Department of Biosignaling and Radioisotope Experiment, Interdisciplinary Center for Science Research, Organization for Research, Shimane University, Izumo 693-8501, Japan.
Department of Pharmacology, Shimane University School of Medicine, Izumo 693-8501, Japan.
Int J Mol Med. 2014 Apr;33(4):1035-47. doi: 10.3892/ijmm.2014.1627. Epub 2014 Jan 17.
The pathogenesis of abdominal aortic aneurysms (AAAs) and that of thoracic aortic aneurysms (TAAs) is distinct. In this study, to reveal the differences in their biochemical properties, we performed quantitative proteomic analysis of AAAs and TAAs compared with adjacent normal aorta (NA) tissues. The proteomic analysis revealed 176 non-redundant differentially expressed proteins in the AAAs and 189 proteins in the TAAs which were common in at least 5 samples within 7 samples of each. Among the identified proteins, 55 and 68 proteins were unique to the AAAs and TAAs, respectively, whereas 121 proteins were identified in both the AAAs and TAAs. Panther overrepresentation analysis of the unique proteins in the AAAs and TAAs revealed a significant downregulation of the blood coagulation pathway in the AAAs and that of the integrin signaling pathway in the TAAs. On the other hand, Genesis analysis revealed distinct expression patterns of 58 proteins among the 121 proteins. Panther overrepresentation analysis of these 58 proteins revealed that the expression of these proteins in the blood coagulation and the plasminogen activating cascade was decreased in the AAAs, whereas it was increased in the TAAs compared with the NA tissues. On the other hand, the protein expression in the integrin signaling pathway was increased in the AAAs, whereas it was decreased in the TAAs compared with the NA tissues. Thus, the data presented in this study indicate that the proteins that show differential expression patterns in AAAs and TAAs may be involved in the distinct pathogenesis of AAAs and TAAs.
腹主动脉瘤 (AAA) 和胸主动脉瘤 (TAA) 的发病机制不同。在这项研究中,为了揭示它们生化特性的差异,我们对 AAA 和 TAA 与相邻正常主动脉 (NA) 组织进行了定量蛋白质组学分析。蛋白质组学分析显示,AAA 中有 176 个非冗余差异表达蛋白,TAA 中有 189 个蛋白,这两种蛋白在 7 个样本中的至少 5 个样本中是共同的。在所鉴定的蛋白质中,55 个和 68 个蛋白分别是 AAA 和 TAA 所特有的,而 121 个蛋白在 AAA 和 TAA 中都有鉴定到。对 AAA 和 TAA 中特有的蛋白质进行 Panther 过表达分析显示,AAA 中血液凝固途径显著下调,TAA 中整合素信号通路显著下调。另一方面,Genesis 分析显示在 121 个蛋白中有 58 个蛋白的表达模式不同。对这 58 个蛋白进行 Panther 过表达分析显示,与 NA 组织相比,AAA 中血液凝固和纤溶酶原激活级联的蛋白表达降低,而 TAA 中则升高。另一方面,AAA 中整合素信号通路的蛋白表达增加,而 TAA 中则降低。因此,本研究提供的数据表明,在 AAA 和 TAA 中表现出差异表达模式的蛋白质可能参与了 AAA 和 TAA 不同的发病机制。