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Differential protein expression between EBV-positive and negative epithelial cells
Cancer Research Institute, Central South University, Changsha, China
Department of Gastroenterology, Third Xiangya Hospital, Central South University, Changsha, China
Cancer Research Institute, Central South University, Changsha, China
Cancer Research Institute, Central South University, Changsha, China
Cancer Research Institute, Central South University, Changsha, China
Cancer Research Institute, Central South University, Changsha, China
Cancer Research Institute, Central South University, Changsha, China
Department of Gastroenterology, Third Xiangya Hospital, Central South University, Changsha, China
Cancer Research Institute, Central South University, Changsha, China
Cancer Research Institute, Central South University, Changsha, China
Cancer Research Institute, Central South University, Changsha, China
- 1 Cancer Research Institute, Central South University, Changsha, China
- 2 Department of Gastroenterology, Third Xiangya Hospital, Central South University, Changsha, China
- 3 Cancer Research Institute, Central South University, Changsha, China
- 4 Cancer Research Institute, Central South University, Changsha, China
- 5 Cancer Research Institute, Central South University, Changsha, China
- 6 Cancer Research Institute, Central South University, Changsha, China
- 7 Cancer Research Institute, Central South University, Changsha, China
- 8 Department of Gastroenterology, Third Xiangya Hospital, Central South University, Changsha, China
- 9 Cancer Research Institute, Central South University, Changsha, China
- 10 Cancer Research Institute, Central South University, Changsha, China
- 11 Cancer Research Institute, Central South University, Changsha, China
Journal of Biophysical Chemistry·Volume 04 (2013)·Pages 80–83·Published 24 May 2013·DOI10.4236/jbpc.2013.42011
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Abstract
Epstein Barr virus infection is believed to play a role in the development of nasopharyngeal carcinoma. In order to investigate the function of EBV in epithelial cell, proteomic methods were used to find and identify the differential proteins and expected to elucidate the mechanism of EBV. Altered protein expressions were found between 293 cell (HEK293) and EBV infected cell (293-EBV). In this study, we separated differential expressed proteins using 2D-DIGE method while matrix-assisted laser desorption/ionization tandem time of flight mass spectrometry (MALDI-TOF-MS) method was used to identify proteins. The results showed that 14 proteins were up regulated and 3 proteins were down regulated in 293-EBV cells. Bioinformatic analysis showed that these proteins are involved in cell proliferation, metastasis, apoptosis, metabolism, and signal transduction. Western blotting analysis was further carried out to verify the MS results. Thus, EBV may exert its functions by mediating differential expression of these proteins.
KeywordsEBVDifferential In-Gelelectrophoresis (DIGE)Mass Spectrometry
- Zou, J., Yu, X., Bao, Z. and Dong, J. (2011) Proteome of human colon cancer stem cells: A comparative analysis. World Journal of Gastroenterology, 17, 1276-1285. doi:10.3748/wjg.v17.i10.1276
- Beere, H.M., Wolf, B.B., Cain, K., Mosser, D.D., Mahboubi, A., Kuwana, T., Tailor, P., Morimoto, R.I., Cohen, G.M. and Green, D.R. (2000) Heat-shock protein 70 inhibits apoptosis by preventing recruitment of procaspase-9 to the Apaf-1 apoptosome. Nature Cell Biology, 2, 469-475. doi:10.1038/35019501
- Jolly, C. and Morimoto, R.I. (2000) Role of the heat shock response and molecular chaperones in oncogenesis and cell death. Journal of National Cancer Institute, 92, 1564-1572.
- Millar, D.G., Garza, K.M., Odermatt, B., Elford, A.R., Ono, N., Li, Z. and Ohashi, P. (2003) Hsp70 promotes antigenpresenting cell function and converts T-cell tolerance to autoimmunity in vivo. National Medicine, 9, 1469-1476. doi:10.1038/nm962
- Mayer, M.P. (2005) Recruitment of Hsp70 chaperones: A crucial part of viral survival strategies. Reviews of Physiology, Biochemistry & Pharmacology, 153, 1-46. doi:10.1007/s10254-004-0025-5
- Kregel, K.C. (2002) Heat shock proteins: Modifying factors in physiological stress responses and acquired thermotolerance. Journal of Applied Physiology, 92, 2177-2186.
- Kampinga, H.H. and Craig, E.A. (2010) The HSP70 chaperone machinery: J proteins as drivers of functional specificity. Nature Reviews Molecular Cell Biology, 11, 579-592. doi:10.1038/nrm2941
- Rérole, A.L., Gobbo, J., Thonel, A.D., Schmitt, E., Barros, J.P., Hammann, A., Lanneau, D., Fourmaux, E., Deminov, O., Micheau, O., Lagrost, L., Colas, P., Kroemer, G. and Garrido, C. (2011) Peptides and Aptamers Targeting HSP70: A Novel Approach for Anticancer Chemotherapy. Cancer Research, 71, 484-495. doi:10.1158/0008-5472.CAN-10-1443
- Walsh, N., Larkin, A., Swan, N., Conlon, K., Dowling, P., McDermott, R. and Clynes, M. (2011) RNAi knockdown of Hop (Hsp70/Hsp90 organising protein) decreases invasion via MMP-2 down regulation. Cancer Letters, 306, 180-189. doi:10.1016/j.canlet.2011.03.004
- Jiang, B., Liang, P.F., Deng, G.H., Tu, Z.Z., Liu M.D. and Xiao, X.Z. (2010) Increased stability of Bcl-2 in HSP70-mediated protection against apoptosis induced by oxidative stress. Cell Stress and Chaperones, 16, 143-152.