Biotechnology Division, Biomedical Research Foundation, Academy of Athens, Greece.
Mol Cell Proteomics. 2012 Apr;11(4):M111.009449. doi: 10.1074/mcp.M111.009449. Epub 2011 Dec 8.
Of the most important clinical needs for bladder cancer (BC) management is the identification of biomarkers for disease aggressiveness. Urine is a "gold mine" for biomarker discovery, nevertheless, with multiple proteins being in low amounts, urine proteomics becomes challenging. In the present study we applied a fractionation strategy of urinary proteins based on the use of immobilized metal affinity chromatography for the discovery of biomarkers for aggressive BC. Urine samples from patients with non invasive (two pools) and invasive (two pools) BC were subjected to immobilized metal affinity chromatography fractionation and eluted proteins analyzed by 1D-SDS-PAGE, band excision and liquid chromatography tandem MS. Among the identified proteins, multiple corresponded to proteins with affinity for metals and/or reported to be phosphorylated and included proteins with demonstrated association with BC such as MMP9, fibrinogen forms, and clusterin. In agreement to the immobilized metal affinity chromatography results, aminopeptidase N, profilin 1, and myeloblastin were further found to be differentially expressed in urine from patients with invasive compared with non invasive BC and benign controls, by Western blot or Elisa analysis, nevertheless exhibiting high interindividual variability. By tissue microarray analysis, profilin 1 was found to have a marked decrease of expression in the epithelial cells of the invasive (T2+) versus high risk non invasive (T1G3) tumors with occasional expression in stroma; importantly, this pattern strongly correlated with poor prognosis and increased mortality. The functional relevance of profilin 1 was investigated in the T24 BC cells where blockage of the protein by the use of antibodies resulted in decreased cell motility with concomitant decrease in actin polymerization. Collectively, our study involves the application of a fractionation method of urinary proteins and as one main result of this analysis reveals the association of profilin 1 with BC paving the way for its further investigation in BC stratification.
对于膀胱癌(BC)管理,最重要的临床需求之一是确定疾病侵袭性的生物标志物。尿液是发现生物标志物的“金矿”,然而,由于多种蛋白质含量低,尿液蛋白质组学变得具有挑战性。在本研究中,我们应用了一种基于固定金属亲和层析的尿液蛋白质分级策略,用于发现侵袭性 BC 的生物标志物。非侵袭性(两个池)和侵袭性(两个池)BC 患者的尿液样本进行固定金属亲和层析分级,然后用 1D-SDS-PAGE、胶条切取和液相色谱串联质谱分析洗脱蛋白。在鉴定的蛋白质中,多个蛋白质与金属亲和力有关,或报道为磷酸化蛋白,包括与 BC 有明确关联的蛋白质,如 MMP9、纤维蛋白原形式和聚集素。与固定金属亲和层析结果一致,氨基肽酶 N、原肌球蛋白 1 和髓样白血病细胞分化蛋白在侵袭性 BC 患者的尿液中进一步发现与非侵袭性 BC 和良性对照相比差异表达,通过 Western blot 或 ELISA 分析,但表现出高个体间变异性。通过组织微阵列分析,发现原肌球蛋白 1 在侵袭性(T2+)上皮细胞中的表达明显低于高风险非侵袭性(T1G3)肿瘤,偶尔在基质中表达;重要的是,这种模式与预后不良和死亡率增加强烈相关。在 T24 BC 细胞中研究了原肌球蛋白 1 的功能相关性,使用抗体阻断该蛋白导致细胞迁移能力下降,同时肌动蛋白聚合减少。总之,我们的研究涉及尿液蛋白质分级方法的应用,作为该分析的一个主要结果,揭示了原肌球蛋白 1 与 BC 的关联,为其在 BC 分层中的进一步研究铺平了道路。