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LMP-1 and Nasopharyngeal Carcinoma (NPC)

Year 2014, Volume: 39 Issue: 3, 480 - 487, 22.07.2014
https://doi.org/10.17826/cutf.53492

Abstract

Purpose: This study aims to determine the interaction of LMP-1 with H2O2 , nitrosamine, and nicotine to predict the external factor that affected LMP-1, which activates lytic phase on nasopharyngeal carcinoma (NPC). Materials and Methods: The amino acid sequence of human LMP1 (GI: 343177335) and compound structure of H2O2 (ID:784), nicotine (ID: 89594), and nitrosamine (ID: 37183) was obtained from database The National center of Biotechnology Information. The 3-dimension modeling structure of LMP-1 predicted using SWISS-MODEL web server. Hex 6.12 was used for the purpose of docking of the lead with the target molecule. Ligand details interaction then detected by LigPlus+ v.1.4.4 software. Molecular graphics and analysis were performed with PyMOL. Results: LMP-1 has interaction with H2O2 , nitrosamine, and nicotine. Total energy that use of LMP-1 to interaction with H2O2 (-67,79 kJ/mol) is lowest than interaction with nicotine (-149,43 kJ/mol) and nitrosamine (-82,93 kJ/mol). The kind of interaction between LMP-1 and H2O2 is hydrogen bond whereas interaction of LMP-1 between nicotine and nitrosamine are hydrophobic bond. Conclusions:LMP-1 has strongest interaction with H2O2 than nicotine and nitrosamine. This is predicted that H2O2 is external factor that affect LMP-1 switching to lytic infection in NPC patients.

References

  • Cho WC. Nasopharyngeal carcinoma: molecular biomarker discovery and progress. Molecular Cancer. 2007;6:1-9.
  • Lo KW, To KF, Huang DP. Focus on nasopharyngeal carcinoma. Cancer Cell. 2004;5: 423-8.
  • Yoshizaki T, Kondo S, Wakisaka N, Murono S, Endo K, Sugimoto H, Nakanishi S, Tsuji A, Ito M. Pathogenic role of Epstein-Barr virus latent membrane protein-1 in the development of nasopharyngeal carcinoma. Cancer Letters. 2013;337:1-7.
  • Young LS & Rickinson AB. Epstein-Barr virus: 40 years on. Nat Rev Cancer. 2004;4:757–68.
  • Du CW, Wen BG, Li DR, Lin YC, Zheng YW, Chen L, Chen JY, Lin W, Wu MY.Latent membrane protein-1 of Epstein-Barr virus increases sensitivity to arsenic trioxide-induced apoptosis in nasopharyngeal carcinoma cell. Exp Oncol. 2005;27:267-72.
  • Budiningrum AI, Rofi’i A, Suharjono S, Fatchiyah F. PARP-1 expression against Epstein-Barr virus LMP-1 and BZLF-1 in undifferentiated nasopharyngeal carcinoma. J Exp Integr Med. 2013;3:299-304.
  • Lassoued S, Gargouri B, El Feki Ael F, Attia H, van Pelt J. Transcription of the Epstein-Barr Virus lytic cycle activator BZLF-1 during oxidative stress induction. Biol Trace Elem Res. 2010;137:13-22.
  • Rofi’i A, Fatchiyah F, Rahayu P, Muhyi R, Sumitro SB. Reactive oxygen species, NFᴋB, and p53 levels in tissue of undifferentiated nasopharyngeal carcinoma. Oxid Antioxid Med Sci. 2013;2:143-7.
  • Dood LE, Sengupta S, Chen I-H, den Bonn JA, Cheng Y-J, Westra W, Newton MA, Mittl BF, McShane L, Chen C-J, Ahlquist P, Hildesheim A. Genes involved in DNA repair and nitrosamine metabolism and those located on chromosome 14q32 are dysregulated in nasopharyngeal carcinoma. Cancer Epidemiol Biomarkers Prev. 2006;15:2216-25.
  • Yu MC & Yuan JM. Epidemiology of nasopharyngeal carcinoma. Semin Cancer Biol. 2002;12:421-9.
  • Shields PG. Long-term nicotine replacement therapy: cancer risk in context. Cancer Prev Res. 2011;4:1719-23.
  • Arnold K, Bordoli L, Kopp J, Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modeling. Bioinformatics. 2006;22:195-201.
  • Macindoe GL, Mavridis V, Venkatraman MD, Devignes DW, Ritchie. HexServer: an FFT-based protein docking server powered by graphics processors. Nucleic Acids Res. 2010;38:445-9.
  • Cleave SS, Panda R, Suresh PK. In silico exploration of phenytoin binding site in two catalytic states of human P-glycoprotein models. Indian J. Biochem. Biophysic. 2013;50:7-13.
  • DeLano, W.L. The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos, CA, USA. 200 http://www.pymol.org Lin JC, Cherng JM, Lin HJ, Tsang CW, Liu YX, Lee SP. Amino acid changes in functional domains of latent membrane protein 1 of Epstein-Barr virus in nasopharyngeal carcinoma of southern China and Taiwan: prevalence of an HLA-A2-resticted ‘epitopeloss variant’. J Gen Virol. 2004;85:2023-34.
  • Tang YL, Lu JH, Cao L, Wu MH. Peng SP, Zhou HD, Huang C, Yang YX, Zhou YH, Chen Q, Li XL, Zhou M, Li GY. Genetic variations of EBV-LMP1 from nasopharyngeal carcinoma biopsies: potential loss of T cell epitopes. Brazilian Journal of Medical and Biological Research. 2008;41:110-6.
  • Liu J, Zhan X, Li M, Li G, Zhang P, Xiao Z, Shao M, Peng F, Hu R, Chen Z. Mitochondrial protemics of nasopharyngeal carcinoma metastasis. BMC Medical Genomics. 2012;5: 62-78.
  • Autrup H, Stoner GD. Metabolism of N-nitrosamines by cultured human and rat esophagus. Cancer Research. 1982;42:1307-11.
  • Yuan JM, Wang XL, Xiang YB, Gao YT, Ross RK, Yu MC. Non-dietary risk factor for nasopharyngeal carcinoma in Shanghai, China. Int J. Cancer. 2000;85:364-9.
  • Chan ASC, To KF, Lo KW, Mak KF, Pak W, Chiu B, Tse GMK, Ding M, Li X, Lee JCK, Huang DP. High frequency of chromosome 3p deletion in histologically normal nasopharyngeal epithelia from Southern Chinese. Cancer Res. 2000;60:5365-70. Yazışma Adresi / Address for Correspondence: Dr.Fatchiyah Department of Biology Faculty of Mathematic and Sciences, University of Brawijaya Jl. Veteran, Malang, 65145, INDONESIA. Fax: +62341575841. E-mail: fatchiya@ub.ac.id ; fatchiya@gmail.com G eliş tarihi/Received on: 06.01.2014 Kabul tarihi/Accepted on:14.02.2014

