Redox proteomics: identification and functional role of glutathionylated proteins

被引:64
作者
Fratelli, M [1 ]
Gianazza, E [1 ]
Ghezzi, P [1 ]
机构
[1] Ist Ric Farmacol Mario Negri, I-20157 Milan, Italy
关键词
chaperones; cytoskeletal proteins; glutathione; glycolytic enzymes; oxidative stress; post-translational protein modifications; redox signaling; S-glutathiolation; S-thiolation;
D O I
10.1586/14789450.1.3.365
中图分类号
Q5 [生物化学];
学科分类号
071010 ; 081704 ;
摘要
Although radical oxygen and nitrogen species are harmful molecules that destroy cell functions, many operate as mediators of important cell signaling pathways when not in excess. Oxidants can modify protein function through the covalent, reversible addition of glutathione to cysteine. This review addresses different proteomic methods of identifying glutathionylation targets and emphasizes ways of defining their pattern of modification in response to oxidative stimuli in cells. Finally, the literature on nonproteomic studies that investigate the functional changes induced by glutathionylation are reviewed and future studies are commented on.
引用
收藏
页码:365 / 376
页数:12
相关论文
共 78 条
  • [1] Adachi T, 2004, J BIOL CHEM
  • [2] S-glutathionylation decreases Mg2+ inhibition and S-nitrosylation enhances Ca2+ activation of RyR1 channels
    Aracena, P
    Sánchez, G
    Donoso, P
    Hamilton, SL
    Hidalgo, C
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (44) : 42927 - 42935
  • [3] Regulation of PTP1B via glutathionylation of the active site cysteine 215
    Barrett, WC
    DeGnore, JP
    König, S
    Fales, HM
    Keng, YF
    Zhang, ZY
    Yim, MB
    Chock, PB
    [J]. BIOCHEMISTRY, 1999, 38 (20) : 6699 - 6705
  • [4] Dopamine biosynthesis is regulated by S-glutathionylation -: Potential mechanism of tyrosine hydroxylase inhibition during oxidative stress
    Borges, CR
    Geddes, T
    Watson, JT
    Kuhn, DM
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2002, 277 (50) : 48295 - 48302
  • [5] Redox events in interleukin-1 signaling
    Brigelius-Flohé, R
    Banning, A
    Kny, M
    Böl, GF
    [J]. ARCHIVES OF BIOCHEMISTRY AND BIOPHYSICS, 2004, 423 (01) : 66 - 73
  • [6] Regulation of annexin A2 by reversible glutathionylation
    Caplan, JF
    Filipenko, NR
    Fitzpatrick, SL
    Waisman, DM
    [J]. JOURNAL OF BIOLOGICAL CHEMISTRY, 2004, 279 (09) : 7740 - 7750
  • [7] Proteomic analysis of brain proteins in the gracile axonal dystrophy (gad) mouse, a syndrome that emanates from dysfunctional ubiquitin carboxyl-terminal hydrolase L-1, reveals oxidation of key proteins
    Castegna, A
    Thongboonkerd, V
    Klein, J
    Lynn, BC
    Wang, YL
    Osaka, H
    Wada, K
    Butterfield, DA
    [J]. JOURNAL OF NEUROCHEMISTRY, 2004, 88 (06) : 1540 - 1546
  • [8] Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain.: Part II:: dihydropyrimidinase-related protein 2, α-enolase and heat shock cognate 71
    Castegna, A
    Aksenov, M
    Thongboonkerd, V
    Klein, JB
    Pierce, WM
    Booze, R
    Markesbery, WR
    Butterfield, DA
    [J]. JOURNAL OF NEUROCHEMISTRY, 2002, 82 (06) : 1524 - 1532
  • [9] Proteomic identification of oxidatively modified proteins in Alzheimer's disease brain. Part 1: Creatine kinase bb, glutamine synthase, and ubiquitin carboxy-terminal hydrolase L-1
    Castegna, A
    Aksenov, M
    Aksenova, M
    Thongboonkerd, V
    Klein, JB
    Pierce, WM
    Booze, R
    Markesbery, WR
    Butterfield, DA
    [J]. FREE RADICAL BIOLOGY AND MEDICINE, 2002, 33 (04) : 562 - 571
  • [10] Reversal of protein S-glutathiolation by glutaredoxin in the retinal pigment epithelium
    Chai, YC
    Hoppe, G
    Sears, J
    [J]. EXPERIMENTAL EYE RESEARCH, 2003, 76 (02) : 155 - 159