Proteomic profiling for cancer progression: Differential display analysis for the expression of intracellular proteins between regressive and progressive cancer cell lines
Proteomic profiling for cancer progression: Differential display analysis for the expression of intracellular proteins between regressive and progressive cancer cell lines
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DOI：
10.1002/pmic.200401132
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发表时间：
2005-03-01
期刊：
影响因子：
3.4
通讯作者：
Nakamura, K
中科院分区：
文献类型：
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作者：
Hayashi, E;Kuramitsu, Y;Nakamura, K
肿瘤发展和进展由一系列涉及基因表达的多重变化的复杂过程组成（Paolo等人，Physiol. Rev.，1993，73，161-195; Lance等人，Cell.，1991，64，327-336）。肿瘤细胞获得侵袭性和转移性表型，这是癌症患者死亡的主要原因。因此，为了早期诊断和有效的治疗干预，我们需要在分子基础上检测与良性肿瘤细胞向恶性肿瘤细胞转变相关的改变。为了揭示与肿瘤进展有关的改变，蛋白质组学方法引起了极大的关注，因为它可以识别蛋白质组成的定性和定量变化，包括翻译后修饰。在这项研究中，我们进行了蛋白质组差异显示分析的细胞内蛋白质的表达在倒退的癌细胞系QR-32和炎症细胞促进进行性癌细胞系QRsP-11的小鼠纤维肉瘤通过二维凝胶电泳和质谱使用Agilent 1100 LC/MSD Trap XCT。我们发现11个蛋白质点的表达是不同的QR-32和QRsP-11细胞，并确定了9个蛋白质，其中7个，钙网蛋白前体，原肌球蛋白1 α链，膜联蛋白A5，热休克蛋白（HSP）90-α，HSP 90-β，PEBP，和Prx II，过表达，和两个，Anp 32 e和HDGF，这是下调。这些结果表明，蛋白质组学在识别肿瘤进展中的分子异常方面具有重要的补充作用。
Tumor development and progression consist of a series of complex processes involving multiple changes in gene expression (Paolo et al. Physiol. Rev., 1993, 73, 161-195; Lance et al. Cell., 1991, 64, 327-336). Tumor cells acquire an invasive and metastatic phenotype that is the main cause of death for cancer patients. Therefore, for early diagnosis and effective therapeutic intervention, we need to detect the alterations associated with transition from benign to malignant tumor cells on a molecular basis. To unravel alterations concerned with tumor progression, the proteomic approach has attracted great attention because it can identify qualitative and quantitative changes in protein composition, including post-translational modifications. In this study, we performed proteomic differential display analysis for the expression of intracellular proteins in the regressive cancer cell line QR-32 and the inflammatory cell-promoting progressive cancer cell line QRsP-11 of murine fibrosarcoma by two-dimensional gel electrophoresis and mass spectrometry using an Agilent 1100 LC/MSD Trap XCT. We found 11 protein spots whose expression was different between QR-32 and QRsP-11 cells and identified nine proteins, seven of which, calreticulin precursor, tropomyosin 1 alpha chain, annexin A5, heat shock protein (HSP)90-alpha, HSP90-beta, PEBP, and Prx II, were over-expressed, and two, Anp32e and HDGF, which were down-regulated. The results suggest an important complementary role for proteomics in identification of molecular abnormalities in tumor progression.