Post-transcriptional regulation of BIRC5/survivin expression and induction of apoptosis in breast cancer cells by tristetraprolin

References

• Siegel RL, Miller KD, Fuchs HE, et al. Cancer statistics, 2021. Ca A Cancer J Clinicians. 2021;71(1):7–33. doi: 10.3322/caac.21654
   PubMed Web of Science ®Google Scholar
• Hanahan D, Weinberg RA. The hallmarks of cancer. Cell. 2000;100(1):57–70. doi: 10.1016/S0092-8674(00)81683-9
   PubMed Web of Science ®Google Scholar
• Ghobrial IM, Witzig TE, Adjei AA. Targeting apoptosis pathways in cancer therapy. CA Cancer J Clin. 2005;55(3):178–194. doi: 10.3322/canjclin.55.3.178
   PubMed Web of Science ®Google Scholar
• Li GY, Jung KH, Lee H, et al. A novel imidazopyridine derivative, HS-106, induces apoptosis of breast cancer cells and represses angiogenesis by targeting the PI3K/mTOR pathway. Cancer Lett. 2013;329(1):59–67. doi: 10.1016/j.canlet.2012.10.013
   PubMed Web of Science ®Google Scholar
• Khan KH, Blanco-Codesido M, Molife LR. Cancer therapeutics: targeting the apoptotic pathway. Crit Rev Oncol Hematol. 2014;90(3):200–219. doi: 10.1016/j.critrevonc.2013.12.012
   PubMed Web of Science ®Google Scholar
• Kasibhatla S, Tseng B. Why target apoptosis in cancer treatment? Mol Cancer Ther. 2003;2(6):573–580.
   PubMed Web of Science ®Google Scholar
• Sohn DM, Kim SY, Baek MJ, et al. Expression of survivin and clinical correlation in patients with breast cancer. Biomed Pharmacother. 2006;60(6):289–292. doi: 10.1016/j.biopha.2006.06.008
   PubMed Web of Science ®Google Scholar
• Xu C, Yamamoto-Ibusuki M, Yamamoto Y, et al. High survivin mRNA expression is a predictor of poor prognosis in breast cancer: a comparative study at the mRNA and protein level. Breast Cancer. 2014;21(4):482–490. doi: 10.1007/s12282-012-0403-9
   PubMed Web of Science ®Google Scholar
• Hernandez JM, Farma JM, Coppola D, et al. Expression of the antiapoptotic protein survivin in colon cancer. Clin Colorectal Cancer. 2011;10(3):188–193. doi: 10.1016/j.clcc.2011.03.014
   PubMed Web of Science ®Google Scholar
• Zhou XL, Wang M. Expression levels of survivin, bcl-2, and KAI1 proteins in cervical cancer and their correlation with metastasis. Genet Mol Res. 2015;14(4):17059–17067. doi: 10.4238/2015.December.16.6
   PubMed Web of Science ®Google Scholar
• Zhang M, Ho A, Hammond EH, et al. Prognostic value of survivin in locally Advanced prostate cancer: study based on RTOG 8610. Int J Radiat Oncol Biol Phys. 2009;73(4):1033–1042. doi: 10.1016/j.ijrobp.2008.06.1489
   PubMed Web of Science ®Google Scholar
• Altieri DC, Altieri DC. Survivin – The inconvenient IAP. Survivin – the inconvenient IAP. Seminars In Cell & Developmental Biology. 2015;39:91–96. doi: 10.1016/j.semcdb.2014.12.007
   PubMed Web of Science ®Google Scholar
• Mirza A, McGuirk M, Hockenberry TN, et al. Human survivin is negatively regulated by wild-type p53 and participates in p53-dependent apoptotic pathway. Oncogene. 2002;21(17):2613–2622. doi: 10.1038/sj.onc.1205353
   PubMed Web of Science ®Google Scholar
• Guha M, Plescia J, Leav I, et al. Endogenous tumor suppression mediated by PTEN involves survivin gene silencing. Cancer Res. 2009;69(12):4954–4958. doi: 10.1158/0008-5472.CAN-09-0584
   PubMed Web of Science ®Google Scholar
