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胆囊癌组织的比较蛋白质组学分析
引用本文:谈燚,孟海萍,王富强,承泽农,吴穷,吴浩荣. 胆囊癌组织的比较蛋白质组学分析[J]. 中华肿瘤杂志, 2010, 32(1). DOI: 10.3760/cma.j.issn.0253-3766.2010.01.007
作者姓名:谈燚  孟海萍  王富强  承泽农  吴穷  吴浩荣
作者单位:1. 215004苏州大学附属第二医院普外科
2. 蚌埠医学院附属第一医院检验科
3. 南京医科大学大型仪器中心
4. 蚌埠医学院附属第一医院病理科
摘    要:目的 通过分离、鉴定胆囊癌和胆囊良性组织的差异表达蛋白质,探讨可能用于早期诊断或治疗胆囊癌的肿瘤标志物.方法 对6例人胆囊癌组织和胆囊良性组织进行比较蛋白质组学研究,采用双向凝胶电泳分离蛋白,经图像分析识别差异表达的蛋白.应用基质辅助激光解析电离飞行时间质谱(MALD-TOF-MS)鉴定差异蛋白质.采用免疫组化技术对差异蛋白磷脂酰乙醇胺结合蛋白1(PEBP1)进行验证.结果 获得了分辨率和重复性均较好的凝胶蛋白图谱.共筛选出46个在胆囊癌组织中明显差异表达的蛋白点,其中17个蛋白质鉴定成功.在这17个蛋白质中,胆囊癌组织中高表达9个,低表达8个.PEBP1在胆囊癌组织中的阳性表达率为74.0%.结论 成功鉴定了17个胆囊癌相关蛋白,为进一步筛选胆囊癌的诊断、治疗和预后评估的分子标志物奠定了基础.

关 键 词:胆囊肿瘤  蛋白质组  磷脂酰乙醇胺结合蛋白1

Comparative proteomic analysis of human gallbladder carcinoma
TAN Yi,MENG Hai-ping,WANG Fu-qiang,CHENG Ze-nong,WU Qiong,WU Hao-rong. Comparative proteomic analysis of human gallbladder carcinoma[J]. Chinese Journal of Oncology, 2010, 32(1). DOI: 10.3760/cma.j.issn.0253-3766.2010.01.007
Authors:TAN Yi  MENG Hai-ping  WANG Fu-qiang  CHENG Ze-nong  WU Qiong  WU Hao-rong
Abstract:Objective To find out potential molecular targets for gallbladder carcinoma diagnosis and treatment by analyzing and comparing the proteins expressed in human gallbladder carcinoma tissue and benign gallbladder tissue. Methods Proteomic analysis of 6 human gallbladder carcinoma tissues and 6 benign gallbladder tissues was carried out. Total proteins of the carcinoma tissue and benign gallbladder tissue were separated by two-dimensional gel electrophoresis (2-DE). The differentially expressed proteins were analyzed and identified by matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALD1-TOF-MS). Immunohistochemistry was used to examine the expression of PEBP1 protein in an independent series of samples. Results Protein extracts of individual samples in each type of tissues were separated on two-dimensional gels. There were forty six differentially expressed proteins in the gallbladder carcinom tissues. Seventeen proteins were successfully identified by MS, in which nine proteins were overexpressed in tumors while the other eight proteins were underexpressed. The increased level of PEBP1 protein in gallbladder carcinoma was further confirmed by immunohistochemical analysis. Conclusion Seventeen differentially expressed proteins were successfully characterized by comparative proteomic analysis. Those results may provide scientific foundation for screening the molecular biomarkers which can be used in diagnosis and treatment of gallbladder carcinoma, as well as to improve its prognosis and provide a new clue for carcinogenesis research of gallbladder carcinoma.
Keywords:Gallbladder neoplasms  Proteome  PEBP1
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