Overexpression of CUGBP1 is associated with the progression of non-small cell lung cancer

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• 作者：Caihong Gao ; Zhuang Yu ; Shihai Liu ; Hou Xin ; Xiumei Li
• 关键词：Non ; small ; cell lung cancer ; CUG ; binding protein 1 ; Apoptosis ; Proliferation ; Prognosis
• 刊名：Tumor Biology
• 出版年：2015
• 出版时间：June 2015
• 年：2015
• 卷：36
• 期：6
• 页码：4583-4589
• 全文大小：993 KB
• 参考文献：1.Hecht SS. Tobacco smoke carcinogens and lung cancer. J Natl Cancer Inst. 1999;91:1194-10.PubMed View Article
  2.Jemal A, Siegel R, Ward E, Hao Y, Xu J, et al. Cancer statistics. CA Cancer J Clin. 2008;58:71-6.PubMed View Article
  3.Siegel R, Naishadham D, Jemal A. Cancer statistics, 2012. CA Cancer J Clin. 2012;62:10-9.PubMed View Article
  4.Kang S, Koh ES, Vinod SK, Jalaludin B. Cost analysis of lung cancer management in South Western Sydney. J Med Imaging Radiat Oncol. 2012;56:235-1.PubMed View Article
  5.Parkin DM, Bray F, Ferlay J, Pisani P. Global cancer statistics, 2002. CA Cancer J Clin. 2005;55:74-08.PubMed View Article
  6.Koshelev M, Sarma S, Price RE, Wehrens XH, Cooper TA. Heart-specific overexpression of CUGBP1 reproduces functional and molecular abnormalities of myotonic dystrophy type 1. Hum Mol Genet. 2010;19:1066-5.PubMed Central PubMed View Article
  7.Ward AJ, Rimer M, Killian JM, Dowling JJ, Cooper TA. CUGBP1 overexpression in mouse skeletal muscle reproduces features of myotonic dystrophy type 1. Hum Mol Genet. 2010;19:3614-2.PubMed Central PubMed View Article
  8.Mulders SA, van den Broek WJ, Wheeler TM, Croes HJ, van Kuik-Romeijn P, et al. Triplet-repeat oligonucleotide-mediated reversal of RNA toxicity in myotonic dystrophy. Proc Natl Acad Sci U S A. 2009;106:13915-0.PubMed Central PubMed View Article
  9.Moraes KC, Wilusz CJ, Wilusz J. CUG-BP binds to RNA substrates and recruits PARN deadenylase. RNA. 2006;12:1084-1.PubMed Central PubMed View Article
  10.Rattenbacher B, Beisang D, Wiesner DL, Jeschke JC, von Hohenberg M, et al. Analysis of CUGBP1 targets identifies GU-repeat sequences that mediate rapid mRNA decay. Mol Cell Biol. 2010;30:3970-0.PubMed Central PubMed View Article
  11.Vlasova IA, Tahoe NM, Fan D, Larsson O, Rattenbacher B, et al. Conserved GU-rich elements mediate mRNA decay by binding to CUG-binding protein 1. Mol Cell. 2008;29:263-0.PubMed Central PubMed View Article
  12.Zheng Y, Miskimins WK. CUG-binding protein represses translation of p27Kip1 mRNA through its internal ribosomal entry site. RNA Biol. 2011;8:365-1.PubMed Central PubMed View Article
  13.Zhang L, Lee JE, Wilusz J, Wilusz CJ. The RNA-binding protein CUGBP1 regulates stability of tumor necrosis factor mRNA in muscle cells: implications for myotonic dystrophy. J Biol Chem. 2008;283:22457-3.PubMed Central PubMed View Article
  14.Salisbury E, Sakai K, Schoser B, Huichalaf C, Schneider-Gold C, et al. Ectopic expression of cyclin D3 corrects differentiation of DM1 myoblasts through activation of RNA CUG-binding protein, CUGBP1. Exp Cell Res. 2008;314:2266-8.PubMed Central PubMed View Article
  15.Jiao W, Zhao J, Wang M, Wang Y, Luo Y, et al. CUG-binding protein 1 (CUGBP1) expression and prognosis of non-small cell lung cancer. Clin Transl Oncol. 2013;15:789-5.PubMed View Article
  16.Gartel AL, Kandel ES. RNA interference in cancer. Biomol Eng. 2006;23:17-4.PubMed View Article
  17.Talwar S, Balasubramanian S, Sundaramurthy S, House R, Wilusz CJ, et al. Overexpression of RNA-binding protein CELF1 prevents apoptosis and destabilizes pro-apoptotic mRNAs in oral cancer cells. RNA Biol. 2013;10:277-6.PubMed Central PubMed View Article
  18.Zhou BP, Hung MC. Wnt, hedgehog and snail: sister pathways that control by GSK-3beta and beta-Trcp in the regulation of metastasis. Cell Cycle. 2005;4:772-.PubMed View Article
  19.Ciervide R, Dhage S, Guth A, Shapiro RL, Axelrod DM, et al. Five year outcome of 145 patients with ductal carcinoma in situ (DCIS) after accelerated breast radiotherapy. Int J Radiat Oncol Biol Phys. 2012;83:e159-4.PubMed View Article
  20.Oji Y, Kitamura Y, Kamino E, Kitano A, Sawabata N, et al. WT1 IgG antibody for early detection of nonsmall cell lung cancer and as its prognostic factor. Int J Cancer. 2009;125:381-.PubMed View Article
  21.Beisang D, Rattenbacher B, Louis IAV, Bohjanen PR. Regulation of CUG-binding protein 1 (CUGBP1) binding to target transcripts upon T cell activation. J Biol Chem. 2012;287:950-0.PubMed Central PubMed View Article
  22.Gareau C, Fournier M, Filion C, Coudert L, Martel D, et al. p21WAF1/CIP1 upregulation through the stress granule-associated protein CUGBP1 confers resistance to bortezomib-mediated apoptosis. PLoS One. 2011;6:e20254.PubMed Central PubMed View Article
  23.Greenburg G, Hay ED. Epithelia suspended in collagen gels can lose polarity and express characteristics of migrating mesenchymal cells. J Cell Biol. 1982;95:333-.PubMed View Article
  
