Signal-dependent Elk-1 target genes involved in transcript processing and cell migration

Biochimica et Biophysica Acta - Gene Regulatory Mechanisms

Volumn 1829, Issue 10, 2013, Pages 1026-1033

  Kasza, Aneta ^a  

^a JAGIELLONIAN UNIVERSITY   (Poland)

Author keywords

Cancer; Elk 1; MCPIP1; MMPs; PAI 1; Tristetraprolin

Indexed keywords

FIBROBLAST GROWTH FACTOR 2; GELATINASE A; GELATINASE B; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 12P40; INTERLEUKIN 1BETA; INTERLEUKIN 6; KALLIKREIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; MONOCYTE CHEMOTACTIC PROTEIN 1; NUCLEAR RECEPTOR NUR77; PLASMINOGEN; PLASMINOGEN ACTIVATOR INHIBITOR 1; PROTEIN C FOS; STAT1 PROTEIN; STAT3 PROTEIN; TISSUE PLASMINOGEN ACTIVATOR; TOLL LIKE RECEPTOR; TOLL LIKE RECEPTOR 9; TRANSCRIPTION FACTOR EGR 1; TRANSCRIPTION FACTOR ELK 1; TRANSFORMING GROWTH FACTOR BETA; TUMOR NECROSIS FACTOR RECEPTOR 1; TUMOR NECROSIS FACTOR RECEPTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 2; TUMOR NECROSIS FACTOR RECEPTOR ASSOCIATED FACTOR 3; UROKINASE; VASCULOTROPIN; VITRONECTIN;

ANGIOGENESIS; CELL MIGRATION; CELL SURVIVAL; ENDOCYTOSIS; GENE CONTROL; GENE EXPRESSION; HUMAN; INFLAMMATION; LEUKOCYTE MIGRATION; MESSENGER RNA SYNTHESIS; NEOPLASM; NONHUMAN; PLASMINOGEN ACTIVATION; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN PROCESSING; REVIEW; SIGNAL TRANSDUCTION;

CANCER; ELK-1; MCPIP1; MMPS; PAI-1; TRISTETRAPROLIN;

ANIMALS; CELL MOVEMENT; ETS-DOMAIN PROTEIN ELK-1; GENE EXPRESSION REGULATION; HUMANS; SIGNAL TRANSDUCTION; TRANSCRIPTION, GENETIC;

EID: 84880722876     PISSN: 18749399     EISSN: 18764320     Source Type: Journal    
DOI: 10.1016/j.bbagrm.2013.05.004     Document Type: Review

References (94)