• Asanuma H, Torigoe T, Kamiguchi K, et al. Survivin expression is regulated by coexpression of human epidermal growth factor receptor 2 and epidermal growth factor receptor via phosphatidylinositol 3-Kinase/AKT Signaling pathway in breast cancer cells. Cancer Res. 2005;65(23):11018–11025. doi: 10.1158/0008-5472.CAN-05-0491
   PubMed Web of Science ®Google Scholar
• Gritsko T, Williams A, Turkson J, et al. Persistent activation of Stat3 Signaling induces survivin gene expression and confers resistance to apoptosis in human breast cancer cells. Clin Cancer Res. 2006;12(1):11–19. doi: 10.1158/1078-0432.CCR-04-1752
   PubMed Web of Science ®Google Scholar
• Wang H, Holloway MP, Ma L, et al. Acetylation directs survivin nuclear localization to repress STAT3 oncogenic activity. J Biol Chem. 2010;285(46):36129–36137. doi: 10.1074/jbc.M110.152777
   PubMed Web of Science ®Google Scholar
• Vong QP, Cao K, Li HY, et al. Chromosome alignment and segregation regulated by ubiquitination of survivin. Science. 2005;310(5753):1499. doi: 10.1126/science.1120160
   PubMed Web of Science ®Google Scholar
• O’Connor DS, Grossman D, Plescia J, et al. Regulation of apoptosis at cell division by p34cdc2 phosphorylation of survivin. Proc Natl Acad Sci U S A. 2000;97(24):13103–13107. doi: 10.1073/pnas.240390697
   PubMed Web of Science ®Google Scholar
• Barrett RMA, Osborne TP, Wheatley SP. Phosphorylation of survivin at threonine 34 inhibits its mitotic function and enhances its cytoprotective activity. Cell Cycle. 2009;8(2):278–283. doi: 10.4161/cc.8.2.7587
   PubMed Web of Science ®Google Scholar
• Yang R, Liu M, Liang H, et al. miR-138-5p contributes to cell proliferation and invasion by targeting survivin in bladder cancer cells. Mol Cancer. 2016;15(1):82–82. doi: 10.1186/s12943-016-0569-4
   PubMedGoogle Scholar
• Li P-L, Zhang X, Wang L-L, et al. MicroRNA-218 is a prognostic indicator in colorectal cancer and enhances 5-fluorouracil-induced apoptosis by targeting BIRC5. Carcinogenesis. 2015;36(12):1484–1493. doi: 10.1093/carcin/bgv145
   PubMed Web of Science ®Google Scholar
• Hu Y, Xu K, Yagüe E. miR-218 targets survivin and regulates resistance to chemotherapeutics in breast cancer. Breast Cancer Res Treat. 2015;151(2):269–280. doi: 10.1007/s10549-015-3372-9
   PubMed Web of Science ®Google Scholar
• Wang C, Zheng X, Shen C, et al. MicroRNA-203 suppresses cell proliferation and migration by targeting BIRC5 and LASP1 in human triple-negative breast cancer cells. J Exp Clin Cancer Res. 2012;31(1):58–58. doi: 10.1186/1756-9966-31-58
   PubMedGoogle Scholar
• Lai WS, Carballo E, Strum JR, et al. Evidence that tristetraprolin binds to AU-Rich elements and promotes the deadenylation and destabilization of tumor necrosis factor alpha mRNA. Mol Cell Biol. 1999;19(6):4311–4323. doi: 10.1128/MCB.19.6.4311
   PubMed Web of Science ®Google Scholar
• Stoecklin G, Tenenbaum SA, Mayo T, et al. Genome-wide analysis identifies interleukin-10 mRNA as target of tristetraprolin. J Biol Chem. 2008;283(17):11689–11699. doi: 10.1074/jbc.M709657200
   PubMed Web of Science ®Google Scholar
• Hitti E, Bakheet T, Al-Souhibani N, et al. Systematic analysis of AU-Rich element expression in cancer reveals common functional clusters regulated by key RNA-Binding proteins. Cancer Res. 2016;76(14):4068–4080. doi: 10.1158/0008-5472.CAN-15-3110
   PubMed Web of Science ®Google Scholar
