喉癌及喉正常黏膜组织蛋白质组差异表达的初步研究

目的 研究喉癌及癌旁喉正常黏膜组织蛋白质组的差异表达。方法 用固相PH梯度双向凝胶电泳分离喉癌及癌旁喉正常黏膜组织总蛋白质，银染显色、PD(HYEST2DE软件分析所获得的双向凝胶电泳图谱，找出差异表达的蛋白质点。取差异表达的蛋白质点进行质谱鉴定。结果 获得分辨率和重复性均较好的双向凝胶电泳图谱，并鉴定出与喉癌发生密切相关的12种蛋白质。其中有10种蛋白质在喉癌组织中特异表达，分别是An-giopietin-2，sprouty homologues，Inhibitor of apoptosis-1ike protein2(ILP-2)，urokinase type plasminogen activator re-ceptor uPAR，Wnt-3a protein，癌基因Transforming protein N-Ras、P21以及c-Met．等.connexin31．1，原肌球蛋白Tropomyosin两种蛋白质在癌旁喉正常黏膜组织中特异表达。结论 本研究利用固相PH梯度双向凝胶电泳技术分离喉癌及癌旁喉正常黏膜组织总蛋白质，首次建立了重复性较强的喉癌及喉正常黏膜组织蛋白质组表达图谱，且两者蛋白质的表达明显不同，差异表达的蛋白质分别参与细胞的癌变、细胞间的信号传导、肿瘤血管生成，这对研究喉癌的癌变机制，寻找与喉癌诊断和治疗相关的肿瘤标志物相当重要。

Comparative proteomics analysis of human laryngeal cancer and laryngeal normal mucosa

Objective To establish two-dimensional electrophoresis profiles with high resolution and reproducibility from laryngeal squamous carcinoma tissue and paired normal tumor-adjacent mucosa epithelia tissue, and to identify the differential expression proteins. Methods The total proteins of laryngeal cancer tissue and paired normal tumor-adjacent mucosa epithelial tissue were seperated by means of immobilized pH gradient-based two-dimensional gel electrophoresis (2-DE). The differential expression proteins were analyzed by using ImageMaster 2D analysis software, then identified by peptide mass fingerprint (PMF) based on matrix-assisted laser desorption/ionization time of flight mass spectrometry (MALDI-TOF-MS) and database searching. Result We obtained well-resolved, reproducible 2-DE patterns of laryngeal squamous carcinoma and adjacent normal mucosa epithelial. Differential protein spots were defined as spots in 2-DE gels.12 proteins were preliminarily identified, among which ten proteins were upregulate in laryngeal cancer tissue. Such as Angiopietin-2, as a permissive angiogenic signal. Inhibitor of apoptosis-like protein 2 (ILP-2), urokinase type plasminogen activator receptor uPAR, correlated with tumor progression and metastasis. Transforming protein N-Ras and so on. There are two proteins uprugulate in normal mucosa tissue, which are connexin 31.1 and Tropomyosin. Conclusion We established the expression maps of proteomics in laryngeal cancer and normal mucosa epithelial. Laryngeal cancer tissue proteome might reflect the underlying pathological state. There were significant differences among proteome of laryngeal cancer and normal mucosa epithelial. Some proteins were the products of oncogenes and others were involved in signal transduction and angiogenic. These data may be valuable for studying mechanisms of laryngeal carcinogenesis, or as diagnostic markers and therapeutic targets for laryngeal cancer.