1. Treisman R. Ternary complex factors: growth factor regulated transcriptional activators. Curr. Opin. Genet. Dev. 1994, 4:96-101.
2. Yang S.H., Sharrocks A.D. Convergence of the SUMO and MAPK pathways on the ETS-domain transcription factor Elk-1. Biochem. Soc. Symp. 2006, 73:121-129. (Review).
3. Sharrocks A.D. The ETS-domain transcription factor family. Nat. Rev. Mol. Cell Biol. 2001, 2:827-837. (Review).
4. Boros J., O'Donnell A., Donaldson I.J., Kasza A., Zeef L., Sharrocks A.D. Overlapping promoter targeting by Elk-1 and other divergent ETS-domain transcription factor family members. Nucleic Acids Res. 2009, 37:7368-7380. 10.1093/nar/gkp804. Epub.
5. Hollenhorst P.C., Shah A.A., Hopkins C., Graves B.J. Genome-wide analyses reveal properties of redundant and specific promoter occupancy within the ETS gene family. Genes Dev. 2007, 21:1882-1894. (Epub 2007 Jul 24.).
6. Cesari F., Brecht S., Vintersten K., Vuong L.G., Hofmann M., Klingel K., Schnorr J.J., Arsenian S., Schild H., Herdegen T., Wiebel F.F., Nordheim A. Mice deficient for the ets transcription factor elk-1 show normal immune responses and mildly impaired neuronal gene activation. Mol. Cell. Biol. 2004, 24:294-305.
7. Jorissen R.N., Walker F., Pouliot N., Garrett T.P., Ward C.W., Burgess A.W. Epidermal growth factor receptor: mechanisms of activation and signalling. Exp. Cell Res. 2003, 284:31-53. (Review).
8. Reuter C.W., Morgan M.A., Eckardt A. Targeting EGF-receptor-signalling in squamous cell carcinomas of the head and neck. Br. J. Cancer 2007, 96:408-416. (Review).
9. Hsieh H.L., Wu C.Y., Yang C.M. Bradykinin induces matrix metalloproteinase-9 expression and cell migration through a PKC-delta-dependent ERK/Elk-1 pathway in astrocytes. Glia Apr. 15 2008, 56(6):619-632. 10.1002/glia.20637.
10. Dinarello C.A. Interleukin-1 in the pathogenesis and treatment of inflammatory diseases. Blood 2011, 117:3720-3732. (Review).
11. O'Neill L.A. The interleukin-1 receptor/Toll-like receptor superfamily: 10years of progress. Immunol. Rev. 2008, 226:10-18. (Review).
12. Haeusgen W., Herdegen T., Waetzig V. The bottleneck of JNK signaling: molecular and functional characteristics of MKK4 and MKK7. Eur. J. Cell Biol. 2011, 90:536-544. (Review).
13. Johnson G.L., Nakamura K. The c-jun kinase/stress-activated pathway: regulation, function and role in human disease. Biochim. Biophys. Acta 2007, 1773:1341-1348. (Review).
14. Lang V., Symons A., Watton S.J., Janzen J., Soneji Y., Beinke S., Howell S., Ley S.C. ABIN-2 forms a ternary complex with TPL-2 and NF-kappa B1 p105 and is essential for TPL-2 protein stability. Mol. Cell. Biol. 2004, 24:5235-5248.
15. Waterfield M.R., Zhang M., Norman L.P., Sun S.C. NF-kappaB1/p105 regulates lipopolysaccharide-stimulated MAP kinase signaling by governing the stability and function of the Tpl2 kinase. Mol. Cell. 2003, 11:685-694.
16. Matsushita K., Takeuchi O., Standley D.M., Kumagai Y., Kawagoe T., Miyake T., Satoh T., Kato H., Tsujimura T., Nakamura H., Akira S. Zc3h12a is an RNase essential for controlling immune responses by regulating mRNA decay. Nature 2009, 458:1185-1190.
17. Mizgalska D., Wegrzyn P., Murzyn K., Kasza A., Koj A., Jura J., Jarzab B., Jura J. Interleukin-1-inducible MCPIP protein has structural and functional properties of RNase and participates in degradation of IL-1beta mRNA. FEBS J. 2009, 276:7386-7399.