• 作者单位：Caihong Gao (1)
  Zhuang Yu (1)
  Shihai Liu (2)
  Hou Xin (1)
  Xiumei Li (1)
  
  1. Department of Oncology, The Affiliated Hospital of Qingdao University, Qingdao, Shandong, 266071, People’s Republic of China
  2. The Central Laboratory, The Affiliated Hospital of Qingdao University, Qingdao, Shandong, People’s Republic of China
  
• 刊物主题：Cancer Research;
• 出版者：Springer Netherlands
• ISSN：1423-0380

文摘

The multifunctional RNA-binding protein CUGBP1 regulates multiple aspects of nuclear and cytoplasmic messenger RNA (mRNA) processing, including splicing, stabilization, and translation of mRNAs. Previous studies have shown that CUGBP1 is overexpressed in non-small-cell lung cancer (NSCLC) tissues, but the pathological functions of CUGBP1 in tumorigenesis and development are unknown. Here, we provide the first evidence demonstrating the clinicopathological significance of CUGBP1 in NSCLC. Using immunohistochemistry, the levels of CUGBP1 expression in NSCLC tissues and adjacent non-cancerous tissues were examined and determined to be associated with differentiation. Short hairpin RNA-induced downregulation of CUGBP1 promoted apoptosis and decreased proliferation in the A549 NSCLC cell line. Moreover, Western blot analysis indicated that the depletion of CUGBP1 increased the protein levels of cyclin D1, BAD, BAX, Jun D, and E-cadherin, while the cyclin B1 level decreased. Knockdown of CUGBP1 decreased β-catenin and vimentin levels and increased E-cadherin expression, suggesting that CUGBP1 may contribute significantly to epithelial to mesenchymal transition (EMT) progression. These results demonstrate the importance of CUGBP1 in the biological and pathological functions of NSCLC and indicate its potential as a therapeutic target for NSCLC.