• Al-Souhibani N, Al-Ahmadi W, Hesketh JE, et al. The RNA-binding zinc-finger protein tristetraprolin regulates AU-rich mRnas involved in breast cancer-related processes. Oncogene. 2010;29(29):4205–4215. doi: 10.1038/onc.2010.168
   PubMed Web of Science ®Google Scholar
• Lee HH, Son YJ, Lee WH, et al. Tristetraprolin regulates expression of VEGF and tumorigenesis in human colon cancer. Int J Cancer. 2010;126(8):1817–1827. doi: 10.1002/ijc.24847
   PubMed Web of Science ®Google Scholar
• Al-Souhibani N, Al-Ghamdi M, Al-Ahmadi W, et al. Posttranscriptional control of the chemokine receptor CXCR4 expression in cancer cells. Carcinogenesis. 2014;35(9):1983–1992. doi: 10.1093/carcin/bgu080
   PubMed Web of Science ®Google Scholar
• Brennan CM, Kuwano Y, Alkharouf N, et al. The mRNA-destabilizing protein tristetraprolin is suppressed in many cancers, altering tumorigenic phenotypes and patient prognosis. Cancer Res. 2009;69(12):5168–5176. doi: 10.1158/0008-5472.CAN-08-4238
   PubMed Web of Science ®Google Scholar
• de Silanes I L, Fan J, Yang X, et al. Role of the RNA-binding protein HuR in colon carcinogenesis. Oncogene. 2003;22(46):7146–7154. doi: 10.1038/sj.onc.1206862
   PubMed Web of Science ®Google Scholar
• Denkert C, Weichert W, Pest S, et al. Overexpression of the embryonic-lethal abnormal vision-like protein HuR in ovarian carcinoma is a prognostic factor and is associated with increased cyclooxygenase 2 expression. Cancer Res. 2004;64(1):189–195. doi: 10.1158/0008-5472.CAN-03-1987
   PubMed Web of Science ®Google Scholar
• Al-Ahmadi W, Al-Ghamdi M, Al-Haj L, et al. Alternative polyadenylation variants of the RNA binding protein, HuR: abundance, role of AU-rich elements and auto-regulation. Nucl Acids Res. 2009;37(11):3612–3624. doi: 10.1093/nar/gkp223
   PubMed Web of Science ®Google Scholar
• Hitti E, Al-Yahya S, Al-Saif M, et al. A versatile ribosomal protein promoter-based reporter system for selective assessment of RNA stability and post-transcriptional control. RNA. 2010;16(6):1245–1255. doi: 10.1261/rna.2026310
   PubMed Web of Science ®Google Scholar
• Al-Haj L, Al-Ahmadi W, Al-Saif M, et al. Cloning-free regulated monitoring of reporter and gene expression. BMC Mol Biol. 2009;10(1):20. doi: 10.1186/1471-2199-10-20
   PubMedGoogle Scholar
• Lánczky A, Győrffy B. Web-based survival analysis tool tailored for medical Research (KMplot): development and implementation. J Med Internet Res. 2021;23(7):e27633. doi: 10.2196/27633
   PubMed Web of Science ®Google Scholar
• Donahue James M, Chang Elizabeth T, Xiao L, et al. The RNA-binding protein HuR stabilizes survivin mRNA in human oesophageal epithelial cells. Biochem J. 2011;437(1):89–96. doi: 10.1042/BJ20110028
   PubMedGoogle Scholar
• Gerstberger S, Hafner M, Tuschl T. A census of human RNA-binding proteins. Nat Rev Genet. 2014;15(12):829–845. doi: 10.1038/nrg3813
   PubMed Web of Science ®Google Scholar
• Ma W-J, Cheng S, Campbell C, et al. Cloning and characterization of HuR, a ubiquitously expressed elav-like protein. J Biol Chem. 1996;271(14):8144–8151. doi: 10.1074/jbc.271.14.8144
   PubMed Web of Science ®Google Scholar
• Ma WJ, Chung S, Furneaux H. The elav-like proteins bind to AU-rich elements and to the poly(A) tail of mRNA. Nucl Acids Res. 1997;25(18):3564–3569. doi: 10.1093/nar/25.18.3564
