Distribution and location of Daxx in cervical epithelial cells with high risk human papillomavirus positive

Diagnostic Pathology

Yan-ping Wan²  Min-jun Yu²  An-yuan Liu²  Yao-lin Li²  Le Li¹  Shuang-yang Tang² 

[1] School of Public Health, University of South China, Hengyang 421001, China;Institute of Pathogenic Biology, University of South China, Hengyang 421001, China

关键词: Intraepithelial neoplasia grade;    Cervical cancer;    Daxx;    Human papillomavirus;   

Others  :  803651
DOI  :  10.1186/1746-1596-9-1

 received in 2013-10-23, accepted in 2014-01-05,  发布年份 2014

【 摘 要 】

Aims

To provide the basis for further exploring the effect and its mechanism of Death domain associated protein (Daxx) on the progress of cervical carcinoma induced by human papillomavirus (HPV), the distribution and location of Daxx in cervical carcinoma with high risk HPV(HR-HPV) positive was analyzed.

Methods

The samples of normal cervical epithelial cells, cervical intraepithelial neoplasia grade I (CINI), CINII CINIII and cervical cancers were collected. Immunohistochemistry assay was used to analyze the distributions and locations of Daxx in the cervical tissue. Indirect immunoinfluorescence test was utilized to observe the locations of Daxx in Caski cells with HPV16 positive.

Results

Under the light microscopy, the brown signals of Daxx distributed in the nuclei of normal cervical epithelial cells; Daxx mainly distributed in nuclear membrane and there were a small amount of Daxx in the nuclei in CINI. Daxx intensively distributed in the cytoplasm and cell membrane in CINII, CINIII and cervical cancer. Under fluorescent microscopy, the distribution and location of Daxx in Caski cells was similarly to that in cervical cells of CINII, CINIII and cervical cancer.

Conclusion

In the progress of the cervical cancer, Daxx gradually translocates from nucleus into nuclear membrane, cytoplasm and cell membrane. Daxx locates in the cytoplasm and cell membrane in CINII, CINIII and cervical cancer.

Virtual slides

The virtual slide(s) for this article can be found here:

http://www.diagnosticpathology.diagnomx.eu/vs/4671548951113870. webcite

【 授权许可】

   
2014 Tang et al.; licensee BioMed Central Ltd.

【 图 表 】

Figure 1.

Figure 2.

【 参考文献 】

• [1]Yang X, Khosravi-Far R, Chang HY, Baltimore D: Daxx, a novel Fas-binding protein that activates JNK and apoptosis. Cell 1997, 89:1067-1076.
• [2]Lindsay CR, Morozov VM, Ishov AM: PML NBs (ND10) and Daxx: from nuclear structure to protein function. Front Biosci 2008, 13:7132-7142.
• [3]Florin L, Schäfer F, Sotlar K, Streeck RE, Sapp M: Reorganization of nuclear domain 10 induced by papillomavirus capsid protein l2. Virology 2002, 295(1):97-107.
• [4]Chen SF, Zhu CM, Wan YP: Progress on the subcellular localization of Daxx. Ai Zheng 2009, 28:1333-1336.
• [5]Zhang H, He J, Li J, Tian D, Gu L, Zhou M: Methylation of RASSF1A gene promoter is regulated by p53 and DAXX. FASEB J 2013, 27(1):232-242.
• [6]Schiller JT, Lowy DR: Prospects for cervical cancer prevention by human papillomavirus vaccination. Cancer Res 2006, 66(21):10229-10232.
• [7]Lin Z, Yemelyanova AV, Gambhira R, Jagu S, Meyers C, Kirnbauer R, Ronnett BM, Gravitt PE, Roden RBS: Expression pattern and subcellular localization of human papillomavirus minor capsid protein L2. Am J Pathol 2009, 174(1):136-143.
• [8]Guccione E, Lethbridge KJ, Killick N, Leppard KN, Banks L: HPV E6 proteins interact with specific PML isoforms and allow distinctions to be made between different POD structures. Oncogene 2004, 23(27):4662-4672.
• [9]Chen SF, Zhu CM, Tang SY, Yu MJ, Su SM, Yang F, Wan YP: Localization of human papillomvirus type 16 E6 protein and hDaxx in a human cervical carcinom cell line HeLa and their effects on cell apoptosis. Chinese J Dermatol 2012, 45:400-403.
• [10]Leal-Sanchez J, Couzinet A, Rossin1 A, Abdel-Sater F, Chakrabandhu K, Luci C, Anjuere F, Stebe E, Hancock D, Hueber AO: Requirement for Daxx in mature T-cell proliferation and activation. Cell Death Differ 2007, 14(4):795-806.
• [11]Li Q, Wang X, Wu X, Rui Y, Liu W, Wang J: Daxx cooperates with the Axin/Hipk2/p53 complex to induce cell death. Cancer Res 2007, 67:66-74.
• [12]Kwan PS, Lau CC, Chiu YT, Man C, Liu J, Tang KD, Wong YC, Ling MT: Daxx regulates mitotic progression and prostate cancer predisposition. Carcinogenesis 2013, 34(4):750-759.
• [13]Dionne KR, Zhuang Y, Leser JS, Tyler KL, Clarke P: Daxx upregulation within the cytoplasm of reovirus-infected cells is mediated by interferon and contributes to apoptosis. J Virol 2013, 87(6):3447-3460.
• [14]Hwang J, Kalejta RF: In vivo analysis of protein sumoylation induced by a viral protein: detection of HCMV pp 71-induced Daxx sumoylation. Methods 2011, 55(2):160-165.
• [15]Hwang J, Kalejta RF: Proteasome-dependent, ubiquitin-independent degradation of Daxx by the viral pp 71 protein in human cytomegalovirus-infected cells. Virology 2007, 367:334-338.
• [16]Zydek M, Uecker R, Tavalai N, Stamminger T, Hagemeier C, Wiebusch L: General blockade of human cytomegalovirus immediate-early mRNA expression in the S/G2 phase by a nuclear, Daxx- and PML-independent mechanism. J Gen Virol 2011, 92:2757-2769.
• [17]Zhao LY, Colosimo AL, Liu Y, Wan Y, Liao D: Adenovirus E1B 55-kilodalton oncoprotein binds to Daxx and eliminates enhancement of p53-dependent transcription by 18 Daxx. J Virol 2003, 77:11809-11821.
• [18]Schreiner S, Wimmer H, Sirma H, et al.: Proteasome-dependent degradation of Daxx by the viral E1B-55 K protein in human adenovirus-infected cells. J Virol 2010, 84:7029-7038.
• [19]Zizzi A, Montironi MA, Mazzucchelli R, Scarpelli M, Lopez-Beltran A, Cheng L, Paone N, Castellini P, Montironi R: Immunohistochemical analysis of chromatin remodeler Daxx in high grade urothelial carcinoma. Diagn Pathol 2013, 8:111. BioMed Central Full Text