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首页> 外文期刊>Amyloid: the international journal of experimental and clinical investigation : the official journal of the International Society of Amyloidosis >Proteomic typing of amyloid deposits in systemic amyloidoses.
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Proteomic typing of amyloid deposits in systemic amyloidoses.

机译：全身性淀粉样蛋白中淀粉样蛋白沉积的蛋白质组学分型。

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摘要

Amyloidoses are characterized by the presence of extracellular amyloid deposits, constituted by fibrillar aggregates of misfolded proteins. Despite the similar morphologic appearance of fibrils, at least 28 different proteins have been detected as causative agents of human amyloidoses, 14 of which associated with systemic forms. Unequivocal typing of the amyloid deposits is a key step in the management of these diseases. Existing drawbacks of traditional, immunohistochemistry-based techniques have driven the search for alternative solutions for direct amyloid typing. Proteomics indicates the comprehensive study of the proteins in a biological sample, centered on analysis by mass spectrometry. The great potential of this approach in describing the composition of amyloid deposits and in studying the molecular features of the amyloidogenic precursors has become immediately clear and the introduction of proteomics in the clinical practice has revolutionized the field of amyloid typing. This review provides a critical overview of the various approaches that have been proposed in this specific context, along with a brief description of the proteomic methods for assessment of the circulating amyloidogenic proteins.
机译：淀粉样糖的特征在于存在由错误折叠的蛋白质的纤维状聚集物构成的细胞外淀粉样沉积物。尽管原纤维具有相似的形态学外观，但已检测到至少28种不同的蛋白质是人类淀粉样蛋白的病原体，其中14种与全身性形式有关。淀粉样蛋白沉积物的明确分型是控制这些疾病的关键步骤。传统的，基于免疫组织化学的技术的现有缺点促使人们寻求直接淀粉样蛋白分型的替代解决方案。蛋白质组学表明，对生物样品中蛋白质的全面研究以质谱分析为中心。这种方法在描述淀粉样蛋白沉积物的组成以及研究淀粉样蛋白生成前体的分子特征方面的巨大潜力已经变得显而易见，并且蛋白质组学在临床实践中的引入彻底改变了淀粉样蛋白分型领域。这篇综述提供了在此特定情况下已提出的各种方法的重要概述，并简要介绍了用于评估循环淀粉样蛋白的蛋白质组学方法。

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