18. Li M., Cao W., Liu H., Zhang W., Liu X., Cai Z., Guo J., Wang X., Hui Z., Zhang H., Wang J., Wang L. MCPIP1 down-regulates IL-2 expression through an ARE-independent pathway. PLoS One 2012, 7:e49841. (Epub 2012 Nov 21). 10.1371/journal.pone.0049841.
19. Liang J., Saad Y., Lei T., Wang J., Qi D., Yang Q., Kolattukudy P.E., Fu M. MCP-induced protein 1 deubiquitinates TRAF proteins and negatively regulates JNK and NF-kappaB signaling. J. Exp. Med. 2010, 207:2959-2973.
20. Zhou L., Azfer A., Niu J., Graham S., Choudhury M., Adamski F.M., Younce C., Binkley P.F., Kolattukudy P.E. Monocyte chemoattractant protein-1 induces a novel transcription factor that causes cardiac myocyte apoptosis and ventricular dysfunction. Circ. Res. 2006, 98:1177-1185.
21. Lin R.J., Chien H.L., Lin S.Y., Chang B.L., Yu H.P., Tang W.C., Lin Y.L. MCPIP1 ribonuclease exhibits broad-spectrum antiviral effects through viral RNA binding and degradation. Nucleic Acids Res. 2013, 41:3314-3326. (Epub 2013 Jan 25). 10.1093/nar/gkt019.
22. Skalniak L., Mizgalska D., Zarebski A., Wyrzykowska P., Koj A., Jura J. Regulatory feedback loop between NF-kappaB and MCP-1-induced protein 1 RNase. FEBS 2009, 276:5892-5905.
23. Kasza A., Wyrzykowska P., Horwacik I., Tymoszuk P., Mizgalska D., Palmer K., Rokita H., Sharrocks A.D., Jura J. Transcription factors Elk-1 and SRF are engaged in IL1-dependent regulation of ZC3H12A expression. BMC Mol. Biol. 2010, 11:14.
24. Suzuki H.I., Arase M., Matsuyama H., Choi Y.L., Ueno T., Mano H., Sugimoto K., Miyazono K. MCPIP1 ribonuclease antagonizes dicer and terminates microRNA biogenesis through precursor microRNA degradation. Mol. Cell 2011, 44:424-436.
25. Taylor G.A., Lai W.S., Oakey R.J., Seldin M.F., Shows T.B., Eddy R.L., Blackshear P.J. The human TTP protein: sequence, alignment with related proteins, and chromosomal localization of the mouse and human genes. Nucleic Acids Res. 1991, 19:3454.
26. Taylor G.A., Thompson M.J., Lai W.S., Blackshear P.J. Mitogens stimulate the rapid nuclear to cytosolic translocation of tristetraprolin, a potential zinc-finger transcription factor. Mol. Endocrinol. 1996, 10:140-146.
27. Carballo E., Lai W.S., Blackshear P.J. Feedback inhibition of macrophage tumor necrosis factor-alpha production by tristetraprolin. Science 1998, 281:1001-1005.
28. Hau H.H., Walsh R.J., Ogilvie R.L., Williams D.A., Reilly C.S., Bohjanen P.R. Tristetraprolin recruits functional mRNA decay complexes to ARE sequences. J. Cell. Biochem. 2007, 100:1477-1492.
29. Stoecklin G., Tenenbaum S.A., Mayo T., Chittur S.V., George A.D., Baroni T.E., Blackshear P.J., Anderson P. Genome-wide analysis identifies interleukin-10 mRNA as target of tristetraprolin. J. Biol. Chem. 2008, 283:11689-11699.
30. Ishmael F.T., Fang X., Galdiero M.R., Atasoy U., Rigby W.F., Gorospe M., Cheadle C., Stellato C. Role of the RNA-binding protein tristetraprolin in glucocorticoid-mediated gene regulation. J. Immunol. 2008, 180:8342-8353.
31. Sanduja S., Blanco F.F., Young L.E., Kaza V., Dixon D.A. The role of tristetraprolin in cancer and inflammation. Front. Biosci. 2012, 17:174-188. (Review).
32. Essafi-Benkhadir K., Onesto C., Stebe E., Moroni C., Pagés G. Tristetraprolin inhibits Ras-dependent tumor vascularization by inducing vascular endothelial growth factor mRNA degradation. Mol. Cell. Biol. 2007, 18:4648-4658.
