Trehalose effects on α-crystallin aggregates

被引：17

作者：

Attanasio, Francesco

Cascio, Claudia

Fisichella, Salvatore

Nicoletti, Vincenzo Giuseppe

Pignataro, Bruno

Savarino, Anna

Rizzarelli, Enrico ^{[1
]}

机构：

[1] Univ Catania, Dipartimento Sci Chim, I-95124 Catania, Italy

[2] CNR, IBB, Catania, Italy

[3] Consorzio Catania Ric, Catania, Italy

[4] Univ Palermo, Dipartimento Chim Fis, I-90133 Palermo, Italy

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2007年 / 354卷 / 04期

关键词：

alpha-crystallin; trehalose; aggregates; chaperone activity; thermal stability;

D O I：

10.1016/j.bbrc.2007.01.061

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：

alpha-Crystallin in its native state is a large, heterogeneous, low-molecular weight (LMW) aggregate that under certain conditions may progressively became part of insoluble high-molecular weight (HMW) systems. These systems are supposed to play a relevant role in eye lens opacification and vision impairment. In this paper, we report the effects of trehalose on alpha-crystallin aggregates. The role of trehalose in alpha-crystallin stress tolerance, chaperone activity and thermal stability is studied. The results show that trehalose stabilizes the alpha-crystallin native structure, inhibits alpha-crystallin aggregation, and disaggregates preformed LMW systems not affecting its chaperone activity. (c) 2007 Elsevier Inc. All rights reserved.

引用

页码：899 / 905

页数：7

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