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NonO蛋白在丁酸钠诱导小鼠红白血病细胞分化过程中的表达
桑婷婷 胡江江 薛建有 戚武林 赵辅昆 张世馥*
解剖学报 ›› 2014, Vol. 45 ›› Issue (4) : 516-520.
NonO蛋白在丁酸钠诱导小鼠红白血病细胞分化过程中的表达
Expression of NonO protein during murine erythroleukemia cell differentiation induced by sodium butyrate
目的 探讨NonO蛋白在丁酸钠诱导小鼠红白血病（MEL）细胞向红细胞系分化过程中的表达变化。方法 利用联苯胺染色观察丁酸钠诱导MEL细胞红细胞系分化情况，通过Western blotting、免疫细胞化学检测NonO蛋白在丁酸钠诱导MEL细胞分化的过程中表达量的变化，PCR技术检测NonO基因在RNA水平上的表达变化，免疫细胞化学技术检测NonO蛋白在MEL细胞中的定位。 结果 发现NonO在丁酸钠诱导MEL细胞向红细胞系分化过程中在基因水平和蛋白水平上均上调表达，NonO蛋白在MEL细胞中定位于细胞质和细胞核。结论 NonO蛋白与丁酸钠诱导MEL细胞分化密切相关。
Objective To study NonO protein expression changes in murine erythroleukemia (MEL) cell differentiation induced by sodium butyrate.Methods Benzidine staining was used to test sodium butyrate-induced erythroid differentiation of MEL cells. We detected NonO protein expression changes in MEL cell differentiation induced by sodium butyrate and NonO protein localization in MEL cells by Western blotting and immunocytochemistry. Furthermore, we applied PCR technique to detect NonO RNA expression in differentiation process. Results We found that NonO protein was upregulated at gene and protein levels in the erythroid differentiation process of MEL cells induced by sodium butyrate and located in cytoplasm and nucleus in MEL cells. Conclusion These results show that NonO protein is closely related with MEL cell differentiation induced by sodium butyrate，which may provide important clues for further study of the mechanism of leukemia.
NonO蛋白 / 小鼠红白血病细胞 / 丁酸钠 / 红细胞系 / 分化 / 免疫组织化学 / 免疫印迹法
NonO protein / Murine erythroleukemia cell / Sodium butyrate / Erythroid / Differentiation / Immunohistochemistry / Western blotting
［1］Hanke JH, Landolfi NF, Tucker PW, et al. Identification of murine nuclear proteins that bind to the conserved octamer sequence of the immunoglobulin promoter region［J］. Proc Natl Acad Sci USA, 1988, 85(10): 3560-3564.
［2］Dong B, Horowitz DS, Kobayashi R, et al. Purification and cDNA cloning of HeLa cell p54nrb, a nuclear protein with two RNA recognition motifs and extensive homology to human splicing factor PSF and drosophila NONA/BJ6［J］. Nucleic Acids Res, 1993, 21(17): 4085-4092.
［3］Krietsch J, Caron MC, Gagne JP, et al. PARP activation regulates the RNA-binding protein NONO in the DNA damage response to DNA double-strand breaks［J］. Nucleic Acids Res, 2012, 40(20): 10287-10301.
［4］Ong SA, Tan JJ, Tew WL, et al. Rasd1 modulates the coactivator function of NonO in the cyclic AMP pathway［J］. PLoS One, 2011, 6(9): e24401.
［5］Salton M, Lerenthal Y, Wang SY,et al. Involvement of Matrin 3 and STPQ/NONO in the DNA damage response［J］. Cell Cycle, 2010, 9(8): 1568-1576.
［6］Shav-Tal Y, Zipori D. PSF and p54(nrb)/NonO—multi-functional nuclear proteins［J］. FEBS Letters, 2002, 531(2): 109-114.
［7］Emili A, Shales M, McCracken S,et al. Splicing and transcription-associated proteins PSF and p54nrb/NonO bind to the RNA polymerase II CTD［J］. RNA, 2002, 8(9): 1102-1111.
［8］Yang YS, Yang MC, Tucker PW, et al. NonO enhances the association of many DNA-binding proteins to their targets［J］. Nucleic Acids Res, 1997, 25(12): 2284-2292.
