Glutathione directly reduces an oxidoreductase in the endoplasmic reticulum of mammalian cells.
AuthorsJessop CE, Bulleid NJ
JournalJ Biol Chem
PubMed ID15507438
'The formation of disulfide bonds is an essential step in the folding of many glycoproteins and secretory proteins. Non-native disulfide bonds are often formed between incorrect cysteine residues, and thus the cell has dedicated a family of oxidoreductases that are thought to isomerize non-native bonds. For an oxidoreductase to be ... More
S-glutathiolation by peroxynitrite of p21ras at cysteine-118 mediates its direct activation and downstream signaling in endothelial cells.
AuthorsClavreul N, Adachi T, Pimental DR, Ido Y, Schöneich C, Cohen RA
JournalFASEB J
PubMed ID16415107
'The highly reactive species, peroxynitrite, is produced in endothelial cells in pathological states in which the production of superoxide anion and NO is increased. Here, we show that peroxynitrite added exogenously or generated endogenously in response to exposure to an NO donor or oxidized low-density lipoproteins (oxLDL) increases p21ras activity ... More
Detection and affinity purification of oxidant-sensitive proteins using biotinylated glutathione ethyl ester.
AuthorsSullivan DM, Levine RL, Finkel T,
JournalMethods Enzymol
PubMed ID12078486
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Detecting oxidative post-translational modifications in proteins.
AuthorsGianazza E, Crawford J, Miller I
JournalAmino Acids
PubMed ID17021655
Oxidative stress induces various post-translational modifications (PTM); some are reversible in vivo via enzymatic catalysis. The present paper reviews specific procedures for the detection of oxidative PTM in proteins, most of them including electrophoresis. Main topics are carbonylated and glutathionylated proteins as well as modification of selected amino acids (Cys, ... More
Glutathione binding to the Bcl-2 homology-3 domain groove: a molecular basis for Bcl-2 antioxidant function at mitochondria.
Bcl-2 protects cells against mitochondrial oxidative stress and subsequent apoptosis. However, the mechanism underlying the antioxidant function of Bcl-2 is currently unknown. Recently, Bax and several Bcl-2 homology-3 domain (BH3)-only proteins (Bid, Puma, and Noxa) have been shown to induce a pro-oxidant state at mitochondria (1-4). Given the opposing effects ... More
Superoxide dismutase 1 regulates caspase-1 and endotoxic shock.
AuthorsMeissner F, Molawi K, Zychlinsky A,
JournalNat Immunol
PubMed ID18604212
Caspase-1 serves an essential function in the initiation of inflammation by proteolytically maturing the cytokines interleukin 1 beta and interleukin 18. Several Nod-like receptors activate caspase-1 in response to microbial and 'danger' signals by assembling cytosolic protein complexes called 'inflammasomes'. We show here that superoxide dismutase 1 (SOD1) regulates caspase-1 ... More
S-glutathionylation of the Rpn2 regulatory subunit inhibits 26 S proteasomal function.
AuthorsZmijewski JW, Banerjee S, Abraham E,
JournalJ Biol Chem
PubMed ID19549781
Although increased intracellular concentrations of hydrogen peroxide (H2O2) are associated with inhibition of 26 S proteasomal activity, the mechanisms responsible for such effects have not been well delineated. In the present studies, we found that direct exposure of purified 26 S proteasomes to H2O2 had negligible effects on their activity, ... More
Dynamic redox control of NF-kappaB through glutaredoxin-regulated S-glutathionylation of inhibitory kappaB kinase beta.
AuthorsReynaert NL, van der Vliet A, Guala AS, McGovern T, Hristova M, Pantano C, Heintz NH, Heim J, Ho YS, Matthews DE, Wouters EF, Janssen-Heininger YM
JournalProc Natl Acad Sci U S A
PubMed ID16916935
The transcription factor NF-kappaB, a central regulator of immunity, is subject to regulation by redox changes. We now report that cysteine-179 of the inhibitory kappaB kinase (IKK) beta-subunit of the IKK signalosome is a central target for oxidative inactivation by means of S-glutathionylation. S-glutathionylation of IKK-beta Cys-179 is reversed by ... More
Regulation of annexin A2 by reversible glutathionylation.
The annexin A2-S100A10 heterotetramer (AIIt) is a multifunctional Ca(2+)-dependent, phospholipid-binding, and F-actin-binding phosphoprotein composed of two annexin A2 subunits and two S100A10 subunits. It was reported previously that oxidative stress from exogenous hydrogen peroxide or generated in response to tumor necrosis factor-alpha results in the glutathionylation of Cys(8) of annexin ... More
Glutathiolation regulates tumor necrosis factor-alpha-induced caspase-3 cleavage and apoptosis: key role for glutaredoxin in the death pathway.
AuthorsPan S, Berk BC
JournalCirc Res
PubMed ID17185628
Caspase-3 cleavage and activation are known to play central roles in apoptosis. However, the mechanisms that regulate caspase-3 cleavage remain elusive. Glutaredoxin (Grx) is a ubiquitous redox molecule that is unique in its ability to regulate S-glutathiolation (glutathiolation) of proteins. Here we show the essential role of Grx in caspase-3 ... More
Identification of oxidant-sensitive proteins: TNF-alpha induces protein glutathiolation.
AuthorsSullivan DM, Wehr NB, Fergusson MM, Levine RL, Finkel T
JournalBiochemistry
PubMed ID10998251
Reactive oxygen species are thought to play a role in a variety of physiologic and pathophysiological processes. One possible mediator of oxidant effects at the molecular level is a subset of proteins containing reactive cysteine thiols that can be readily oxidized. The transient incorporation of glutathione into cellular proteins is ... More
The glutaredoxin/glutathione system modulates NF-kappaB activity by glutathionylation of p65 in cinnamaldehyde-treated endothelial cells.
Authors
JournalToxicol Sci
PubMed ID20351055
S-nitrosylation and S-glutathionylation of Cys134 on troponin I have opposing competitive actions on Ca2+ sensitivity in rat fast-twitch muscle fibers.
Authors
JournalAm J Physiol Cell Physiol
PubMed ID27974300
Cell-Autonomous Regulation of Astrocyte Activation by the Circadian Clock Protein BMAL1.
Authors
JournalCell Rep
PubMed ID30282019
Carbon monoxide induces heme oxygenase-1 to modulate STAT3 activation in endothelial cells via S-glutathionylation.