참고문헌
- Multhoff G, Molls M and Radons J (2011) Chronic Inflammation in Cancer Development. Front Immunol 2, Article 98
- DeNardo DG, Johansson M and Coussens LM (2008) Immune Cells as Mediators of Solid Tumor Metastasis. Cancer Metastasis Rev 27, 11-18 https://doi.org/10.1007/s10555-007-9100-0
- Lee H, Jeong AJ and Ye SK (2019) Highlighted STAT3 as a potential drug target for cancer therapy. BMB Rep 52, 415-423 https://doi.org/10.5483/bmbrep.2019.52.7.152
- Darnell JE (1997) STATs and Gene Regulation. Science 277, 1630-1635 https://doi.org/10.1126/science.277.5332.1630
- Park Y and Kim J (2019) Regulation of IL-6 signaling by miR-125a and let-7e in endothelial cells controls vasculogenic mimicry formation of breast cancer cells. BMB Rep 52, 214-219 https://doi.org/10.5483/bmbrep.2019.52.3.308
- Inoue H, Ogawa W, Ozaki M et al (2004) Role of STAT-3 in regulation of hepatic gluconeogenic genes and carbohydrate metabolism in vivo. Nat Med 10, 168-174 https://doi.org/10.1038/nm980
- Yu H and Jove R (2004) The STATs of Cancer-New Molecular Targets Come of Age. Nat Rev Cancer 4, 97-105 https://doi.org/10.1038/nrc1275
- Demaria M, Giorgi C, Lebiedzinska M et al (2010) A STAT3-Mediated Metabolic Switch is Involved in Tumour Transformation and STAT3 Addiction. Aging (Albany NY) 2, 823-842 https://doi.org/10.18632/aging.100232
- Li J, Liu T, Zhao L et al (2015) Ginsenoside 20 (S)-Rg3 Inhibits the Warburg Effect through STAT3 Pathways in Ovarian Cancer Cells. Int J Oncol 46, 775-781 https://doi.org/10.3892/ijo.2014.2767
- Svinka J, Mikulits W and Eferl R (2014) STAT3 in hepatocellular carcinoma: new perspectives. Hepat Oncol 1, 107-120 https://doi.org/10.2217/hep.13.7
- Lee S, Lee M, Kim JB et al (2016) 17beta-estradiol exerts anticancer effects in anoikis-resistant hepatocellular carcinoma cell lines by targeting IL-6/STAT3 signaling. Biochem Biophys Res Commun 473, 1247-1254 https://doi.org/10.1016/j.bbrc.2016.04.049
- Kim M, Morales L, Jang IS, Cho YY and Kim D (2018) Protein Tyrosine Phosphatases as Potential Regulators of STAT3 Signaling. Int J Mol Sci 19, E2708
- Sekine Y, Tsuji S, Ikeda O et al (2006) Regulation of STAT3-Mediated Signaling by LMW-DSP2. Oncogene 25, 5801-5806 https://doi.org/10.1038/sj.onc.1209578
- Hou J, Xu J, Jiang R et al (2013) Estrogen-sensitive PTPRO expression represses hepatocellular carcinoma progression by control of STAT3. Hepatology 57, 678-688 https://doi.org/10.1002/hep.25980
- Ishibashi T, Bottaro DP, Chan A, Miki T and Aaronson SA (1992) Expression Cloning of a Human Dual-Specificity Phosphatase. Proc Natl Acad Sci U S A 89, 12170-12174 https://doi.org/10.1073/pnas.89.24.12170
- Wang JY, Yeh CL, Chou HC et al (2011) Vaccinia H1-Related Phosphatase (VHR) is a Phosphatase of ErbB Receptors and is Down-Regulated in Non-Small Cell lung Cancer. J Biol Chem 286, 10177-10184 https://doi.org/10.1074/jbc.M110.163295
- Todd JL, Rigas JD, Rafty LA and Denu JM (2002) Dual-Specificity Protein Tyrosine Phosphatase VHR Down-Regulates c-Jun N-terminal Kinase (JNK). Oncogene 21, 2573-2583 https://doi.org/10.1038/sj.onc.1205344
- Todd JL, Tanner KG and Denu JM (1999) Extracellular Regulated Kinases (ERK) 1 and ERK2 are Authentic Substrates for the Dual-Specificity Protein-Tyrosine Phosphatase VHR. A Aovel Role in Down-Regulating the ERK Pathway. J Biol Chem 274, 13271-13280 https://doi.org/10.1074/jbc.274.19.13271
-
Liu L, McBride KM and Reich NC (2005) STAT3 Nuclear Import is Independent of Tyrosine Phosphorylation and Mediated by Importin-
${\alpha}3$ . Proc Natl Acad Sci U S A 102, 8150-8155 https://doi.org/10.1073/pnas.0501643102 - Bromberg J and Wang TC (2009) Inflammation and Cancer: IL-6 and STAT3 Complete the Link. Cancer Cell 15, 79-80 https://doi.org/10.1016/j.ccr.2009.01.009
- Kumar J, Fraser F, Riley C, Ahmed N, McCulloch D and Ward A (2015) Granulocyte Colony-Stimulating Factor Receptor Signalling via Janus Kinase 2/Signal Transducer and Activator of Transcription 3 in Ovarian Cancer. Br J Cancer 113, 1642-1643
