Amyloidogenicity and cytotoxicity of recombinant mature human islet amyloid polypeptide (rhIAPP)
Amyloidogenicity and cytotoxicity of recombinant mature human islet amyloid polypeptide (rhIAPP)
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DOI：
10.1074/jbc.m406108200
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发表时间：
2004-10-08
影响因子：
4.8
通讯作者：
Sogayar, MC
中科院分区：
文献类型：
--
作者：
Dahabada, HJL;Colin, C;Sogayar, MC
由胰岛淀粉样多肽（IAPP）形成的胰腺淀粉样斑块存在于超过95%的II型糖尿病患者中，并且它们的丰度与疾病的严重程度相关。IAPP目前被认为是已知的最具淀粉样蛋白生成性的肽，但其聚集的分子基础仍不完全清楚。淀粉样蛋白形成机制的详细表征需要大量的纯材料。因此，重组IAPP的可用性，在足够的量，这样的研究构成了一个重要的一步，阐明淀粉样蛋白的机制。在这里，我们报告，为第一次，成功地表达，纯化和表征的淀粉样变性和细胞毒性的重组人成熟的IAPP。这种方法很可能是有用的其他淀粉样蛋白生成肽或蛋白质的生产是难以获得的化学合成。
Pancreatic amyloid plaques formed by the pancreatic islet amyloid polypeptide ( IAPP) are present in more than 95% of type II diabetes mellitus patients, and their abundance correlates with the severity of the disease. IAPP is currently considered the most amyloidogenic peptide known, but the molecular bases of its aggregation are still incompletely understood. Detailed characterization of the mechanisms of amyloid formation requires large quantities of pure material. Thus, availability of recombinant IAPP in sufficient amounts for such studies constitutes an important step toward elucidation of the mechanisms of amyloidogenicity. Here, we report, for the first time, the successful expression, purification and characterization of the amyloidogenicity and cytotoxicity of recombinant human mature IAPP. This approach is likely to be useful for the production of other amyloidogenic peptides or proteins that are difficult to obtain by chemical synthesis.