国际淀粉样变性学会（ISA）命名委员会在该学会的XVth研讨会上开会，2016年7月3日-7月7日,乌普萨拉,瑞典,评估和制定淀粉样蛋白的命名法和淀粉样蛋白的临床分类的建议。淀粉样蛋白原纤维必须对刚果红和绿色具有亲和力，当用偏振光观察刚果红染色的沉积物时，黄色或橙色双折射。虽然血友病和双折射仍然是证明淀粉样沉积物的黄金标准，新的染色和成像技术被证明是有用的。要包含在术语列表中，除了血友病和双折射，蛋白质的化学特性必须在可能的情况下通过蛋白质序列分析明确地表征。总的来说,在没有证实淀粉样蛋白原蛋白的变异变化的情况下,鉴定候选淀粉样蛋白的基因中的突变是不够的。淀粉样变性的每种不同形式的独特特征在于沉积在组织和器官的细胞外空间中并引起疾病综合征的淀粉样原纤维蛋白的化学特性。原纤维蛋白被指定为蛋白A,随后是作为亲本或前体蛋白名称的缩写的后缀。迄今为止,人类中有36种已知的细胞外原纤维蛋白，其中2种在本质上是医源性的，其中9种也已在动物中鉴定。两种新发现的原纤维蛋白，来自载脂蛋白I的ApoCII和来自载脂蛋白II的ApoCIII，已添加。ApoCII淀粉样变性和ApoCIII淀粉样变性是遗传性系统性淀粉样变性。细胞内蛋白质内含物显示淀粉样蛋白的一些特性，已经报道了“细胞内淀粉样蛋白”。两种以前被称为细胞内包涵体的蛋白质，tau和α-突触核蛋白，现在被认为在细胞死亡时形成细胞外沉积物，因此已作为ATau和AαSyn包括在表1中。
The Nomenclature Committee of the International Society of Amyloidosis (ISA) met during the XVth Symposium of the Society, 3 July-7 July 2016, Uppsala, Sweden, to assess and formulate recommendations for nomenclature for amyloid fibril proteins and the clinical classification of the amyloidoses. An amyloid fibril must exhibit affinity for Congo red and with green, yellow or orange birefringence when the Congo red-stained deposits are viewed with polarized light. While congophilia and birefringence remain the gold standard for demonstration of amyloid deposits, new staining and imaging techniques are proving useful. To be included in the nomenclature list, in addition to congophilia and birefringence, the chemical identity of the protein must be unambiguously characterized by protein sequence analysis when possible. In general, it is insufficient to identify a mutation in the gene of a candidate amyloid protein without confirming the variant changes in the amyloid fibril protein. Each distinct form of amyloidosis is uniquely characterized by the chemical identity of the amyloid fibril protein that deposits in the extracellular spaces of tissues and organs and gives rise to the disease syndrome. The fibril proteins are designated as protein A followed by a suffix that is an abbreviation of the parent or precursor protein name. To date, there are 36 known extracellular fibril proteins in humans, 2 of which are iatrogenic in nature and 9 of which have also been identified in animals. Two newly recognized fibril proteins, AApoCII derived from apolipoprotein CII and AApoCIII derived from apolipoprotein CIII, have been added. AApoCII amyloidosis and AApoCIII amyloidosis are hereditary systemic amyloidoses. Intracellular protein inclusions displaying some of the properties of amyloid, \"intracellular amyloid\" have been reported. Two proteins which were previously characterized as intracellular inclusions, tau and α-synuclein, are now recognized to form extracellular deposits upon cell death and thus have been included in Table 1 as ATau and AαSyn.
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