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NOB1在结直肠癌中的表达及其临床意义 被引量:5

Expression and clinical significance of colorectal cancer
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摘要 目的:研究NOB1编码蛋白在结直肠癌及正常结直肠黏膜(距癌组织边缘5cm以上)、结直肠良性息肉中的表达特征。探讨结直肠癌中NOB1表达的临床病理意义。方法:利用免疫组织化学SABC法检测87例结直肠癌组织、22例正常结直肠黏膜组织18例结直肠息肉组织中NOB1的表达。结果:NOB1在结直肠癌,结直肠良性息肉及正常结直肠黏膜中的阳性表达率分别为74.7%、44.4%、13.6%,三组进行比较,差异有统计学意义(P<0.01)。细胞分化差的结直肠癌NOB1蛋白阳性率表达高(P<0.05)与患者年龄,性别,肿瘤浸润深度及淋巴结转移无明显相关性。结论:NOB1蛋白在结直肠癌中表达升高,并与大肠癌临床病理学特征有关。 Objective:Researched the expression and clinical significance of NOB1 in colorectal cancer and their corresponding normal colorectal tissue and colorectal benign polups.Methods:The expression of NOB1 was detected by SABC immunohistochemical technique in 87 cases of colorectal cancer and their corresponding normal colorectal tissue(n =22) and 18 cases of colorectal polys.Results:Positive rate of NOB1 was 74.7% in colorectal cancer and 44.4% in colorectal benign polyps and 13.6% in normal colorectal tissue,with a significant difference between the two groups(P < 0.01).The expression of NOB1 was associated with differentiation grade in colorectal cancer but not with the age,gender,infiltration depth and lymphatic node metastasis in colorectal of patients.Conclusion:The expression of NOB1 is higher in colorectal cancer than in normal colorectal tissue,so NOB1 may play an important role in the progression of colorectal cancer.
出处 《现代肿瘤医学》 CAS 2013年第9期2044-2047,共4页 Journal of Modern Oncology
关键词 NOB1蛋白 结直肠癌 免疫组化学 NOB1 colorectal cancer immunohistochemistry
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  • 1Zhang Y, Ni J, Zhou G, et al. Cloning expression and characteriza- tion of the human NOB1 gene[ J]. Mol Biol Rep,2005,32 (3) :185 - 189.
  • 2Tone Y ,Toh - EA. Noblp is required for biogenesis of the 26S pm- teasome and degraded upon its maturation in Saccharomyces cere- visiae [ J ]. Gene Dev,2002,16 (24) :3142 - 3157.
  • 3Gerbi SA,Borovjagin AV,Lange TS. The nucleolus: a site of ribo- nucleoprotein maturation [ J ]. Curr Opin Cell Biol, 2003,15 ( 3 ) : 318 -325.
  • 4Fatica A, Oeffinger M, Dlakicr M. Nobl p is required for cleavage of the 3:ud of 18S rRNA [ J]. Mol Cell Biol,2003,23 (5):1798 - 1807.
  • 5Ferrell K, Wilkinson CRM, Dubiel W, et al. Regulatory subunit in- teractions of the 26S proteasome, a complex problem [ J ]. Trends Bioehem Sei,2000,25 : 83 - 88.
  • 6Zachariae W,Nasmyth K. Whose end is destruction: cell division and the anaphase - promoting complex[ J]. Gene Dev, 1999,19 : 2039 - 2058.
  • 7Fujimuro M, Takada H, Saeki Y, et al. Growth - dependent change of the 26S proteasome in budding yeast[ J]. Biochem Biophy Res Com,1998,251:818 -823.
  • 8Vierstra RD. The ubiquitin/26S proteasome pathway, the complex last chapter in the life of many plant proteins [ J ]. Trends Plant Sci,2003,8:135 - 142.
  • 9Tone Y, Tanahashi N, Tanaka K, et al. Nobl p, a new essential pro- tein, associates with the 26S proteasome of growing Saccharomyces cerevisiae cells [ J ] . Gene,2000,243 ( 1/2 ) : 37 - 45.
  • 10倪晓光,赵平.泛素-蛋白酶体途径与恶性肿瘤关系的研究进展[J].中华肿瘤防治杂志,2007,14(19):1512-1515. 被引量:20

二级参考文献18

  • 1倪晓光,赵平.泛素-蛋白酶体途径的组成和功能[J].生理科学进展,2006,37(3):255-258. 被引量:43
  • 2Mukhopadhyay D, Riezman H. Proteasome-independent functions of ubiquitin in endocytosis and signaling [J]. Science, 2007, 315(5809):201-205.
  • 3Yamasaki L, Pagano M. Cell cycle, proteolysis and cancer[J]. Curr Opin Cell Biol, 2004, 16(6) :623--628.
  • 4Moberg K H, Bell D W, Wahrer D C, et al. Archipelago regulates Cyclin E levels in Drosophila and is mutated in human cancer cell lines[J]. Nature, 2001, 413(6853):311--316.
  • 5Hao B, Zheng N, Schulman B A, et al. Structural basis of the Cksl-dependent recognition of p27(Kipl) by the SCF(Skp2) ubiquitin ligase[J]. Mol Cell, 2005, 20(1):9--19.
  • 6Zhang H G, Wang J, Yang X, et al. Regulation of apoptosis proteins in cancer cells by ubiquitin [J]. Oncogene, 2004, 23( 11 ) :2009 -2015.
  • 7Fuchs S Y. The role of ubiquitin-proteasome pathway in oncogenic signaling[J]. Cancer Biol Ther, 2002, 1(4): 337--341.
  • 8Perkins N D. Post-translational modifications regulating the activity and function of the nuclear factor kappa B pathway[J]. Oncogene, 2006, 25(51):6717-6730.
  • 9Swaminathan G, Tsygankov A Y. The Cbl fam ly proteins: ring leaders in regulation of cell signaling[J]. J Cell Physiol, 2006, 209(1):21--43.
  • 10Schmidt M H, Furnari F B, Cavenee W K, et ah Epidermal growth factor receptor signaling intensity determines intracellular protein interactions, ubiquitination, and intcrnalization[J].Proc Natl Acad Sci U S A, 2003, 100(11): 6505--6510.

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