Functional amyloids signal their arrival.

Functional amyloids signal their arrival.
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DOI:
10.1126/scisignal.280pe43
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发表时间:
2009-07-21
期刊:
影响因子:
7.3
通讯作者:
Chapman MR
Chapman MR
中科院分区:
生物学1区
文献类型:
--
作者:
Badtke MP;Hammer ND;Chapman MR

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传统上,淀粉样蛋白与错误折叠的蛋白质聚集体和使人衰弱的神经退行性疾病有关。然而,现在越来越多的功能性淀粉样蛋白被描述,证明淀粉样蛋白的形成可以是正常细胞生理学的一个组成部分。功能性淀粉样蛋白的产生受到高度调控,产生的纤维为产生它们的细胞发挥多种作用。淀粉样蛋白作为哺乳动物分泌颗粒内肽激素储存库的新作用已被发现。超过 30 种不同的肽激素已被发现在体外形成淀粉样蛋白,大鼠和小鼠均已被证明可以在分泌颗粒中储存激素淀粉样蛋白沉积物。因此,新出现的证据增加了淀粉样蛋白的多种作用,并对肽激素和功能性淀粉样蛋白领域提出了有趣的问题。
Amyloids have traditionally been associated with misfolded protein aggregates and debilitating neurodegenerative diseases. However, a growing number of functional amyloids have now been described that demonstrate that amyloid formation can be an integral part of normal cellular physiology. Functional amyloid production is highly regulated, and the resulting fibers serve a variety of roles for the cells that produce them. A new role for amyloid as storage reservoirs for peptide hormones within mammalian secretory granules has been discovered. More than 30 different peptide hormones have been found to form amyloids in vitro, and both rats and mice have been shown to store hormone amyloid deposits in secretory granules. Thus, the emerging evidence adds to the diverse roles of amyloid and raises intriguing questions for both the peptide hormone and the functional amyloid fields.
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