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Post-transcriptional Regulation of NK Cell Activation

  • Kim, Tae-Don (Cell Therapy Research Center, Korea Research Institute of Bioscience and Biotechnology, University of Science and Technology) ;
  • Park, Ju-Yeong (Cell Therapy Research Center, Korea Research Institute of Bioscience and Biotechnology, University of Science and Technology) ;
  • Choi, In-Pyo (Cell Therapy Research Center, Korea Research Institute of Bioscience and Biotechnology, University of Science and Technology)
  • Received : 2009.05.26
  • Accepted : 2009.06.02
  • Published : 2009.08.31
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Abstract

Natural killer (NK) cells play key roles in innate and adaptive immune defenses. NK cell responses are mediated by two major mechanisms: the direct cytolysis of target cells, and immune regulation by production of various cytokines. Many previous reports show that the complex NK cell activation process requires de novo gene expression regulated at both transcriptional and post-transcriptional levels. Specialized un-translated regions (UTR) of mRNAs are the main mechanisms of post-transcriptional regulation. Analysis of posttranscriptional regulation is needed to clearly understand NK cell biology and, furthermore, harness the power of NK cells for therapeutic aims. This review summarizes the current understanding of mRNA metabolism during NK cell activation, focusing primarily on post-transcriptional regulation.

