과제정보
This work was supported by the Research Institute for Veterinary Science and BK21 PLUS Program for Creative Veterinary Science Research Center, Seoul National University, and by a National Research Foundation of Korea (NRF) grant funded by the Korean government (2021R1A2B2002923). We are particularly grateful for the technical assistance of Mr. Jaehak Lee at the Seoul National University.
참고문헌
- McFann SE, Shvartsman SY and Toettcher JE (2022) Putting in the Erk: growth factor signaling and mesoderm morphogenesis. Curr Top Dev Biol 149, 263-310 https://doi.org/10.1016/bs.ctdb.2022.02.007
- Caunt CJ and Keyse SM (2013) Dual-specificity MAP kinase phosphatases (MKPs): shaping the outcome of MAP kinase signalling. FEBS J 280, 489-504 https://doi.org/10.1111/j.1742-4658.2012.08716.x
- Huang CY and Tan TH (2012) DUSPs, to MAP kinases and beyond. Cell Biosci 2, 24
- Kucharska A, Rushworth LK, Staples C, Morrice NA and Keyse SM (2009) Regulation of the inducible nuclear dual-specificity phosphatase DUSP5 by ERK MAPK. Cell Signal 21, 1794-1805 https://doi.org/10.1016/j.cellsig.2009.07.015
- Buffet C, Catelli MG, Hecale-Perlemoine K et al (2015) 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, e0145484
- Kidger AM, Rushworth LK, Stellzig J et al (2017) Dual-specificity phosphatase 5 controls the localized inhibition, propagation, and transforming potential of ERK signaling. Proc Natl Acad Sci U S A 114, E317-E326 https://doi.org/10.1073/pnas.1614684114
- Liu T, Sun H, Liu S et al (2018) The suppression of DUSP5 expression correlates with paclitaxel resistance and poor prognosis in basal-like breast cancer. Int J Med Sci 15, 738-747 https://doi.org/10.7150/ijms.24981
- Cai C, Chen JY, Han ZD et al (2015) Down-regulation of dual-specificity phosphatase 5 predicts poor prognosis of patients with prostate cancer. Int J Clin Exp Med 8, 4186-4194
- Shin SH, Park SY and Kang GH (2013) 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, 1275-1285 https://doi.org/10.1016/j.ajpath.2013.01.004
- Nunes-Xavier CE, Tarrega C, Cejudo-Marin R et al (2010) 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. J Biol Chem 285, 26417-26430 https://doi.org/10.1074/jbc.M110.121830
- Azam H, Pierro L, Reina M, Gallagher WM and Prencipe M (2022) Emerging role for the Serum Response Factor (SRF) as a potential therapeutic target in cancer. Expert Opin Ther Targets 26, 155-169 https://doi.org/10.1080/14728222.2022.2032652
- Chai J and Tarnawski AS (2002) Serum response factor: discovery, biochemistry, biological roles and implications for tissue injury healing. J Physiol Pharmacol 53, 147-157
- Choi HN, Kim KR, Lee JH et al (2009) Serum response factor enhances liver metastasis of colorectal carcinoma via alteration of the E-cadherin/beta-catenin complex. Oncol Rep 21, 57-63
- Patten LC, Belaguli NS, Baek MJ, Fagan SP, Awad SS and Berger DH (2004) Serum response factor is alternatively spliced in human colon cancer. J Surg Res 121, 92-100 https://doi.org/10.1016/j.jss.2004.02.031
- Almatroodi SA, Alsahli MA, Almatroudi A et al (2021) 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, 1315
- Vafadar A, Shabaninejad Z, Movahedpour A et al (2020) Quercetin and cancer: new insights into its therapeutic effects on ovarian cancer cells. Cell Biosci 10, 32
- Boots AW, Haenen GR and Bast A (2008) Health effects of quercetin: from antioxidant to nutraceutical. Eur J Pharmacol 585, 325-337 https://doi.org/10.1016/j.ejphar.2008.03.008
