Aspects on human amyloid forms and their fibril polypeptides

被引：187

作者：

Westermark, P ^{[1
]}

机构：

[1] Uppsala Univ, Rudbeck Lab, Dept Genet & Pathol, SE-75185 Uppsala, Sweden

来源：

FEBS JOURNAL | 2005年 / 272卷 / 23期

关键词：

amyloid; deposition; prion; protein folding; seeding;

D O I：

10.1111/j.1742-4658.2005.05024.x

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Amyloid is an in vivo fibrillar substance containing a fibril protein and several additional molecules. Presently, 25 proteins have been reported as main fibril components. Why just a few proteins form amyloid in vivo is still insufficiently understood. Many fibril proteins appear as fragments of larger precursors and for some types it is not clear whether fragmentation comes before or after fibrillation. The self-assembly by amyloid proteins can be speeded up by seeding with preformed fibrils. In mice, systemic amyloidoses are transmissible by a seeding mechanism. Whether this prion-like mechanism occurs in humans is not known, but can definitely not be ruled out.

引用

页码：5942 / 5949

页数：8

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