33. Nabors L.B., Gillespie G.Y., Harkins L., King P.H. HuR, a RNA stability factor, is expressed in malignant brain tumors and binds to adenine- and uridine-rich elements within the 3' untranslated regions of cytokine and angiogenic factor mRNAs. Cancer Res. 2001, 61:2154-2161.
34. Al-Souhibani N., Al-Ahmadi W., Hesketh J.E., Blackshear P.J., Khabar K.S. The RNA-binding zinc-finger protein tristetraprolin regulates AU-rich mRNAs involved in breast cancer-related processes. Oncogene 2010, 29:4205-4215.
35. Ross C.R., Brennan-Laun S.E., Wilson G.M. Tristetraprolin: roles in cancer and senescence. Ageing Res. Rev. 2012, 11:473-484.
36. Brooks S.A., Connolly J.E., Rigby W.F. The role of mRNA turnover in the regulation of tristetraprolin expression: evidence for an extracellular signal-regulated kinase-specific, AU-rich element-dependent, autoregulatory pathway. J. Immunol. 2004, 172:7263-7271.
37. Florkowska M., Tymoszuk P., Balwierz A., Skucha A., Kochan J., Wawro M., Stalinska K., Kasza A. EGF activates TTP expression by activation of ELK-1 and EGR-1 transcription factors. BMC Mol. Biol. 2012, 13:8.
38. Odrowaz Z., Sharrocks A.D. ELK1 uses different DNA binding modes to regulate functionally distinct classes of target genes. PLoS Genet. 2012, 8:e1002694. (Epub 2012 May 10). 10.1371/journal.pgen.1002694.
39. Odrowaz Z., Sharrocks A.D. The ETS transcription factors ELK1 and GABPA regulate different gene networks to control MCF10A breast epithelial cell migration. PLoS One 2012, 7:e49892. (Epub 2012 Dec 20). 10.1371/journal.pone.0049892.
40. Andreasen P.A., Kjøller L., Christensen L., Duffy M.J. The urokinase-type plasminogen activator system in cancer metastasis: a review. Int. J. Cancer 1997, 72:1-22. (Review).
41. Castellino F.J., Ploplis V.A. Structure and function of the plasminogen/plasmin system. Thromb. Haemost. 2005, 93:647-654. (Review).
42. Madureira P.A., O'Connell P.A., Surette A.P., Miller V.A., Waisman D.M. The Biochemistry and Regulation of S100A10: A Multifunctional Plasminogen Receptor Involved in Oncogenesis. J. Biomed. Biotechnol. 2012, 353687. 10.1155/2012/353687.
43. Andreasen P.A., Egelund R., Petersen H.H. The plasminogen activation system in tumor growth, invasion, and metastasis. Cell Mol. Life Sci. 2000, 57:25-40. (Review).
44. Kasza A., Petersen H.H., Heegaard C.W., Oka K., Christensen A., Dubin A., Chan L., Andreasen P.A. Specificity of serine proteinase/serpin complex binding to very-low-density lipoprotein receptor and alpha2-macroglobulin receptor/low-density-lipoprotein-receptor-related protein. Eur. J. Biochem. 1997, 248:270-281.
45. Durand M.K., Bødker J.S., Christensen A., Dupont D.M., Hansen M., Jensen J.K., Kjelgaard S., Mathiasen L., Pedersen K.E., Skeldal S., Wind T., Andreasen P.A. Plasminogen activator inhibitor-I and tumour growth, invasion, and metastasis. Thromb. Haemost. 2004, 91:438-449. (Review).
46. Bruckner A., Filderman A.E., Kirchheimer J.C., Binder B.R., Remold H.G. Endogenous receptor-bound urokinase mediates tissue invasion of the human lung carcinoma cell lines A549 and Calu-1. Cancer Res. 1992, 52:3043-3047.
47. Kobayashi H., Moniwa N., Gotoh J., Sugimura M., Terao T. Role of activated protein C in facilitating basement membrane invasion by tumor cells. Cancer Res. 1994, 54:261-267.
48. Praus M., Collen D., Gerard R.D. Both u-PA inhibition and vitronectin binding by plasminogen activator inhibitor 1 regulate HT1080 fibrosarcoma cell metastasis. Int. J. Cancer 2002, 102:584-591.