LMP-1 ve Nazofaringial Karsinoma

Year 2014, Volume: 39 Issue: 3, 480 - 487, 22.07.2014
https://doi.org/10.17826/cutf.53492

Abstract

Amaç: Bu çalışmanın amacı nazofaringial karsinomun litik fazı üzerine etkili olduğu düşünülen LMP-1, ile H2O2 , nitrozamin ve nikotinin gibi dış faktörler arasındaki etkileşimi belirlemektir. Materyal ve Metod: insan LMP-1 (GI: 343177335) aminoasid sekansı ile nikotin (ID: 89594), nitrozamin (ID: 37183) ve H2O2 (ID: 37183) nin yapısal içeriği The National center of Biotechnology Information'a ait veri tabanına göre açıklanmıştır. LMP-1 in 3 boyutlu yapısı SWISS-MODEL web ağı kullanarak tasarlandı. Hex 6,12 hedef moleküle öncülük etmesi için kullanıldı. LigPlus+1.4.4 software ile ligand detayları tarandı. Moleküler grafikler ve analizler PyMOL ile yapıldı. Bulgular: LMP-1 in H2O2 , nitrozamin ve nikotin ile etkileşimi vardır. LMP-1 in H2O2 etkileşimi için harcadığı enerji (-67,79 kj/mol), nikotin (-149,43 kj/mol) ve nitrozamin (-82,93 kj/mol) için kullanılandan daha düşüktür. LMP-1 ile H2O2 arasındaki etkileşimin türü Hidrojen bağı iken LMP-1 ile nitrozamin ve nikotin arasındaki etkileşim hidrofobik bağdır. Sonuç: LMP-1 H2O2 ile nitrozamin ve nikotine göre daha güçlü bağ kurar. Dış etken olan H2O2 nin LMP-1 i etkileyerek NPC li hastalarda litik enfeksiyon fazına geçişe neden olduğu tahmin edilmektedir.