- Puente XS, Pinyol M, Quesada V et al (2011) Whole-Genome Sequencing Identifies Recurrent Mutations in Chronic Lymphocytic Leukaemia. Nature 475, 101-105 https://doi.org/10.1038/nature10113
- Devarajan E and Huang S (2009) STAT3 as a Central Regulator of Tumor Metastases. Curr Mol Med 9, 626-633 https://doi.org/10.2174/156652409788488720
- Hoyt R, Zhu W, Cerignoli F, Alonso A, Mustelin T and David M (2007) Cutting Edge: Selective Tyrosine Dephosphorylation of Interferon-Activated Nuclear STAT5 by the VHR Phosphatase. J Immunol 179, 3402-3406 https://doi.org/10.4049/jimmunol.179.6.3402
- Stahl N, Boulton TG, Farruggella T et al (1994) Association and Activation of Jak-Tyk Kinases by CNTF-LIFOSM- IL-6 Beta Receptor Components. Science 263, 92-95 https://doi.org/10.1126/science.8272873
- Han Y, Amin HM, Franko B, Frantz C, Shi X and Lai R (2006) Loss of SHP1 Enhances JAK3/STAT3 Signaling and Decreases Proteosome Degradation of JAK3 and NPM-ALK in ALK+ Anaplastic Large-Cell Lymphoma. Blood 108, 2796-2803
- Li C and Friedman JM (1999) Leptin Receptor Activation of SH2 Domain Containing Protein Tyrosine Phosphatase 2 Modulates Ob Receptor SignalTtransduction. Proc Natl Acad Sci U S A 96, 9677-9682 https://doi.org/10.1073/pnas.96.17.9677
- Wakahara R, Kunimoto H, Tanino K et al (2012) Phospho-Ser727 of STAT3 Regulates STAT3 Activity by Enhancing Dephosphorylation of Phospho-Tyr705 Largely through TC45. Genes Cells 17, 132-145 https://doi.org/10.1111/j.1365-2443.2011.01575.x
- Veeriah S, Brennan C, Meng S et al (2009) The Tyrosine Phosphatase PTPRD is a Tumor Suppressor that is Frequently Inactivated and Mutated in Glioblastoma and Other Human Cancers. Proc Natl Acad Sci U S A 106, 9435-9440 https://doi.org/10.1073/pnas.0900571106
- Zhang X, Guo A, Yu J et al (2007) Identification of STAT3 as a Substrate of Receptor Protein Tyrosine Phosphatase T. Proc Natl Acad Sci U S A 104, 4060-4064 https://doi.org/10.1073/pnas.0611665104
- Chen YW, Guo T, Shen L et al (2015) Receptor-Type Tyrosine-Protein Phosphatase Kappa Directly Targets STAT3 Activation for Tumor Suppression in Nasal NK/T-Cell Lymphoma. Blood 125, 1589-1600 https://doi.org/10.1182/blood-2014-07-588970
- Alonso A, Sasin J, Bottini N et al (2004) Protein tyrosine phosphatases in the human genome. Cell 117, 699-711 https://doi.org/10.1016/j.cell.2004.05.018
- Bourdeau A, Dube N and Tremblay ML (2005) Cytoplasmic protein tyrosine phosphatases, regulation and function: the roles of PTP1B and TC-PTP. Curr Opin Cell Biol 17, 203-209 https://doi.org/10.1016/j.ceb.2005.02.001
- Lee H, Morales LD, Slaga TJ and Kim DJ (2015) Activation of T-cell protein-tyrosine phosphatase suppresses keratinocyte survival and proliferation following UVB irradiation. J Biol Chem 290, 13-24 https://doi.org/10.1074/jbc.M114.611681
- Pavic K, Duan G and Kohn M (2015) VHR/DUSP3 Phosphatase: Structure, Function and Regulation. FEBS J 282, 1871-1890 https://doi.org/10.1111/febs.13263
- Vandereyken M, Jacques S, Van Overmeire E et al (2017) Dusp3 Deletion in Mice Promotes Experimental Lung Tumour Metastasis in a Macrophage Dependent Manner. PLoS One 12, e0185786 https://doi.org/10.1371/journal.pone.0185786
- Singh P, Dejager L, Amand M et al (2015) DUSP3 Genetic Deletion Confers M2-Like Macrophage-Dependent Tolerance to Septic Shock. J Immunol 194, 4951-4962 https://doi.org/10.4049/jimmunol.1402431
- Takaishi K, Komohara Y, Tashiro H et al (2010) Involvement of M2-Polarized Macrophages in the Ascites from Advanced Epithelial Ovarian Carcinoma in Tumor Progression via Stat3 Activation. Cancer Sci 101, 2128-2136 https://doi.org/10.1111/j.1349-7006.2010.01652.x
- Shiraishi D, Fujiwara Y, Komohara Y, Mizuta H and Takeya M (2012) Glucagon-Like Peptide-1 (GLP-1) Induces M2 Polarization of Human Macrophages via STAT3 Activation. Biochem Biophys Res Commun 425, 304-308 https://doi.org/10.1016/j.bbrc.2012.07.086
- Perovic V, Sumonja N, Gemovic B, Toska E, Roberts SG and Veljkovic N (2017) TRI_Tool: a Web-Tool for Prediction of Protein-Protein Interactions in Human Transcriptional Regulation. Bioinformatics 33, 289-291 https://doi.org/10.1093/bioinformatics/btw590