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http://dx.doi.org/10.7314/APJCP.2012.13.6.2699

Expression of Proteasome Activator REGγ in Human Laryngeal Carcinoma and Associations with Tumor Suppressor Proteins  

Li, Li-Ping (Department of Otorhinolaryngology and Translational Neuroscience Center, West China Hospital of Sichuan University)
Cheng, Wei-Bo (Department of Pathology, West China School of Public Health, Sichuan University)
Li, Hong (The Joint Research Center, West China Second University Hospital and University of Hong Kong)
Li, Wen (Department of Otorhinolaryngology and Translational Neuroscience Center, West China Hospital of Sichuan University)
Yang, Hui (Department of Otorhinolaryngology and Translational Neuroscience Center, West China Hospital of Sichuan University)
Wen, Ding-Hou (Department of Otorhinolaryngology and Translational Neuroscience Center, West China Hospital of Sichuan University)
Tang, Yue-Di (Department of Otorhinolaryngology and Translational Neuroscience Center, West China Hospital of Sichuan University)
Publication Information
Asian Pacific Journal of Cancer Prevention / v.13, no.6, 2012 , pp. 2699-2703 More about this Journal
Abstract
The functional significance of the proteasome activator $REG{\gamma}$ in the regulation of cell proliferation and apoptosis has been recognized. However, pathological contributions to tumor development remain to be elucidated. Both oncogenic proteins and tumor suppressors are targeted by $REG{\gamma}$ for proteasomal degradation. It has been proposed that the role of the $REG{\gamma}$ in the pathogenesis of cancer is cell- and context-specific. In this study, we aimed to explore the potential involvement of $REG{\gamma}$ in laryngeal carcinomas, comparing protein expression in tumor and adjacent tissues by immunohistochemical staining and Western blot analysis. We also characterized the correlation between the expression of $REG{\gamma}$ and the previously identified substrates p53 and p21. We showed that $REG{\gamma}$ was abnormally highly expressed in cancer tissues. Statistical analysis revealed that there was a positive relationship between the level of $REG{\gamma}$ and the expression of p53 and p21. Our study suggests that $REG{\gamma}$ overexpression can facilitate the growth of laryngeal cancer cells.
Keywords
$REG{\gamma}$; laryngeal carcinoma; p53; p21;
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1 Ciechanover A (1998). The ubiquitin-proteasome pathway: on protein death and cell life. EMBOJ, 17, 7151-60.   DOI   ScienceOn
2 Ciechanover A, Orian A, Schwartz AL (2000). Ubiquitinmediated proteolysis: biological regulation via destruction. Bioessays, 22, 442-51.   DOI
3 El-Deiry WS, Harper JW, O'Connor PM, et al (1994). WAF1/CIP1 is induced in p53-mediated G1 arrest and apoptosis. Cancer Res, 54, 1169-74.
4 Finlay CA, Hinds PW, Tan TH, et al (1988). Activating mutations for transformation by p53 produce a gene product that forms an HSC 70-p53 complex with an altered half-life. Mol Cell Biol, 8, 531-9.
5 Harper JW, Adami GR, Wei N, et al (1993). The p21 cdkinteracting protein Cip1 is a potent inhibitor of G1cyclindependent kinases. Cell, 75, 805-16.   DOI   ScienceOn
6 Hochstrasser M (1995). Ubiquitin, proteasomes, and the regulation of intracellular protein degradation. Curr. Opin. Cell Biol, 7, 215-23.   DOI
7 Jin YT, Kayser S, Kemp BL, et al (1998). The Prognostic Significance of the Biomarkers p21WAF1/CIP1, p53, and bcl-2 in Laryngeal Squamous Cell Carcinoma. Cancer, 82, 2159-65.   DOI
8 Lane DP (1992). Cancer: p53, guardian of the genome. Nature, 358, 15-6.   DOI   ScienceOn
9 Reich NC, Oven M, Levine AJ (1983). Two distinct mechanisms regulate the levels of cellular tumor antigen p53. Mol Cell Biol, 3, 2143-50.
10 Roessler M, Rollinger W, Mantovani-Endl L, et al (2006). Identification of PSME3 as a novel serum tumor marker for colorectal cancer by combining two-dimensional polyacrylamide gel electrophoresis with a strictly mass spectrometry-based approach for data analysis. Mol Cell Proteomics, 5, 2092-101.   DOI
11 Li X, Amazit L, Long W, et al (2007). Ubiquitin- and ATPindependent proteolytic turnover of p21 by the REGgammaproteasome pathway. Mol Cell, 26, 831-42.   DOI
12 Li X, Lonard DM, Jung SY, et al (2006). The SRC-3/AIB1 coactivator is degraded in a ubiquitin- and ATP-independent manner by the REGgamma proteasome. Cell, 124, 381-92.   DOI
13 Luo H, Wong J, Wong B (2010). Protein degradation systems in viral myocarditis leading to dilated cardiomyopathy. Cardiovasc Res, 85, 347-56.   DOI
14 Roninson IB (2002). Oncogenic functions of tumour suppressor p21(Waf1/Cip1/Sdi1): association with cell senescence and tumour-promoting activities of stromal fibroblasts. Cancer Lett, 179, 1-14.   DOI
15 Sarafoleanu D, Postelnicu V, Iosif C, et al (2009). The role of p53, PCNA and Ki-67 as outcome predictors in the treatment of laryngeal cancer. J Med Life, 2, 219-26.