49. Liu G., Shuman M.A., Cohen R.L. Co-expression of urokinase, urokinase receptor and PAI-1 is necessary for optimum invasiveness of cultured lung cancer cells. Int. J. Cancer 1995, 60:501-506.
50. Soff G.A., Sanderowitz J., Gately S., Verrusio E., Weiss I., Brem S., Kwaan H.C. Expression of plasminogen activator inhibitor type 1 by human prostate carcinoma cells inhibits primary tumor growth, tumor-associated angiogenesis, and metastasis to lung and liver in an athymic mouse model. J. Clin. Invest. 1995, 96:2593-2600.
51. Harbeck N., Kates R.E., Gauger K., Willems A., Kiechle M., Magdolen V., Schmitt M. Urokinase-type plasminogen activator (uPA) and its inhibitor PAI-I: novel tumor-derived factors with a high prognostic and predictive impact in breast cancer. Thromb Haemost 2004, 91:450-456. (Review).
52. Ghosh A.K., Vaughan D.E. PAI-1 in tissue fibrosis. J. Cell. Physiol. 2012, 227:493-507. (Review).
53. Nagamine Y. Transcriptional regulation of the plasminogen activator inhibitor type 1-with an emphasis on negative regulation. Thromb. Haemost. 2008, 100:1007-1013. (Review).
54. Dimova E.Y., Kietzmann T. Metabolic, hormonal and environmental regulation of plasminogen activator inhibitor-1 (PAI-1) expression: lessons from the liver. Thromb. Haemost. 2008, 100:992-1006. (Review).
55. Wyrzykowska P., Stalińska K., Wawro M., Kochan J., Kasza A. Epidermal growth factor regulates PAI-1 expression via activation of the transcription factor Elk-1. Biochim Biophys Acta - Gene Regul Mech. 2010, 1799:616-621.
56. Kruithof E.K. Regulation of plasminogen activator inhibitor type 1 gene expression by inflammatory mediators and statins. Thromb. Haemost. 2008, 100:969-975. (Review).
57. Zeerleder S., Schroeder V., Hack C.E., Kohler H.P., Wuillemin W.A. TAFI and PAI-1 levels in human sepsis. Thromb. Res. 2006, 118:205-212.
58. Gruber F., Hufnagl P., Hofer-Warbinek R., Schmid J.A., Breuss J.M., Huber-Beckmann R., Lucerna M., Papac N., Harant H., Lindley I., de Martin R., Binder B.R. Direct binding of Nur77/NAK-1 to the plasminogen activator inhibitor 1 (PAI-1) promoter regulates TNF alpha-induced PAI-1 expression. Blood 2003, 101:3042-3048.
59. Kasza A., Kiss D.L., Gopalan S., Xu W., Rydel R.E., Koj A., Kordula T. Mechanism of plasminogen activator inhibitor-1 regulation by oncostatin M and interleukin-1 in human astrocytes. J. Neurochem. 2002, 83:696-703.
60. Thapa B., Kim Y.H., Kwon H.J., Kim D.S. Novel regulatory mechanism and functional implication of plasminogen activator inhibitor-1 (PAI-1) expression in CpG-ODN-stimulated macrophages. Mol. Immunol. 2011, 49:572-581. (Epub 2011 Nov 9). 10.1016/j.molimm.2011.10.004.
61. Buchwalter G., Gross C., Wasylyk B. The ternary complex factor Net regulates cell migration through inhibition of PAI-1 expression. Mol. Cell. Biol. 2005, 25:10853-10862.
62. Ma Z., Paek D., Oh C.K. Plasminogen activator inhibitor-1 and asthma: role in the pathogenesis and molecular regulation. Clin. Exp. Allergy 2009, 39:1136-1144. (Review).
63. De Taeye B., Smith L.H., Vaughan D.E. Plasminogen activator inhibitor-1: a common denominator in obesity, diabetes and cardiovascular disease. Curr. Opin. Pharmacol. 2005, 5:149-154. (Review).
64. Cho S., Kang J., Lyttle C., Harris K., Daley B., Grammer L., Avila P., Kumar R., Schleimer R. Association of elevated plasminogen activator inhibitor 1 levels with diminished lung function in patients with asthma. Ann. Allergy Asthma Immunol. 2011, 106:371-377.
