Amyloid Formation: Age-Related Mechanism in Creutzfeldt-Jakob Disease?

被引：6

作者：

Luers, L. ^{[2
]}

Panza, G. ^{[2
]}

Henke, F. ^{[1
]}

Agyenim, T. ^{[2
]}

Weiss, J. ^{[3
]}

Willbold, D. ^{[1
,2
]}

Birkmann, E. ^{[1
,2
]}

机构：

[1] Forschungszentrum Julich, Inst Strukturbiol & Biophys ISB 3, D-52425 Julich, Germany

[2] Univ Dusseldorf, Inst Phys Biol, D-4000 Dusseldorf, Germany

[3] Deutsch Diabet Zentrum, Inst Klin Biochem & Pathobiochem, Dusseldorf, Germany

来源：

REJUVENATION RESEARCH | 2010年 / 13卷 / 2-3期

关键词：

PRION PROTEIN;

D O I：

10.1089/rej.2009.0932

中图分类号：

R592 [老年病学]; C [社会科学总论];

学科分类号：

03 ; 0303 ; 100203 ;

摘要：

Protein aggregation occurs in many age-related neurodegenerative diseases, where it can lead to deposits of naturally occurring proteins in the brain. In case of Creutzfeldt-Jakob disease (CJD), these deposits consist of prion protein (PrP). CJD has three etiologies: spontaneous, genetic, or caused by infection. A polymorphism within the PrP gene is associated with susceptibility of infection. The main event in prion diseases is the conversion of PrP from its naturally occurring isoform to its disease-associated isoform. Here, we present the adaption of a previously reported in vitro conversion system based on hamster recombinant PrP to analyze amyloid fibril formation of human recombinant PrP. We further compare the aggregation characteristics of the human PrP according to the polymorphism variants M129 and V129.

引用

页码：214 / 216

页数：3

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