［9］Izumi H, McCloskey A, Shinmyozu K,et al. p54nrb/NonO and PSF promote U snRNA nuclear export by accelerating its export complex assembly［J］. Nucleic Acids Res, 2014,42(6):3998-4007.
［10］Yadav SP, Hao H, Yang HJ, et al. The transcription-splicing protein NonO/p54nrb and three NonO-interacting proteins bind to distal enhancer region and augment rhodopsin expression［J］. Hum Mole Genet, 2014, 23(8):2132-2144.
［11］Schiffner S, Zimara N, Schmid R, et al. p54nrb is a new regulator of progression of malignant melanoma［J］. Carcinogenesis, 2011, 32(8): 1176-1182.
［12］Clark J, Lu YJ, Sidhar SK, et al. Fusion of splicing factor genes psf and NonO (p54nrb) to the TFE3 gene in papillary renal cell carcinoma［J］. Oncogene, 1997, 15(18): 2233-2239.
［13］Dammer EB, Fallini C, Gozal YM, et al. Coaggregation of RNA-binding proteins in a model of TDP-43 proteinopathy with selective RGG motif methylation and a role for RRM1 ubiquitination［J］. PLoS One, 2012, 7(6): e38658.
［14］Hallier M, Tavitian A, Moreau-Gachelin F. The transcription factor Spi-1/PU.1 binds RNA and interferes with the RNA-binding protein p54nrb［J］. J Biol Chem, 1996, 271(19): 11177-11181.
［15］Davie JR. Inhibition of histone deacetylase activity by butyrate［J］. J Nutr, 2003, 133(7): 2485S-2493S.
［16］Li L, Zhang G, Zhang Y, et al. Sodium butyrate-induced upregulation of p18( INK4C) gene affects K562 cell G(0)/G (1) arrest and differentiation［J］. Mol Cell Biochem, 2008, 319(1-2): 9-15.
［17］Lozzio CB, Lozzio BB, Machado EA, et al. Effects of sodium butyrate on human chronic myelogenous leukaemia cell line K562［J］. Nature, 1979, 281(5733): 709-710.
［18］Rivero JA, Adunyah SE. Sodium butyrate induces tyrosine phosphorylation and activation of MAP kinase (ERK-1) in human K562 cells［J］. Biochem Biophys Rese Commun, 1996, 224(3): 796-801.
［19］Friend C, Scher W, Holland JG, et al. Hemoglobin synthesis in murine virus-induced leukemic cells in vitro: stimulation of erythroid differentiation by dimethyl sulfoxide［J］. Proc Natl Acad Sci USA, 1971, 68(2): 378-382.
［20］Gomes I, Sharma TT, Edassery S, et al. Novel transcription factors in human cd34 antigen-positive hematopoietic cells［J］. Blood, 2002, 100(1): 107-119.
［21］Voo KS, Skalnik DG. Elf-1 and PU.1 induce expression of gp91(phox) via a promoter element mutated in a subset of chronic granulomatous disease patients［J］. Blood, 1999, 93(10): 3512-3520.
［22］Fisher RC, Slayton WB, Chien C, et al. PU.1 supports proliferation of immature erythroid progenitors［J］. Leuk Res, 2004, 28(1): 83-89.
［23］Park Y, Lee JM, Hwang MY, et al. NonO binds to the CPG island of oct4 promoter and functions as a transcriptional activator of oct4 gene expression［J］. Mol Cells, 2013, 35(1): 61-69.
［24］Yang YS, Hanke JH, Carayannopoulos L, et al. NonO, a non-POU-domain-containing, octamer-binding protein, is the mammalian homolog of Drosophila nonAdiss［J］. Mol Cell Biol, 1993, 13(9): 5593-5603.
［25］Hui DY. A no-no for NonO and JNK in extracellular matrix homeostasis and vascular stability［J］. Arterioscler Thromb, Vasc Biol, 2007, 27(8): 1677-1678.
［26］Zhang C, Zhang MX, Shen YH, et al. Role of NonO-histone interaction in TNFalpha-suppressed prolyl-4-hydroxylase alpha1［J］. Biochim Biophys Acta, 2008, 1783(8): 1517-1528.
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