65. Visse R., Nagase H. Matrix metalloproteinases and tissue inhibitors of metalloproteinases: structure, function, and biochemistry. Circ. Res. 2003, 92:827-839. (Review).
66. Bauvois B. New facets of matrix metalloproteinases MMP-2 and MMP-9 as cell surface transducers: outside-in signaling and relationship to tumor progression. Biochim Biophys Acta. 2012, 1825:29-36. (Epub 2011 Oct 12. Review). 10.1016/j.bbcan.2011.10.001.
67. Baluk P., Raymond W.W., Ator E., Coussens L.M., McDonald D.M., Caughey G.H. Matrix metalloproteinase-2 and -9 expression increases in Mycoplasma-infected airways but is not required for microvascular remodeling. Am. J. Physiol. Lung Cell. Mol. Physiol. 2004, 287:307-317. (Epub 2004 Apr 9.).
68. Hotary K., Li X.Y., Allen E., Stevens S.L., Weiss S.J. A cancer cell metalloprotease triad regulates the basement membrane transmigration program. Genes Dev. 2006, 20:2673-2686. (Epub 2006 Sep 18. Erratum in: Genes Dev. 21 (2007) 1139).
69. Sabeh F., Li X.Y., Saunders T.L., Rowe R.G., Weiss S.J. Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion. J. Biol. Chem. 2009, 284:23001-23011. (Epub 2009 Jun 19). 10.1074/jbc.M109.002808.
70. Xu J., Rodriguez D., Petitclerc E., Kim J.J., Hangai M., Moon Y.S., Davis G.E., Brooks P.C. Proteolytic exposure of a cryptic site within collagen type IV is required for angiogenesis and tumor growth in vivo. J. Cell Biol. 2001, 154:1069-1079. (Erratum in: J Cell Biol 155 (2001) 859).
71. Giannelli G., Falk-Marzillier J., Schiraldi O., Stetler-Stevenson W.G., Quaranta V. Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5. Science 1997, 277:225-228.
72. Yu Q., Stamenkovic I. Cell surface-localized matrix metalloproteinase-9 proteolytically activates TGF-beta and promotes tumor invasion and angiogenesis. Genes Dev. 2000, 14:163-176.
73. Yang L., DeBusk L.M., Fukuda K., Fingleton B., Green-Jarvis B., Shyr Y., Matrisian L.M., Carbone D.P., Lin P.C. Expansion of myeloid immune suppressor Gr+CD11b+cells in tumor-bearing host directly promotes tumor angiogenesis. Cancer Cells 2004, 6:409-421.
74. Ardi V.C., den Steen PE Van, Opdenakker G., Schweighofer B., Deryugina E.I., Quigley J.P. Neutrophil MMP-9 proenzyme, unencumbered by TIMP-1, undergoes efficient activation in vivo and catalytically induces angiogenesis via a basic fibroblast growth factor (FGF-2)/FGFR-2 pathway. J. Biol. Chem. 2009, 284:25854-25866. (Epub 2009 Jul 16). 10.1074/jbc.M109.033472.
75. Levi E., Fridman R., Miao H.Q., Ma Y.S., Yayon A., Vlodavsky I. Matrix metalloproteinase 2 releases active soluble ectodomain of fibroblast growth factor receptor 1. Proc. Natl. Acad. Sci. U. S. A. 1996, 93:7069-7074.
76. Gearing A.J., Beckett P., Christodoulou M., Churchill M., Clements J., Davidson A.H., Drummond A.H., Galloway W.A., Gilbert R., Gordon J.L., et al. Processing of tumour necrosis factor-alpha precursor by metalloproteinases. Nature 1994, 370:555-557.
77. Nelissen I., Martens E., Van den Steen P.E., Proost P., Ronsse I., Opdenakker G. Gelatinase B/matrix metalloproteinase-9 cleaves interferon-beta and is a target for immunotherapy. Brain 2003, 126:1371-1381.
78. Gong Y., Hart E., Shchurin A., Hoover-Plow J. Inflammatory macrophage migration requires MMP-9 activation by plasminogen in mice. J. Clin. Invest. 2008, 118:3012-3024. 10.1172/JCI32750.
79. Moore B.A., Manthey C.L., Johnson D.L., Bauer A.J. Matrix metalloproteinase-9 inhibition reduces inflammation and improves motility in murine models of postoperative ileus. Gastroenterology 2011, 141:1283-1292. (Epub 2011 Jun 22, 1292.e1-4). 10.1053/j.gastro.2011.06.035.