Keywords

References

  1. V\acute{e}ly F, Vivier E: Natural killer cell receptor signaling pathway in mammals. Sci STKE 12;cm7, 2005
  2. Shu Y, Hong-Hui L: Transcription, translation, degradation,and circadian clock. Biochem Biophys Res Commun 321;1-6, 2004 https://doi.org/10.1016/j.bbrc.2004.06.093
  3. Allgayer H: Regulation and clinical significance of urokinase-receptor (u-PAR), an invasion-related molecule. Z Gastroenterol 44;503-511, 2006 https://doi.org/10.1055/s-2006-926584
  4. Shetty S: Protein synthesis and urokinase mRNA metabolism. Mol Cell Biochem 271;13-22, 2005 https://doi.org/10.1007/s11010-005-3453-x
  5. Velusamy T, Shetty P, Bhandary YP, Liu MC, Shetty S:Posttranscriptional regulation of urokinase receptor expression by heterogeneous nuclear ribonuclear protein C. Biochemistry 47;6508-6517, 2008 https://doi.org/10.1021/bi702338y
  6. Shetty P, Velusamy T, Bhandary YP, Shetty RS, Liu MC, Shetty S: Urokinase expression by tumor suppressor protein p53: a novel role in mRNA turnover. Am J Respir Cell Mol Biol 39;364-372, 2008 https://doi.org/10.1165/rcmb.2007-0406OC
  7. Shetty S, Velusamy T, Idell S, Shetty P, Mazar AP, Bhandary YP, Shetty RS: Regulation of urokinase receptor expression by p53: novel role in stabilization of uPAR mRNA. Mol Cell Biol 27;5607-5618, 2007 https://doi.org/10.1128/MCB.00080-07
  8. Al-Atrash G, Shetty S, Idell S, Xue Y, Kitson RP, Halady PK, Goldfarb RH: IL-2-mediated upregulation of uPA and uPAR in natural killer cells. Biochem Biophys Res Commun 292;184-189, 2002 https://doi.org/10.1006/bbrc.2002.6627
  9. Suarez-Alvarez B, Lopez-Vazquez A, Baltar JM, Ortega F, Lopez-Larrea C: Potential role of NKG2D and its ligands in organ transplantation: new target for immunointervention. Am J Transplant 9;251-257, 2009 https://doi.org/10.1111/j.1600-6143.2008.02526.x
  10. Stern-Ginossar N, Elefant N, Zimmermann A, Wolf DG, Saleh N, Biton M, Horwitz E, Prokocimer Z, Prichard M, Hahn G, Goldman-Wohl D, Greenfield C, Yagel S, Hengel H, Altuvia Y, Margalit H, Mandelboim O: Host immune sys tem gene targeting by a viral miRNA. Science 317;376-381,2007 https://doi.org/10.1126/science.1140956
  11. Stern-Ginossar N, Gur C, Biton M, Horwitz E, Elboim M, Stanietsky N, Mandelboim M, Mandelboim O: Human microRNAs regulate stress-induced immune responses mediated by the receptor NKG2D. Nat Immunol 9;1065-1073, 2008 https://doi.org/10.1038/ni.1642
  12. Cai SF, Fehniger TA, Cao X, Mayer JC, Brune JD, French AR, Ley TJ: Differential expression of granzyme B and C in murine cytotoxic lymphocytes. J Immunol 182;6287-6297, 2009 https://doi.org/10.4049/jimmunol.0804333
  13. Chowdhury D, Lieberman J: Death by a thousand cuts: granzyme pathways of programmed cell death. Annu Rev Immunol 26;389-420, 2008 https://doi.org/10.1146/annurev.immunol.26.021607.090404
  14. Fehniger TA, Cai SF, Cao X, Bredemeyer AJ, Presti RM,French AR, Ley TJ: Acquisition of murine NK cell cytotoxicity requires the translation of a pre-existing pool of granzyme B and perforin mRNAs. Immunity 26;798-811, 2007 https://doi.org/10.1016/j.immuni.2007.04.010
  15. Hodge DL, Martinez A, Julias JG, Taylor LS, Young HA: Regulation of nuclear gamma interferon gene expression by interleukin 12 (IL-12) and IL-2 represents a novel form of posttranscriptional control. Mol Cell Biol 22;1742-1753, 2002 https://doi.org/10.1128/MCB.22.6.1742-1753.2002
  16. Eberhardt W, Doller A, Akool el S, Pfeilschifter J: Modulation of mRNA stability as a novel therapeutic approach. Pharmacol Ther 114;56-73, 2007 https://doi.org/10.1016/j.pharmthera.2007.01.002
  17. Ogilvie RL, Sternjohn JR, Rattenbacher B, Vlasova IA, Williams DA, Hau HH, Blackshear PJ, Bohjanen PR: Tristetraprolin mediates interferon-gamma mRNA decay. J Biol Chem 284;11216-11223, 2009 https://doi.org/10.1074/jbc.M901229200
  18. Nagy E, Buhlmann JE, Henics T, Waugh M, Rigby WF:Selective modulation of IFN-gamma mRNA stability by IL-12/NKSF. Cell Immunol 159;140-151, 1994 https://doi.org/10.1006/cimm.1994.1303
  19. Muller WE, Slor H, Pfeifer K, Huhn P, Bek A, Orsulic S, Ushijima H, Schroder HC: Association of AUUUA-binding protein with A+U-rich mRNA during nucleo-cytoplasmic transport. J Mol Biol 226;721-733, 1992 https://doi.org/10.1016/0022-2836(92)90628-W
  20. Paste M, Huez G, Kruys V: Deadenylation of interferon-beta mRNA is mediated by both the AU-rich element in the 3'-untranslated region and an instability sequence in the coding region. Eur J Biochem 270;1590-1597, 2003 https://doi.org/10.1046/j.1432-1033.2003.03530.x
  21. Tarr PE: Granulocyte-macrophage colony-stimulating factor and the immune system. Med Oncol 13;133-140, 1996 https://doi.org/10.1007/BF02990841
  22. Dranoff G: GM-CSF-based cancer vaccines. Immunol Rev 188;147-154, 2002 https://doi.org/10.1034/j.1600-065X.2002.18813.x
  23. Buzby JS, Brewer G, Nugent DJ: Developmental regulation of RNA transcript destabilization by A+U-rich elements is AUF1-dependent. J Biol Chem 274;33973-33978, 1999 https://doi.org/10.1074/jbc.274.48.33973
