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Structural Study on Apoptosis of Chronic Eosinophilic Leukemia Cells by Interaction of S100A8 with Splicing Factor, Proline and Glutamine-Rich

  • Won, Yubin (Department of Biomedical Laboratory Science, College of Health Science, Eulji University) ;
  • Choi, Hyosun (BK21 Plus Program, Department of Senior Healthcare, Graduate School, Eulji University) ;
  • Kim, In Sik (BK21 Plus Program, Department of Senior Healthcare, Graduate School, Eulji University) ;
  • Mun, Ji Young (Department of Biomedical Laboratory Science, College of Health Science, Eulji University)
  • Received : 2017.11.08
  • Accepted : 2017.12.15
  • Published : 2017.12.30

Abstract

Chronic eosinophilic leukemia (CEL) is a myeloproliferative disease with an increased number of mature eosinophils and their precursors, which results in infiltration into organs and organ enlargement. The main cause of this disease is the overexpression of tyrosine kinase. However, there is a need for alternative medication, because some patients are resistant to imatinib, which is a tyrosine kinase inhibitor for leukemia. Many studies have indicated that S100A8 and splicing factor proline and glutamine-rich (SFPQ) function as initiation signals of apoptosis in CEL cells. We reviewed structural studies on CEL cells related to S100A8 and SFPQ. Particularly, this review highlighted microscopic results for the study of S100A8 and SFPQ in CEL cells.

