Amyloid deposits derived from the amylin peptide accumulate within pancreatic islet beta-cells in most cases of type-2 diabetes mellitus (T2Dm). Human amylin 'oligomers' are toxic to these cells. Using two different experimental techniques, we found that H(2)O(2) was generated during the aggregation of human amylin into amyloid fibrils. This process was greatly stimulated by Cu(II) ions, and human amylin was retained on a copper affinity column. In contrast, rodent amylin, which is not toxic, failed to generate any H(2)O(2) and did not interact with copper. We conclude that the formation of H(2)O(2) from amylin could contribute to the progressive degeneration of islet cells in T2Dm.

译文

在大多数2型糖尿病 (T2Dm) 病例中,源自胰淀素肽的淀粉样蛋白沉积物积聚在胰岛 β 细胞内。人胰淀素 “寡聚体” 对这些细胞有毒。使用两种不同的实验技术,我们发现H(2)O(2) 是在人淀粉样蛋白聚集成淀粉样原纤维的过程中产生的。Cu(II) 离子极大地刺激了该过程,并且人胰淀素保留在铜亲和柱上。相反,无毒的啮齿动物amylin无法产生任何H(2)O(2),并且不与铜相互作用。我们得出的结论是,胰淀素形成的H(2)O(2) 可能有助于T2Dm中胰岛细胞的进行性变性。

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