Loo Dorothy, Mollee Peter N, Renaut Patricia, Hill Michelle M
The University of Queensland Diamantina Institute, The University of Queensland, Brisbane, QLD 4102, Australia.
J Biomed Biotechnol. 2011;2011:754109. doi: 10.1155/2011/754109. Epub 2011 Oct 29.
Amyloidosis is a group of disorders caused by deposition of misfolded proteins as aggregates in the extracellular tissues of the body, leading to impairment of organ function. Correct identification of the causal amyloid protein is absolutely crucial for clinical management in order to avoid misdiagnosis and inappropriate, potentially harmful treatment, to assess prognosis and to offer genetic counselling if relevant. Current diagnostic methods, including antibody-based amyloid typing, have limited ability to detect the full range of amyloid forming proteins. Recent investigations into proteomic identification of amyloid protein have shown promise. This paper will review the current state of the art in proteomic analysis of amyloidosis, discuss the suitability of techniques based on the properties of amyloidosis, and further suggest potential areas of development. Establishment of mass spectrometry aided amyloid typing procedures in the pathology laboratory will allow accurate amyloidosis diagnosis in a timely manner and greatly facilitate clinical management of the disease.
淀粉样变性是一组由错误折叠的蛋白质聚集体沉积在身体细胞外组织中引起的疾病，导致器官功能受损。正确识别致病淀粉样蛋白对于临床管理至关重要，以避免误诊和不适当的、可能有害的治疗，评估预后，并在相关时提供遗传咨询。目前的诊断方法，包括基于抗体的淀粉样蛋白分型，检测淀粉样蛋白形成蛋白的能力有限。最近对淀粉样蛋白的蛋白质组学鉴定的研究显示出了前景。本文将综述淀粉样变性蛋白质组学分析的当前技术水平，根据淀粉样变性的特性讨论技术的适用性，并进一步提出潜在的发展领域。在病理实验室建立质谱辅助淀粉样蛋白分型程序将能够及时准确地诊断淀粉样变性，并极大地促进该疾病的临床管理。