  24. Xu N, Chen CY, Shyu AB: Versatile role for hnRNP D isoforms in the differential regulation of cytoplasmic mRNA turnover. Mol Cell Biol 21;6960-6971, 2001 https://doi.org/10.1128/MCB.21.20.6960-6971.2001
  25. Raineri I, Wegmueller D, Gross B, Certa U, Moroni C: Roles of AUF1 isoforms, HuR and BRF1 in ARE-dependent mRNA turnover studied by RNA interference. Nucleic Acids Res 32;1279-1288, 2004 https://doi.org/10.1093/nar/gkh282
  26. Fan XC, Steitz JA: Overexpression of HuR, a nuclear-cytoplasmic shuttling protein, increases the in vivo stability of ARE-containing mRNAs. EMBO J 17;3448-3460, 1998 https://doi.org/10.1093/emboj/17.12.3448
  27. Lykke-Andersen J, Wagner E: Recruitment and activation of mRNA decay enzymes by two ARE-mediated decay activation domains in the proteins TTP and BRF-1. Genes Dev 19;351-361, 2005 https://doi.org/10.1101/gad.1282305
  28. Shaw G, Kamen R: A conserved AU sequence from the 3' untranslated region of GM-CSF mRNA mediates selective mRNA degradation. Cell 46;659-667, 1986 https://doi.org/10.1016/0092-8674(86)90341-7
  29. Kruys V, Marinx O, Shaw G, Deschamps J, Huez G:Translational blockade imposed by cytokine-derived UA-rich sequences. Science 245;852-855, 1989 https://doi.org/10.1126/science.2672333
  30. Jarzembowski JA, Rajagopalan LE, Shin HC, Malter JS: The 5'-untranslated region of GM-CSF mRNA suppresses translational repression mediated by the 3' adenosine-uridine-rich element and the poly(A) tail. Nucleic Acids Res 27; 3660-3666, 1999 https://doi.org/10.1093/nar/27.18.3660
  31. Blount DG, Riley EM: IL-10: the master regulator of immunity to infection. J Immunol 180; 5771-7577, 2008 https://doi.org/10.4049/jimmunol.180.9.5771
  32. Maroof A, Beattie L, Zubairi S, Svensson M, Stager S, Kaye PM: Posttranscriptional regulation of II10 gene expression allows natural killer cells to express immunoregulatory function. Immunity 29;295-305, 2008 https://doi.org/10.1016/j.immuni.2008.06.012
  33. Nemeth ZH, Lutz CS, Csoka B, Deitch EA, Leibovich SJ, Gause WC, Tone M, Pacher P, Vizi ES, Hasko G: Adenosine augments IL-10 production by macrophages through an A2B receptor-mediated posttranscriptional mechanism. J Immunol 175;8260-8270, 2005 https://doi.org/10.4049/jimmunol.175.12.8260
  34. Sarkar S, Sinsimer KS, Foster RL, Brewer G, Pestka S: AUF1 isoform-specific regulation of anti-inflammatory IL10 expression in monocytes. (Translated from eng) J Interferon Cytokine Res 28;679-691, 2008 https://doi.org/10.1089/jir.2008.0028
  35. Brewer G, Saccani S, Sarkar S, Lewis A, Pestka S: Increased interleukin-10 mRNA stability in melanoma cells is associated with decreased levels of A+U-rich element binding factor AUF1. (Translated from eng) J Interferon Cytokine Res 23;553-564, 2003 https://doi.org/10.1089/107999003322485053
  36. Sharma A, Kumar M, Aich J, Hariharan M, Brahmachari SK, Agrawal A, Ghosh B: Posttranscriptional regulation of interleukin- 10 expression by hsa-miR-106a. Proc Natl Acad Sci U S A 106;5761-5766, 2009 https://doi.org/10.1073/pnas.0808743106
  37. Aggarwal BB, Shishodia S, Takada Y, Jackson-Bernitsas D,Ahn KS, Sethi G, Ichikawa H: TNF blockade: an inflammatory issue. Ernst Schering Res Found Workshop 161-186, 2006
  38. Dean JL, Wait R, Mahtani KR, Sully G, Clark AR, Saklatvala J: The 3' untranslated region of tumor necrosis factor alpha mRNA is a target of the mRNA-stabilizing factor HuR. Mol Cell Biol 21;721-730, 2001 https://doi.org/10.1128/MCB.21.3.721-730.2001
  39. Katsanou V, Papadaki O, Milatos S, Blackshear PJ, Anderson P, Kollias G, Kontoyiannis DL: HuR as a negative posttranscriptional modulator in inflammation. Mol Cell 19; 777-789, 2005 https://doi.org/10.1016/j.molcel.2005.08.007
  40. Ford LP, Watson J, Keene JD, Wilusz J: ELAV proteins stabilize deadenylated intermediates in a novel in vitro mRNA deadenylation/degradation system. Genes Dev 13;188-201, 1999 https://doi.org/10.1101/gad.13.2.188
  41. Tsutsumi A, Suzuki E, Adachi Y, Murata H, Goto D, Kojo S, Matsumoto I, Zhong L, Nakamura H, Sumida T: Expression of tristetraprolin (G0S24) mRNA, a regulator of tumor necrosis factor-alpha production, in synovial tissues of patients with rheumatoid arthritis. J Rheumatol 31; 1044-1049, 2004
  42. Zhang T, Kruys V, Huez G, Gueydan C: AU-rich element-mediated translational control: complexity and multiple activities of trans-activating factors. Biochem Soc Trans 30;952-958, 2002 https://doi.org/10.1042/BST0300952
  43. Piecyk M, Wax S, Beck AR, Kedersha N, Gupta M, Maritim B, Chen S, Gueydan C, Kruys V, Streuli M, Anderson P: TIA-1 is a translational silencer that selectively regulates the expression of TNF-alpha. EMBO J 19;4154-4163, 2000 https://doi.org/10.1093/emboj/19.15.4154
  44. Shi MM, Godleski JJ, Paulauskis JD: Molecular cloning and posttranscriptional regulation of macrophage inflammatory protein-1 alpha in alveolar macrophages. Biochem Biophys Res Commun 211;289-295, 1995 https://doi.org/10.1006/bbrc.1995.1809

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