   PubMed Web of Science ®Google Scholar
• Fan XC, Steitz JA. Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRnas. EMBO J. 1998;17(12):3448–3460. doi: 10.1093/emboj/17.12.3448
   PubMed Web of Science ®Google Scholar
• Panganiban RP, Vonakis BM, Ishmael FT, et al. Coordinated post-transcriptional regulation of the chemokine system: messages from CCL2. J Interferon Cytokine Res. 2014;34(4):255–266. doi: 10.1089/jir.2013.0149
   PubMed Web of Science ®Google Scholar
• Khabar KSA. Post-transcriptional control of cytokine gene expression in health and disease. J Interferon Cytokine Res. 2014;34(4):215–219. doi: 10.1089/jir.2013.0151
   PubMed Web of Science ®Google Scholar
• Young LE, Dixon DA. Posttranscriptional regulation of cyclooxygenase 2 expression in colorectal cancer. Curr Colorectal Cancer Rep. 2010;6(2):60–67. doi: 10.1007/s11888-010-0044-3
   PubMedGoogle Scholar
• Sanduja S, Blanco FF, Young LE, et al. The role of tristetraprolin in cancer and inflammation. Front Biosci. 2012;17(1):174–188. doi: 10.2741/3920
   Google Scholar
• Essafi-Benkhadir K, Onesto C, Stebe E, et al. Tristetraprolin inhibits ras-dependent tumor vascularization by inducing vascular endothelial growth factor mRNA degradation. ?Mol Biol Cell. 2007;18(11):4648–4658. doi: 10.1091/mbc.e07-06-0570
   Web of Science ®Google Scholar
• Bhandare S, Goldberg DS, Dowell R, et al. Discriminating between HuR and TTP binding sites using the k-spectrum kernel method. PLoS One. 2017;12(3):e0174052. doi: 10.1371/journal.pone.0174052
   PubMed Web of Science ®Google Scholar
• Johnson BA, Geha M, Blackwell TK. Similar but distinct effects of the tristetraprolin/TIS11 immediate-early proteins on cell survival. Oncogene. 2000;19(13):1657–1664. doi: 10.1038/sj.onc.1203474
   PubMed Web of Science ®Google Scholar
• Johnson BB, Blackwell TK. Multiple tristetraprolin sequence domains required to induce apoptosis and modulate responses to TNFα through distinct pathways. Oncogene. 2002;21(27):4237–4246. doi: 10.1038/sj.onc.1205526
   PubMed Web of Science ®Google Scholar
• Virrey JJ, Guan S, Li W, et al. Increased survivin expression confers chemoresistance to tumor-associated endothelial cells. Am J Pathol. 2008;173(2):575–585. doi: 10.2353/ajpath.2008.071079
   PubMed Web of Science ®Google Scholar
• Moriai R, Tsuji N, Moriai M, et al. Survivin plays as a resistant factor against tamoxifen-induced apoptosis in human breast cancer cells. Breast Cancer Res Treat. 2009;117(2):261–271. doi: 10.1007/s10549-008-0164-5
   PubMed Web of Science ®Google Scholar
• Wang S, Huang X, Lee CK, et al. Elevated expression of erbB3 confers paclitaxel resistance in erbB2-overexpressing breast cancer cells via upregulation of survivin. Oncogene. 2010;29(29):4225–4236. doi: 10.1038/onc.2010.180
   PubMed Web of Science ®Google Scholar
• Nestal de Moraes G, Vasconcelos FC, Delbue D, et al. Doxorubicin induces cell death in breast cancer cells regardless of survivin and XIAP expression levels. Eur J Cell Biol. 2013;92(8–9):247–256. doi: 10.1016/j.ejcb.2013.08.001
   PubMed Web of Science ®Google Scholar
• Olie RA, Simões-Wüst AP, Baumann B, et al. A novel antisense oligonucleotide targeting survivin expression induces apoptosis and sensitizes lung cancer cells to chemotherapy. Cancer Res. 2000;60(11):2805.