- Kim YH, Lee DH, Jeong JH, Guo ZS and Lee YJ (2008) Quercetin augments TRAIL-induced apoptotic death: involvement of the ERK signal transduction pathway. Biochem Pharmacol 75, 1946-1958 https://doi.org/10.1016/j.bcp.2008.02.016
- Huang CF, Liu SH, Ho TJ et al (2022) Quercetin induces tongue squamous cell carcinoma cell apoptosis via the JNK activation-regulated ERK/GSK-3alpha/beta-mediated mitochondria-dependent apoptotic signaling pathway. Oncol Lett 23, 78
- Nguyen TT, Tran E, Nguyen TH, Do PT, Huynh TH and Huynh H (2004) The role of activated MEK-ERK pathway in quercetin-induced growth inhibition and apoptosis in A549 lung cancer cells. Carcinogenesis 25, 647-659 https://doi.org/10.1093/carcin/bgh052
- Sugiura R, Satoh R and Takasaki T (2021) ERK: a double-edged sword in cancer. ERK-dependent apoptosis as a potential therapeutic strategy for cancer. Cells 10, 2509
- Chen HF, Chuang HC and Tan TH (2019) Regulation of dual-specificity phosphatase (DUSP) ubiquitination and protein stability. Int J Mol Sci 20, 2668
- Meeusen B and Janssens V (2018) Tumor suppressive protein phosphatases in human cancer: emerging targets for therapeutic intervention and tumor stratification. Int J Biochem Cell Biol 96, 98-134 https://doi.org/10.1016/j.biocel.2017.10.002
- Seo H, Cho YC, Ju A et al (2017) Dual-specificity phosphatase 5 acts as an anti-inflammatory regulator by inhibiting the ERK and NF-kappaB signaling pathways. Sci Rep 7, 17348
- Chen X, Xu P, Zhang H et al (2021) EGFR and ERK activation resists flavonoid quercetin-induced anticancer activities in human cervical cancer cells in vitro. Oncol Lett 22, 754
- Ritt DA, Abreu-Blanco MT, Bindu L et al (2016) Inhibition of Ras/Raf/MEK/ERK pathway signaling by a stress-induced phospho-regulatory circuit. Mol Cell 64, 875-887 https://doi.org/10.1016/j.molcel.2016.10.029
- McCubrey JA, Steelman LS, Chappell WH et al (2007) Roles of the Raf/MEK/ERK pathway in cell growth, malignant transformation and drug resistance. Biochim Biophys Acta 1773, 1263-1284 https://doi.org/10.1016/j.bbamcr.2006.10.001
- Cagnol S, Van Obberghen-Schilling E and Chambard JC (2006) Prolonged activation of ERK1,2 induces FADD-independent caspase 8 activation and cell death. Apoptosis 11, 337-346 https://doi.org/10.1007/s10495-006-4065-y
- Menu E, Kooijman R, Van Valckenborgh E et al (2004) 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, 1076-1083 https://doi.org/10.1038/sj.bjc.6601613
- Mebratu Y and Tesfaigzi Y (2009) How ERK1/2 activation controls cell proliferation and cell death: is subcellular localization the answer? Cell Cycle 8, 1168-1175 https://doi.org/10.4161/cc.8.8.8147
- Onuh JO and Qiu H (2021) Serum response factor-cofactor interactions and their implications in disease. FEBS J 288, 3120-3134 https://doi.org/10.1111/febs.15544
- Ma L, Yu Y and Qu X (2019) Suppressing serum response factor inhibits invasion in cervical cancer cell lines via regulating Egr‑1 and epithelial-mesenchymal transition. Int J Mol Med 43, 614-620
- Liang G, Ahlqvist K, Pannem R, Posern G and Massoumi R (2011) Serum response factor controls CYLD expression via MAPK signaling pathway. PLoS One 6, e19613
- Mongkolpobsin K, Sillapachaiyaporn C, Lertpatipanpong P et al (2023) Cold atmospheric microwave plasma (CAMP) stimulates dermal papilla cell proliferation by inducing beta-catenin signaling. Sci Rep 13, 3089