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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 >Comparison of amyloid fibril formation by two closely related immunoglobulin light chain variable domains
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Comparison of amyloid fibril formation by two closely related immunoglobulin light chain variable domains

机译：比较两个密切相关的免疫球蛋白轻链可变域形成淀粉样蛋白原纤维

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摘要

Light chain amyloidosis AL amyloidosis is a haematological disorder in which a clonal population of B cells expands and secretes enormous amounts of the immunoglobulin light chain protein. These light chains misfold and aggregate into amyloid fibrils, leading to organ dysfunction and death. We have studied the in vitro fibril formation kinetics of two patient-derived immunoglobulin light chain variable domain proteins, designated AL-09 and AL-103, in response to changes in solution conditions. Both proteins are members of the κI O18:O8 germline and therefore are highly similar in sequence, but they presented with different clinical phenotypes. We find that AL-09 forms fibrils more readily and more rapidly than AL-103 in vitro, mirroring the clinical phenotypes of the patients and suggesting a possible connection between the fibril kinetics of the disease protein and the disease progression.
机译：轻链淀粉样变性AL淀粉样变性是一种血液疾病，其中B细胞的克隆种群会扩张并分泌大量的免疫球蛋白轻链蛋白。这些轻链错误折叠并聚集成淀粉样原纤维，导致器官功能障碍和死亡。我们已经研究了两种患者来源的免疫球蛋白轻链可变域蛋白，分别命名为AL-09和AL-103的体外原纤维形成动力学，以响应溶液条件的变化。两种蛋白质都是κ1018：O8生殖系的成员，因此在序列上高度相似，但是它们具有不同的临床表型。我们发现，AL-09在体外比AL-103更容易，更快地形成原纤维，反映了患者的临床表型，并暗示了疾病蛋白的原纤维动力学与疾病进展之间可能存在联系。

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