Laboratory of Proteomics & Analytical Technologies, Cancer Research Technology Program, Frederick National Laboratory for Cancer Research, National Cancer Institute at Frederick, PO Box B, Frederick, MD 21702, USA.
Biomark Med. 2014;8(2):269-86. doi: 10.2217/bmm.13.101.
The discovery of clinically relevant cancer biomarkers using mass spectrometry (MS)-based proteomics has proven difficult, primarily because of the enormous dynamic range of blood-derived protein concentrations and the fact that the 22 most abundant blood-derived proteins constitute approximately 99% of the total plasma protein mass. Immunodepletion of clinical body fluid specimens (e.g., serum/plasma) for the removal of highly abundant proteins is a reasonable and reproducible solution. Often overlooked, clinical tissue specimens also contain a formidable amount of highly abundant blood-derived proteins present in tissue-embedded networks of blood/lymph capillaries and interstitial fluid. Hence, the dynamic range impediment to biomarker discovery remains a formidable obstacle, regardless of clinical sample type (solid tissue and/or body fluid). Thus, we optimized and applied simultaneous immunodepletion of blood-derived proteins from solid tissue and peripheral blood, using clear cell renal cell carcinoma as a model disease. Integrative analysis of data from this approach and genomic data obtained from the same type of tumor revealed concordant key pathways and protein targets germane to clear cell renal cell carcinoma. This includes the activation of the lipogenic pathway characterized by increased expression of adipophilin (PLIN2) along with 'cadherin switching', a phenomenon indicative of transcriptional reprogramming linked to renal epithelial dedifferentiation. We also applied immunodepletion of abundant blood-derived proteins to various tissue types (e.g., adipose tissue and breast tissue) showing unambiguously that the removal of abundant blood-derived proteins represents a powerful tool for the reproducible profiling of tissue proteomes. Herein, we show that the removal of abundant blood-derived proteins from solid tissue specimens is of equal importance to depletion of body fluids and recommend its routine use in the context of biological discovery and/or cancer biomarker research. Finally, this perspective presents the background, rationale and strategy for using tissue-directed high-resolution/accuracy MS-based shotgun proteomics to detect genuine tumor proteins in the peripheral blood of a patient diagnosed with nonmetastatic cancer, employing concurrent liquid chromatography-MS analysis of immunodepleted clinical tissue and blood specimens.
使用基于质谱(MS)的蛋白质组学发现具有临床相关性的癌症生物标志物一直很困难,主要是因为血液来源蛋白浓度的巨大动态范围,以及 22 种最丰富的血液来源蛋白构成了大约 99%的总血浆蛋白质量。免疫耗尽临床体液标本(如血清/血浆)以去除高丰度蛋白是一种合理且可重复的解决方案。通常被忽视的是,临床组织标本中也存在大量存在于组织中嵌入的血液/淋巴毛细血管和间质液网络中的高丰度血液来源蛋白。因此,无论临床样本类型(实体组织和/或体液)如何,发现生物标志物的动态范围障碍仍然是一个巨大的障碍。因此,我们使用透明细胞肾细胞癌作为模型疾病,优化并应用了从实体组织和外周血中同时免疫耗尽血液来源蛋白的方法。对该方法获得的数据和同一肿瘤获得的基因组数据进行综合分析,揭示了与透明细胞肾细胞癌相关的一致关键途径和蛋白质靶标。这包括脂肪生成途径的激活,其特征是脂肪蛋白(PLIN2)的表达增加以及“钙粘蛋白转换”,这是与肾上皮去分化相关的转录重编程的现象。我们还将丰富的血液来源蛋白的免疫耗尽应用于各种组织类型(如脂肪组织和乳腺组织),明确表明去除丰富的血液来源蛋白是组织蛋白质组可重复分析的有力工具。在此,我们表明从实体组织标本中去除丰富的血液来源蛋白与耗尽体液同样重要,并建议在生物发现和/或癌症生物标志物研究的背景下常规使用。最后,本观点提出了使用组织定向高分辨率/准确度 MS 基 shotgun 蛋白质组学来检测在诊断为非转移性癌症的患者的外周血中真正的肿瘤蛋白的背景、原理和策略,同时进行免疫耗尽的临床组织和血液标本的液相色谱-MS 分析。