Aging and molecular chaperones

被引:111
作者
Soti, C [1 ]
Csermely, P [1 ]
机构
[1] Semmelweis Univ, Dept Med Chem, H-1444 Budapest, Hungary
关键词
molecular chaperones; heat shock proteins; stress proteins; Hsp70; Hsp90; protein aggregation; protein denaturation; chaperone overload; HEAT-SHOCK; PROTEIN OXIDATION; HSP90; DETERIORATION; ACTIVATION; SENESCENCE; CELLS; HSF1;
D O I
10.1016/S0531-5565(03)00185-2
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
Chaperone function plays a key role in sequestering damaged proteins and in repairing proteotoxic damage. Chaperones are induced by environmental stress and are called as stress or heat shock proteins. Here, we summarize the current knowledge about protein damage in aged organisms, about changes in proteolytic degradation, chaperone expression and function in the aging process, as well as the involvement of chaperones in longevity and cellular senescence. The role of chaperones in aging diseases, such as in Alzheimer's disease, Parkinson's disease, Huntington's disease and in other neurodegenerative diseases as well as in atherosclerosis and in cancer is discussed. We also describe how the balance between chaperone requirement and availability becomes disturbed in aged organisms, or in other words, how chaperone overload develops. The consequences of chaperone overload are also outlined together with several new research strategies to assess the functional status of chaperones in the aging process. (C) 2003 Elsevier Inc. All rights reserved.
引用
收藏
页码:1037 / 1040
页数:4
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