   PubMed Web of Science ®Google Scholar
• Faversani A, Vaira V, Moro GP, et al. Survivin family proteins as novel molecular determinants of doxorubicin resistance in organotypic human breast tumors. Breast Cancer Res. 2014;16(3):R55–R55. doi: 10.1186/bcr3666
   PubMed Web of Science ®Google Scholar
• Taylor GA, Thompson MJ, Lai WS, et al. Phosphorylation of tristetraprolin, a potential zinc finger transcription factor, by mitogen stimulation in intact cells and by Mitogen-activated protein Kinase in vitro. J Biol Chem. 1995;270(22):13341–13347. doi: 10.1074/jbc.270.22.13341
   PubMed Web of Science ®Google Scholar
• Mahtani KR, Brook M, Dean JLE, et al. Mitogen-activated protein Kinase p38 controls the expression and posttranslational modification of tristetraprolin, a regulator of tumor necrosis factor alpha mRNA stability. Mol Cell Biol. 2001;21(19):6461–6469. doi: 10.1128/MCB.21.9.6461-6469.2001
   PubMed Web of Science ®Google Scholar
• Cao H, Dzineku F, Blackshear PJ. Expression and purification of recombinant tristetraprolin that can bind to tumor necrosis factor-[alpha] mRNA and serve as a substrate for mitogen-activated protein kinases. Arch Biochem Biophys. 2003;412(1):106–120. doi: 10.1016/S0003-9861(03)00012-2
   PubMed Web of Science ®Google Scholar
• Stoecklin G, Stubbs T, Kedersha N, et al. MK2-Induced tristetraprolin: 14-3-3 complexes prevent stress granule association and ARE-mRNA decay. EMBO J. 2004;23(6):1313–1324. doi: 10.1038/sj.emboj.7600163
   PubMed Web of Science ®Google Scholar
• Al-Qahtani QH, Moghrabi WN, Al-Yahya S, et al. Kinome inhibition reveals a role for polo-like kinase 1 in targeting post-transcriptional control in cancer. Mol Oncol. 2021;15(8):2120–2139. doi: 10.1002/1878-0261.12897
   PubMed Web of Science ®Google Scholar
• Hitti E, Iakovleva T, Brook M, et al. Mitogen-activated protein Kinase-activated protein Kinase 2 regulates tumor necrosis factor mRNA stability and translation mainly by altering tristetraprolin expression, stability, and binding to adenine/Uridine-rich element. Mol Cell Biol. 2006;26(6):2399–2407. doi: 10.1128/MCB.26.6.2399-2407.2006
   PubMed Web of Science ®Google Scholar
• Clement SL, Scheckel C, Stoecklin G, et al. Phosphorylation of tristetraprolin by MK2 impairs AU-rich element mRNA decay by preventing deadenylase recruitment. Mol Cell Biol. 2011;31(2):256–266. doi: 10.1128/MCB.00717-10
   PubMed Web of Science ®Google Scholar
• Fabbro D, Cowan-Jacob SW, Möbitz H, et al. Targeting cancer with small-molecular-weight Kinase inhibitors. In: Kuster B, editor Kinase inhibitors: methods and protocols. Totowa, NJ: Humana Press; 2012. pp. 1–34.
   Google Scholar
• Marmiroli S, Fabbro D, Miyata Y, et al. Phosphorylation, Signaling, and cancer: targets and targeting. Biomed Res Int. 2015; 601543–601543.
   Google Scholar