Keywords

References

  1. Asakura M, Karaki F, Fujii H, Atsuda K, Itoh T, and Fujiwara R (2016) Vildagliptin and its metabolite M20.7 induce the expression of S100A8 and S100A9 in human hepatoma HepG2 and leukemia HL-60 cells. Sci Rep 6, 35633. https://doi.org/10.1038/srep35633
  2. Bresnick A R, Weber D J, and Zimmer D B (2015) S100 proteins in cancer. Nat Rev Cancer 15, 96-109. https://doi.org/10.1038/nrc3893
  3. Chakraborty P, Bjork P, Kallberg E, Olsson A, Riva M, Morgelin M, Liberg D, Ivars F, and Leanderson T (2015) Vesicular location and transport of S100A8 and S100A9 proteins in monocytoid cells. PLoS One 10, e0145217. https://doi.org/10.1371/journal.pone.0145217
  4. Demoulin J B and Montano-Almendras C P (2012) Platelet-derived growth factors and their receptors in normal and malignant hematopoiesis. Am J Blood Res 2, 44-56.
  5. Donato R, Cannon B R, Sorci G, Riuzzi F, Hsu K, Weber D J, and Geczy C L (2013) Functions of S100 proteins. Curr Mol Med 13, 24-57. https://doi.org/10.2174/156652413804486214
  6. Dvinge H, Kim E, Abdel-Wahab O, and Bradley R K (2016) RNA splicing factors as oncoproteins and tumour suppressors. Nat Rev Cancer 16, 413-430. https://doi.org/10.1038/nrc.2016.51
  7. Falchi L and Verstovsek S (2015) Eosinophilia in hematologic disorders. Immunol Allergy Clin North Am 35, 439-452. https://doi.org/10.1016/j.iac.2015.04.004
  8. Gotlib J (2015) World Health Organization-defined eosinophilic disorders: 2015 update on diagnosis, risk stratification, and management. Am J Hematol 90, 1077-1089. https://doi.org/10.1002/ajh.24196
  9. Gotlib J, Cools J, Malone J M 3rd, Schrier S L, Gilliland D G, and Coutre S E (2004) The FIP1L1-PDGFRalpha fusion tyrosine kinase in hypereosinophilic syndrome and chronic eosinophilic leukemia: implications for diagnosis, classification, and management. Blood 103, 2879-2891. https://doi.org/10.1182/blood-2003-06-1824
  10. Kerkhoff C, Nacken W, Benedyk M, Dagher M C, Sopalla C, and Doussiere J (2005) The arachidonic acid-binding protein S100A8/A9 promotes NADPH oxidase activation by interaction with p67phox and Rac-2. FASEB J 19, 467-469. https://doi.org/10.1096/fj.04-2377fje
  11. Kujak C and Kolesar J M (2016) Treatment of chronic myelogenous leukemia. Am J Health Syst Pharm 73, 113-120. https://doi.org/10.2146/ajhp140686
  12. Landeras-Bueno S, Jorba N, Perez-Cidoncha M, and Ortin J (2011) The splicing factor proline-glutamine rich (SFPQ/PSF) is involved in influenza virus transcription. PLoS Pathog 7, e1002397. https://doi.org/10.1371/journal.ppat.1002397
  13. Lee M, Sadowska A, Bekere I, Ho D, Gully B S, Lu Y, Iyer K S, Trewhella J, Fox A H, and Bond C S (2015) The structure of human SFPQ reveals a coiled-coil mediated polymer essential for functional aggregation in gene regulation. Nucleic Acids Res 43, 3826-3840. https://doi.org/10.1093/nar/gkv156
  14. Maru Y, Tomita T, Deguchi A, Ieguchi K, Takita M, Tsukahara F, Takemura K, Kitao A, and Gusovsky F (2015) Drug targeting based on a new concept-targeting against TLR4 as an example. Endocr Metab Immune Disord Drug Targets 15, 83-87. https://doi.org/10.2174/187153031502150522123746
  15. Narumi K, Miyakawa R, Ueda R, Hashimoto H, Yamamoto Y, Yoshida T, and Aoki K (2015) Proinflammatory proteins S100A8/S100A9 activate NK cells via interaction with RAGE. J Immunol 194, 5539-5548. https://doi.org/10.4049/jimmunol.1402301
  16. Patton J G, Porro E B, Galceran J, Tempst P, and Nadal-Ginard B (1993) Cloning and characterization of PSF, a novel pre-mRNA splicing factor. Genes Dev 7, 393-406. https://doi.org/10.1101/gad.7.3.393
  17. Quiskamp N, Poeter M, Raabe C A, Hohenester U M, Konig S, Gerke V, and Rescher U (2014) The tumor suppressor annexin A10 is a novel component of nuclear paraspeckles. Cell Mol Life Sci 71, 311-329. https://doi.org/10.1007/s00018-013-1375-4
  18. Ren S, She M, Li M, Zhou Q, Liu R, Lu H, Yang C, and Xiong D (2014) The RNA/DNA-binding protein PSF relocates to cell membrane and contributes cells' sensitivity to antitumor drug, doxorubicin. Cytometry A 85, 231-241. https://doi.org/10.1002/cyto.a.22423
  19. Shav-Tal Y, Lee B C, Bar-Haim S, Schori H, and Zipori D (2001) Reorganization of nuclear factors during myeloid differentiation. J Cell Biochem 81, 379-392. https://doi.org/10.1002/1097-4644(20010601)81:3<379::AID-JCB1052>3.0.CO;2-8
  20. Sury M D, McShane E, Hernandez-Miranda L R, Birchmeier C, and Selbach M (2015) Quantitative proteomics reveals dynamic interaction of c-Jun N-terminal kinase (JNK) with RNA transport granule proteins splicing factor proline- and glutamine-rich (Sfpq) and non-POU domain-containing octamer-binding protein (Nono) during neuronal differentiation. Mol Cell Proteomics 14, 50-65. https://doi.org/10.1074/mcp.M114.039370
  21. Yang L, Yang M, Zhang H, Wang Z, Yu Y, Xie M, Zhao M, Liu L, and Cao L (2012) S100A8-targeting siRNA enhances arsenic trioxide-induced myeloid leukemia cell death by down-regulating autophagy. Int J Mol Med 29, 65-72.
  22. Yang M, Zeng P, Kang R, Yu Y, Yang L, Tang D, and Cao L (2014) S100A8 contributes to drug resistance by promoting autophagy in leukemia cells. PLoS One 9, e97242. https://doi.org/10.1371/journal.pone.0097242
  23. Yang X Y, Zhang M Y, Zhou Q, Wu S Y, Zhao Y, Gu W Y, Pan J, Cen J N, Chen Z X, Guo W G, Chen C S, Yan W H, and Hu S Y (2016) High expression of S100A8 gene is associated with drug resistance to etoposide and poor prognosis in acute myeloid leukemia through influencing the apoptosis pathway. Onco Targets Ther 9, 4887-4899. https://doi.org/10.2147/OTT.S101594
  24. Zolotukhin A S, Michalowski D, Bear J, Smulevitch S V, Traish A M, Peng R, Patton J, Shatsky I N and Felber B K (2003) PSF acts through the human immunodeficiency virus type 1 mRNA instability elements to regulate virus expression. Mol Cell Biol 23, 6618-6630. https://doi.org/10.1128/MCB.23.18.6618-6630.2003