Structural analyses of fibrinogen amyloid fibrils

被引：33
作者：
Serpell, Louise C.
Benson, Merrill
Liepnieks, Juris J.
Fraser, Paul E.
机构：
[1] Univ Sussex, Brighton BN1 9QG, E Sussex, England
[2] Indiana Univ, Sch Med, Dept Pathol & Lab Med, Indianapolis, IN 46202 USA
[3] Richard L Roudebush Vet Affairs Med Ctr, Indianapolis, IN 46202 USA
[4] Univ Toronto, Ctr Res Neurodegenerat Dis, Toronto, ON MS5 3H2, Canada
[5] Univ Toronto, Dept Med Biophys, Toronto, ON MS5 3H2, Canada
来源：
AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS | 2007年 / 14卷 / 03期
基金：
英国生物技术与生命科学研究理事会;
关键词：
fibrinogen; amyloid; protein structure; fiber diffraction; electron microscopy; HEREDITARY RENAL AMYLOIDOSIS; FRAME-SHIFT MUTATION; SYNCHROTRON X-RAY; ALPHA-CHAIN GENE; MOLECULAR-BASIS; TRANSPLANTATION; TRANSTHYRETIN; VARIANT; CORE;
D O I：
10.1080/13506120701461111
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：
Hereditary fibrinogen amyloiclosis is characterized by deposition of amyloid fibrils in renal glomeruli. The subunit protein of the amyloid fibrils is a proteolytic fragment of the fibrinogen A alpha-chain. To investigate the structure of fibrinogen amyloid, fibrils were extracted from the tissues of a patient and studied by X-ray fiber diffraction and electron microscopy. We have carried out a full structural characterization of amyloid fibrils taken from disease tissue. These studies revealed that ex vivo fibrinogen amyloid fibrils have a cross-beta structure similar to other chemical types of amyloid fibrils.
引用
收藏
页码：199 / 203
页数：5
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