Amyloids, prions and the inherent infectious nature of misfolded protein aggregates

被引:204
作者
Soto, C [1 ]
Estrada, L
Castilla, J
机构
[1] Univ Texas, Med Branch, George & Cynthia Mitchell Ctr Alzheimers Dis & Re, Dept Neurol, Galveston, TX 77555 USA
[2] Univ Texas, Med Branch, Dept Neurosci & Cell Biol, Galveston, TX 77555 USA
[3] Univ Texas, Med Branch, Dept Biochem & Mol Biol, Galveston, TX 77555 USA
关键词
D O I
10.1016/j.tibs.2006.01.002
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
Misfolded aggregates present in amyloid fibrils are associated with various diseases known as 'protein misfolding' disorders. Among them, prion diseases are unique in that the pathology can be transmitted by an infectious process involving an unprecedented agent known as a 'prion'. Prions are infectious proteins that can transmit biological information by propagating protein misfolding and aggregation. The molecular mechanism of prion conversion has a striking resemblance to the process of amyloid formation, suggesting that misfolded aggregates have an inherent ability to be transmissible. Intriguing recent data suggest that other protein misfolding disorders might also be transmitted by a prion-like infectious process.
引用
收藏
页码:150 / 155
页数:6
相关论文
共 71 条
[31]   Acceleration of amyloid protein A amyloidosis by amyloid-like synthetic fibrils [J].
Johan, K ;
Westermark, G ;
Engström, U ;
Gustavsson, Å ;
Hultman, P ;
Westermark, P .
PROCEEDINGS OF THE NATIONAL ACADEMY OF SCIENCES OF THE UNITED STATES OF AMERICA, 1998, 95 (05) :2558-2563
[32]   Evidence for seeding of β-amyloid by intracerebral infusion of Alzheimer brain extracts in β-amyloid precursor protein-transgenic mice [J].
Kane, MD ;
Lipinski, WJ ;
Callahan, MJ ;
Bian, F ;
Durham, RA ;
Schwarz, RD ;
Roher, AE ;
Walker, LC .
JOURNAL OF NEUROSCIENCE, 2000, 20 (10) :3606-3611
[33]   Alternative conformations of amyloidogenic proteins govern their behavior [J].
Kelly, JW .
CURRENT OPINION IN STRUCTURAL BIOLOGY, 1996, 6 (01) :11-17
[34]  
KIMBERLIN RH, 1976, SCI PROGRESS-UK, V63, P461
[35]   Protein-only transmission of three yeast prion strains [J].
King, CY ;
Diaz-Avalos, R .
NATURE, 2004, 428 (6980) :319-323
[36]   New clothes for amyloid enhancing factor (AEF): silk as AEF [J].
Kisilevsky, R ;
Lemieux, L ;
Boudreau, L ;
Dun-Sheng, Y ;
Fraser, P .
AMYLOID-INTERNATIONAL JOURNAL OF EXPERIMENTAL AND CLINICAL INVESTIGATION, 1999, 6 (02) :98-106
[37]  
KISILEVSKY R, 1983, LAB INVEST, V48, P53
[38]   CELL-FREE FORMATION OF PROTEASE-RESISTANT PRION PROTEIN [J].
KOCISKO, DA ;
COME, JH ;
PRIOLA, SA ;
CHESEBRO, B ;
RAYMOND, GJ ;
LANSBURY, PT ;
CAUGHEY, B .
NATURE, 1994, 370 (6489) :471-474
[39]   Observation of sequence specificity in the seeding of protein amyloid fibrils [J].
Krebs, MRH ;
Morozova-Roche, LA ;
Daniel, K ;
Robinson, CV ;
Dobson, CM .
PROTEIN SCIENCE, 2004, 13 (07) :1933-1938
[40]   Yeast [PSI+] prion aggregates are formed by small Sup35 polymers fragmented by Hsp104 [J].
Kryndushkin, DS ;
Alexandrov, IM ;
Ter-Avanesyan, MD ;
Kushnirov, VV .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (49) :49636-49643