16 Sharpless NE and DePinho RA (2002). p53: good cop/bad cop. Cell, 110, 9-12.   DOI   ScienceOn
17 Mao I, Liu J, Li X, et al (2008). REGgamma, a proteasome activator and beyond? Cell Mol Life Sci, 65, 3971-80.   DOI
18 Murata S, Kawahara H, Tohma S, et al (1999). Growth retardation in mice lacking the proteasome activator PA28gamma. J Biol Chem, 274, 38211-5.   DOI
19 Okamura T, Taniguchi S, Ohkura T, et al (2003). Abnormally high expression of proteasome activator-gamma in thyroid neoplasm. J Clin Endocrinol. Metab, 88, 1374-83.   DOI
20 Shunqian J, Qimin Z (2002). Oncomolecularbiology is the forefront of basic medical research. World Chin J Dig, 10, 678-80.
21 Soza A, Knuehl C, Groettrup M, et al (1997). Expression and subcellular localization of mouse 20S proteasome activator complex PA28. FEBS Lett, 413, 27-34.   DOI
22 Tomohisa O, Shin-Ichi T, Tsuyoshi O, et al (2003). Abnormally high expression of proteasome activator-cin Thyroid neoplasm. J Clin Endocrinol Metab, 88, 1374-83.   DOI
23 Wang XY, Tu SF, Tan JX, et al (2009). REG gamma: a potential marker in breast cancer and effect on cell cycle and proliferation of breast cancer cell. Med Oncol, 28, 31-41.
24 Weinberg WC, Denning MF (2002). P21Waf1 control of epithelial cell cycle and cell fate. Crit Rev Oral Biol Med, 13, 453-64.   DOI
25 Powell J, Robin PE (1983). Cancer of the head and neck: the present state. In: Head and Neck Cancer. Rhys Evans P, Robin PE & Fielding JWL (eds). Castle House: Tunbridge Wells.
26 Wojcik C, Tanaka K, Paweletz N, et al (1998). Proteasome activator (PA28) subunits, ${\alpha}$, ${\beta}$ and ${\gamma}$ (Ki antigen) in NT2 neuronal precursor cells and HeLa S3 cells. Eur J Cell Biol, 77, 151-60.   DOI
27 Ying H, Furuya F, Zhao L, et al (2006). Aberrant accumulation of PTTG1 induced by a mutated thyroid hormone beta receptor inhibits mitotic progression. J Clin Invest, 116, 2972-84.   DOI
28 Realini C, Jensen CC, Zhang Z, et al (1997). Characterization of recombinant REGalpha, REGbeta, and REGgamma proteasome activators. J Biol Chem, 272, 25483-92.   DOI
29 Zhang Z, Zhang R (2008). Proteasome activator PA28 gamma regulates p53 by enhancing its MDM2-mediated degradation. EMBO J, 27, 852-64.   DOI
30 Zhang M, Gan L, Ren GS (2012). REG${\gamma}$ is a strong candidate for the regulation of cell cycle, proliferation and the invasion by poorly differentiated thyroid carcinoma cells. Braz J Med Biol Res, 45, 459-65.   DOI
31 Ahn K, Erlander M, Leturcq D, et al (1996). In vivo characterization of the proteasome regulator PA28. J Biol Chem, 271, 18237-42.   DOI
32 Barton LF, Runnels HA, Schell TD, et al (2004). Immune defects in 28-kDa proteasome activator gamma-deficient mice. J Immunol, 172, 3948-54.   DOI
33 Bianchi S, Paglierani M, Zampi G, et al (1993). Prognostic value of proliferating cell nuclear antigen in lymph node-negative breast cancer patients. Cancer, 72, 120-5.   DOI
34 Bosari S, Viale G, Roncalli M, et al (1995). p53 gene mutations, p53 protein accumulation and compartmentalization in colorectal adenocarcinoma. Am J Pathol, 147, 790-8.
35 Chen X, Barton LF, Chi Y, et al (2007). Ubiquitin-independent degradation of cell-cycle inhibitors by the REGgamma proteasome. Mol Cell, 26, 843-52.   DOI
36 Ciechanover A (1994). The ubiquitin-proteasome proteolytic pathway. Cell, 79, 13-21.   DOI   ScienceOn