An assessment of proposed mechanisms for sensing hydrogen peroxide in mammalian systems

被引:159
作者
Stone, JR [1 ]
机构
[1] Harvard Univ, Massachusetts Gen Hosp, Sch Med, Dept Pathol, Boston, MA 02114 USA
关键词
tyrosine phosphatase; peroxiredoxin; peroxidase; OxyR; reactive oxygen species; oxidative stress; thiolate; sulfenic acid; hydrogen peroxide; redox;
D O I
10.1016/j.abb.2003.12.029
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
Despite much recent interest in the biochemistry of reactive oxygen species, the mechanisms by which hydrogen peroxide (H2O2) functions in mammalian cells remain poorly defined. Proposed mechanisms for sensing H2O2 in mammalian cells include inactivation of protein tyrosine phosphatases and dual specificity phosphatases as well as inactivation of peroxiredoxins. In this critical review, proteins proposed to serve as sensors for H2O2 in mammals will be compared to peroxidases, catalases, and the bacterial H2O2 sensor OxyR for their ability to react with H2O2, in the context of our current knowledge concerning the concentrations of H2O2 present in cells. (C) 2004 Elsevier Inc. All rights reserved.
引用
收藏
页码:119 / 124
页数:6
相关论文
共 62 条
[51]   The role of hydrogen peroxide in endothelial proliferative responses [J].
Stone, JR ;
Collins, T .
ENDOTHELIUM-JOURNAL OF ENDOTHELIAL CELL RESEARCH, 2002, 9 (04) :231-238
[52]   Rapid phosphorylation of heterogeneous nuclear ribonucleoprotein C1/C2 in response to Physiologic levels of hydrogen peroxide in human endothelial cells [J].
Stone, JR ;
Collins, T .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (18) :15621-15628
[53]   Oxidation state of the active-site cysteine in protein tyrosine phosphatase 1B [J].
van Montfort, RLM ;
Congreve, M ;
Tisi, D ;
Carr, R ;
Jhoti, H .
NATURE, 2003, 423 (6941) :773-777
[54]   The superoxide-generating NADPH oxidase: structural aspects and activation mechanism [J].
Vignais, PV .
CELLULAR AND MOLECULAR LIFE SCIENCES, 2002, 59 (09) :1428-1459
[55]   Reactivity of biologically important thiol compounds with superoxide and hydrogen peroxide [J].
Winterbourn, CC ;
Metodiewa, D .
FREE RADICAL BIOLOGY AND MEDICINE, 1999, 27 (3-4) :322-328
[56]   Reversing the inactivation of peroxiredoxins caused by cysteine sulfinic acid formation [J].
Woo, HA ;
Chae, HZ ;
Hwang, SC ;
Yang, KS ;
Kang, SW ;
Kim, K ;
Rhee, SG .
SCIENCE, 2003, 300 (5619) :653-656
[57]   Peroxiredoxin evolution and the regulation of hydrogen peroxide signaling [J].
Wood, ZA ;
Poole, LB ;
Karplus, PA .
SCIENCE, 2003, 300 (5619) :650-653
[58]   Dimers to doughnuts: Redox-sensitive oligomerization of 2-cysteine peroxiredoxins [J].
Wood, ZA ;
Poole, LB ;
Hantgan, RR ;
Karplus, PA .
BIOCHEMISTRY, 2002, 41 (17) :5493-5504
[59]   Structure, mechanism and regulation of peroxiredoxins [J].
Wood, ZA ;
Schröder, E ;
Harris, JR ;
Poole, LB .
TRENDS IN BIOCHEMICAL SCIENCES, 2003, 28 (01) :32-40
[60]   Inactivation of human peroxiredoxin I during catalysis as the result of the oxidation of the catalytic site cysteine to cysteine-sulfinic acid [J].
Yang, KS ;
Kang, SW ;
Woo, HA ;
Hwang, SC ;
Chae, HZ ;
Kim, K ;
Rhee, SG .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (41) :38029-38036