Institute for Biomedical Technologies Consiglio Nazionale delle Ricerche, Segrate, Italy.
Amyloid. 2012 Jun;19 Suppl 1:11-3. doi: 10.3109/13506129.2012.674989. Epub 2012 May 2.
In Transthyretin amyloidosis (ATTR), tissue deposition of transthyretin fibrils translates into a significant subversion of the tissues proteome. We used multidimensional protein identification technology for profiling the proteome of subcutaneous adipose tissue in patients with ATTR, in comparison with controls and patients with other types of amyloidoses, to identify the global proteomic changes related specifically with this disease. The adipose tissue proteome of five ATTR patients and 11 non-affected controls was analyzed. Samples from patients with Light Chain (AL) or reactive (AA) amyloidosis were studied alongside. In all ATTR samples, mass spectrometry data showed that transthyretin was specifically up-represented, being a marker of the nature of the deposits. Tissue resident proteins, involved in key biological processes, were also found to be differently represented compared to controls. The high-throughput analysis of the proteome of amyloid affected fat, combined with bioinformatic data interpretation, is a powerful tool for identification of perturbed protein expression in ATTR amyloidosis.
在转甲状腺素蛋白淀粉样变性（ATTR）中，转甲状腺素蛋白纤维的组织沉积导致组织蛋白质组发生显著改变。我们使用多维蛋白质鉴定技术对ATTR 患者的皮下脂肪组织蛋白质组进行了分析，与对照组和其他类型淀粉样变性患者进行了比较，以确定与该疾病相关的特定的全局蛋白质组变化。对 5 名ATTR 患者和 11 名无病变对照者的脂肪组织蛋白质组进行了分析。同时研究了患有轻链（AL）或反应性（AA）淀粉样变性的患者的样本。在所有 ATTR 样本中，质谱数据表明转甲状腺素蛋白特异性上调，是沉积物性质的标志物。与对照组相比，还发现组织驻留蛋白在关键生物过程中表达不同。对淀粉样变脂肪的蛋白质组进行高通量分析，并结合生物信息学数据分析，是鉴定ATTR 淀粉样变性中蛋白质表达失调的有力工具。
