Protein homeostasis and molecular chaperones in aging

被引：26

作者：

Arslan, Mehmet Alper ^{[1
]}

Csermely, Peter ^{[1
]}

Soti, Csaba ^{[1
]}

机构：

[1] Semmelweis Univ, Dept Med Chem, H-1444 Budapest 8, Hungary

来源：

BIOGERONTOLOGY | 2006年 / 7卷 / 5-6期

关键词：

heat shock protein; stress protein; chaperones-chaperone overload; aging; neurodegenerative diseases; protein folding; protein damage; zinc; metallothionein; immune response;

D O I：

10.1007/s10522-006-9053-7

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：

Molecular chaperones are ubiquitous, highly conserved proteins responsible for the maintenance of protein folding homeostasis in cells. Environmental stress causes proteotoxic damage, which triggers chaperone induction and the subsequent reparation of cellular damage by chaperones, including disposing irreparable protein ensembles. We summarize the current view of protein damage, turnover, the stress response and chaperone function in aging, and review novel data showing that accumulation of misfolded proteins outcompete and overload the limited resources of the protein folding, maintenance and turnover system, compromising general protein homeastasis and cellular function. Possible involvement of chaperones and proteolysis in immunosenescence is highlighted. Defects in zinc metabolism are also addressed in relation to aging and changes in chaperone levels.

引用

页码：383 / 389

页数：7

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