80. McQuibban G.A., Gong J.H., Tam E.M., McCulloch C.A., Clark-Lewis I., Overall C.M. Inflammation dampened by gelatinase A cleavage of monocyte chemoattractant protein-3. Science 2000, 289:1202-1206.
81. Hsieh H.L., Wu C.Y., Yang C.M. Bradykinin induces matrix metalloproteinase-9 expression and cell migration through a PKC-delta-dependent ERK/Elk-1 pathway in astrocytes. Glia 2008, 56:619-632. 10.1002/glia.20637.
82. Mahmoodzadeh S., Dworatzek E., Fritschka S., Pham T.H., Regitz-Zagrosek V. 17beta-Estradiol inhibits matrix metalloproteinase-2 transcription via MAP kinase in fibroblasts. Cardiovasc. Res. 2010, 85:719-728. (Epub 2009 Oct 27). 10.1093/cvr/cvp350.
83. Choi B.D., Jeong S.J., Wang G., Park J.J., Lim D.S., Kim B.H., Cho Y.I., Kim C.S., Jeong M.J. Secretory leukocyte protease inhibitor is associated with MMP-2 and MMP-9 to promote migration and invasion in SNU638 gastric cancer cells. Int. J. Mol. Med. 2011, 28:527-534. (Epub 2011 Jun 17). 10.3892/ijmm.2011.726.
84. Ozanne B.W., McGarry L., Spence H.J., Johnston I., Winnie J., Meagher L., Stapleton G. Transcriptional regulation of cell invasion: AP-1 regulation of a multigenic invasion programme. Eur. J. Cancer 2000, 36:1640-1648. (Review).
85. Ozanne B.W., Spence H.J., McGarry L.C., Hennigan R.F. Transcription factors control invasion: AP-1 the first among equals. Oncogene 2007, 26:1-10. (Review).
86. Vickers E.R., Kasza A., Kurnaz I.A., Seifert A., Zeef L.A., O'donnell A., Hayes A., Sharrocks A.D. Ternary complex factor-serum response factor complex-regulated gene activity is required for cellular proliferation and inhibition of apoptotic cell death. Mol. Cell. Biol. 2004, 24:10340-10351.
87. Dittmer J., Nordheim A. Ets transcription factors and human disease. Biochim. Biophys. Acta 1998, 1377:F1-F11.
88. Zhang S., Li F., Li W., Lu W., Zhang L. Expression of Elk-1 in non-small cell lung cancer detected by western blot and tissue microarray. Chinese Journal of Cancer Research 2007, 19:7-11.
89. Yang X., Zhao M., Xia M., Liu Y., Yan J., Ji H., Wang G. Selective requirement for Mediator MED23 in Ras-active lung cancer. Proc. Natl. Acad. Sci. U. S. A. 2012, 109:2813-2822. (Epub 2012 Sep 17). 10.1073/pnas.1204311109.
90. Patki M., Chari V., Sivakumaran S., Gonit M., Trumbly R., Ratnam M. The ETS Domain Transcription Factor Elk1 Directs a Critical Component of Growth Signaling by the Androgen Receptor in Prostate Cancer Cells. J. Biol. Chem. 2013, 288:11047-11065.
91. Ying T.H., Hsieh Y.H., Hsieh Y.S., Liu J.Y. Antisense oligonucleotide Elk-1 suppresses the tumorigenicity of human hepatocellular carcinoma cells. Cell Biol. Int. 2008, 32:210-216. (Epub 2007 Sep 7).
92. Booy E.P., Henson E.S., Gibson S.B. Epidermal growth factor regulates Mcl-1 expression through the MAPK-Elk-1 signalling pathway contributing to cell survival in breast cancer. Oncogene 2011, 30:2367-2378. (Epub 2011 Jan 24). 10.1038/onc.2010.616.
93. Chai Y., Chipitsyna G., Cui J., Liao B., Liu S., Aysola K., Yezdani M., Reddy E.S., Rao V.N. c-Fos oncogene regulator Elk-1 interacts with BRCA1 splice variants BRCA1a/1b and enhances BRCA1a/1b-mediated growth suppression in breast cancer cells. Oncogene 2001, 20:1357-1367.
94. Kasza A. IL-1 and EGF regulate expression of genes important in inflammation and cancer. Cytokine 2013, 62:22-33.