Meeusen B, "Tumor suppressive protein phosphatases in human cancer : emerging targets for therapeutic intervention and tumor stratification", Int J Biochem Cell Biol, 96, pp.98~134 (2018)
- Seo H, "Dual-specificity phosphatase 5 acts as an anti-inflammatory regulator by inhibiting the ERK and NF-kappaB signaling pathways", Sci Rep, 7, pp.17348~ (2017)
- Chen X, "EGFR and ERK activation resists flavonoid quercetin-induced anticancer activities in human cervical cancer cells in vitro", Oncol Lett, 22, pp.754~ (2021)
- Ritt DA, "Inhibition of Ras", Raf, ERK pathway signaling by a stress-induced phospho-regulatory circuit, pp.Mol Cell, 2016[DOI]
- McCubrey JA, "Roles of the Raf", MEK, Biochim Biophys Acta, pp.2007, 1773[DOI]
- Cagnol S, "Prolonged activation of ERK1, 2 induces FADD-independent caspase 8 activation and cell death", Apoptosis, 11, pp.337~346 (2006)
- Menu E, "Specific roles for the PI3K and the MEK-ERK pathway in IGF-1-stimulated chemotaxis, VEGF secretion and proliferation of multiple myeloma cells : study in the 5T33MM model", Br J Cancer, 90, pp.1076~1083 (2004)
- Mebratu Y, "How ERK1", 2 activation controls cell proliferation and cell death : is subcellular localization the answer?, 2009, pp.8, 1168~1175
- Onuh JO, "Serum response factor-cofactor interactions and their implications in disease", FEBS J, 288, pp.3120~3134 (2021)
- Ma L, "Suppressing serum response factor inhibits invasion in cervical cancer cell lines via regulating Egr‑1 and epithelial-mesenchymal transition", Int J Mol Med, 43, pp.614~620 (2019)
- Liang G, "Serum response factor controls CYLD expression via MAPK signaling pathway", PLoS One, 6, pp.e19613~ (2011)
- Mongkolpobsin K, "Cold atmospheric microwave plasma(CAMP)stimulates dermal papilla cell proliferation by inducing beta-catenin signaling", Sci Rep, 13, pp.3089~ (2023)