References

  • Cho WC. Nasopharyngeal carcinoma: molecular biomarker discovery and progress. Molecular Cancer. 2007;6:1-9.
  • Lo KW, To KF, Huang DP. Focus on nasopharyngeal carcinoma. Cancer Cell. 2004;5: 423-8.
  • Yoshizaki T, Kondo S, Wakisaka N, Murono S, Endo K, Sugimoto H, Nakanishi S, Tsuji A, Ito M. Pathogenic role of Epstein-Barr virus latent membrane protein-1 in the development of nasopharyngeal carcinoma. Cancer Letters. 2013;337:1-7.
  • Young LS & Rickinson AB. Epstein-Barr virus: 40 years on. Nat Rev Cancer. 2004;4:757–68.
  • Du CW, Wen BG, Li DR, Lin YC, Zheng YW, Chen L, Chen JY, Lin W, Wu MY.Latent membrane protein-1 of Epstein-Barr virus increases sensitivity to arsenic trioxide-induced apoptosis in nasopharyngeal carcinoma cell. Exp Oncol. 2005;27:267-72.
  • Budiningrum AI, Rofi’i A, Suharjono S, Fatchiyah F. PARP-1 expression against Epstein-Barr virus LMP-1 and BZLF-1 in undifferentiated nasopharyngeal carcinoma. J Exp Integr Med. 2013;3:299-304.
  • Lassoued S, Gargouri B, El Feki Ael F, Attia H, van Pelt J. Transcription of the Epstein-Barr Virus lytic cycle activator BZLF-1 during oxidative stress induction. Biol Trace Elem Res. 2010;137:13-22.
  • Rofi’i A, Fatchiyah F, Rahayu P, Muhyi R, Sumitro SB. Reactive oxygen species, NFᴋB, and p53 levels in tissue of undifferentiated nasopharyngeal carcinoma. Oxid Antioxid Med Sci. 2013;2:143-7.
  • Dood LE, Sengupta S, Chen I-H, den Bonn JA, Cheng Y-J, Westra W, Newton MA, Mittl BF, McShane L, Chen C-J, Ahlquist P, Hildesheim A. Genes involved in DNA repair and nitrosamine metabolism and those located on chromosome 14q32 are dysregulated in nasopharyngeal carcinoma. Cancer Epidemiol Biomarkers Prev. 2006;15:2216-25.
  • Yu MC & Yuan JM. Epidemiology of nasopharyngeal carcinoma. Semin Cancer Biol. 2002;12:421-9.
  • Shields PG. Long-term nicotine replacement therapy: cancer risk in context. Cancer Prev Res. 2011;4:1719-23.
  • Arnold K, Bordoli L, Kopp J, Schwede T. The SWISS-MODEL workspace: a web-based environment for protein structure homology modeling. Bioinformatics. 2006;22:195-201.
  • Macindoe GL, Mavridis V, Venkatraman MD, Devignes DW, Ritchie. HexServer: an FFT-based protein docking server powered by graphics processors. Nucleic Acids Res. 2010;38:445-9.
  • Cleave SS, Panda R, Suresh PK. In silico exploration of phenytoin binding site in two catalytic states of human P-glycoprotein models. Indian J. Biochem. Biophysic. 2013;50:7-13.
  • DeLano, W.L. The PyMOL Molecular Graphics System. DeLano Scientific, San Carlos, CA, USA. 200 http://www.pymol.org Lin JC, Cherng JM, Lin HJ, Tsang CW, Liu YX, Lee SP. Amino acid changes in functional domains of latent membrane protein 1 of Epstein-Barr virus in nasopharyngeal carcinoma of southern China and Taiwan: prevalence of an HLA-A2-resticted ‘epitopeloss variant’. J Gen Virol. 2004;85:2023-34.
  • Tang YL, Lu JH, Cao L, Wu MH. Peng SP, Zhou HD, Huang C, Yang YX, Zhou YH, Chen Q, Li XL, Zhou M, Li GY. Genetic variations of EBV-LMP1 from nasopharyngeal carcinoma biopsies: potential loss of T cell epitopes. Brazilian Journal of Medical and Biological Research. 2008;41:110-6.
  • Liu J, Zhan X, Li M, Li G, Zhang P, Xiao Z, Shao M, Peng F, Hu R, Chen Z. Mitochondrial protemics of nasopharyngeal carcinoma metastasis. BMC Medical Genomics. 2012;5: 62-78.
  • Autrup H, Stoner GD. Metabolism of N-nitrosamines by cultured human and rat esophagus. Cancer Research. 1982;42:1307-11.
  • Yuan JM, Wang XL, Xiang YB, Gao YT, Ross RK, Yu MC. Non-dietary risk factor for nasopharyngeal carcinoma in Shanghai, China. Int J. Cancer. 2000;85:364-9.
  • Chan ASC, To KF, Lo KW, Mak KF, Pak W, Chiu B, Tse GMK, Ding M, Li X, Lee JCK, Huang DP. High frequency of chromosome 3p deletion in histologically normal nasopharyngeal epithelia from Southern Chinese. Cancer Res. 2000;60:5365-70. Yazışma Adresi / Address for Correspondence: Dr.Fatchiyah Department of Biology Faculty of Mathematic and Sciences, University of Brawijaya Jl. Veteran, Malang, 65145, INDONESIA. Fax: +62341575841. E-mail: fatchiya@ub.ac.id ; fatchiya@gmail.com G eliş tarihi/Received on: 06.01.2014 Kabul tarihi/Accepted on:14.02.2014
There are 20 citations in total.

Details

Primary Language Turkish
Journal Section Research
Authors

Anggun İndah Budiningrum This is me

Achmad Rofi'i This is me

Suharjono Suharjono This is me

Fatchiyah Fatchiyah This is me

Publication Date July 22, 2014
Published in Issue Year 2014 Volume: 39 Issue: 3

Cite

MLA Budiningrum, Anggun İndah et al. “LMP-1 Ve Nazofaringial Karsinoma”. Cukurova Medical Journal, vol. 39, no. 3, 2014, pp. 480-7, doi:10.17826/cutf.53492.