In vivo thiyl free radical formation from hemoglobin following administration of hydroperoxides

Maples, Kirk R.; Kennedy, Christopher H.; Jordan, Sandra J.; Mason, Ronald P.

doi:10.1016/0003-9861(90)90596-q

Cited by 92 publications

(46 citation statements)

References 26 publications

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“…This suggests that GraPDH may react directly with the large pool of GSH in the cell via an oxiradical-induced thiyl radical intermediate. Recent evidence for the formation of a thiyl radical in hemoglobin in erythrocytes confirms that this process occurs in intact cells [16]. Additionally, studies with creatine kinase, phosphorylase and carbonic anhydrase I11 show that these enzymes can be S-thiolated under conltions where the amount of GSSG formed is not sufficient to cause effective S-thiolation [17, 181.…”

Section: Resultsmentioning

confidence: 99%

S‐Thiolation of human endothelial cell glyceraldehyde‐3‐phosphate dehydrogenase after hydrogen peroxide treatment

Schuppe‐Koistinen

Moldéus

Bergman

et al. 1994

European Journal of Biochemistry

152

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Exposure of human umbilical vein endothelial cells to oxidants such as hydrogen peroxide, tertbutyl hydroperoxide and diamide has been shown to induce oxidant-specific S-thiolation of cellular proteins. In this study one of the main S-thiolated proteins in hydrogen-peroxide-treated cells was identified as the glycolytic enzyme glyceraldehyde-3-phosphate dehydrogenase. Additionally, we have shown that the post-translational modification of the cysteinyl thiols of glyceraldehyde-3-phosphate dehydrogenase accompanies an inhibition of the enzyme and that both events are simultaneously and rapidly reversed upon the removal of the oxidative stimulus.

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Section: Resultsmentioning

confidence: 99%

S‐Thiolation of human endothelial cell glyceraldehyde‐3‐phosphate dehydrogenase after hydrogen peroxide treatment

Schuppe‐Koistinen

Moldéus

Bergman

et al. 1994

European Journal of Biochemistry

152

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“…In the presence of ROS (or RNS), cell-free Hb (αβ) dimers are readily oxidized into ferric HbFe 3+ (αβ), i.e., metHb. In this process, ferryl HbFe 4+ (αβ), a short-lived intermediate is also generated [93], which can result in a potent pro-inflammatory response (Gabriela Silva, unpublished observations). Under homeostatic conditions, ferric HbFe 3+ (αβ) is scavenged by haptoglobin (Hp).…”

Section: Deleterious Effects Of Free Hemementioning

confidence: 99%

A central role for free heme in the pathogenesis of severe malaria: the missing link?

et al. 2008

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“…However, protein radicals are now well recognized as normal intermediates for an increasing number of enzymes and some peroxidase-like hemoproteins. Examples of such radical intermediates include the thiyl radical of ribonucleotide reductase (29 -31); the tyrosyl radicals of prostaglandin H synthase (32), cytochrome c (33), and horse heart myoglobin (34); and the tyrosyl and thiyl radicals of cytochrome c peroxidase (35) and hemoglobin (36,37). GSH, a cysteinecontaining tripeptide, is ubiquitously distributed in nature and is the most abundant low molecular weight thiol in mammalian cells.…”

mentioning

confidence: 99%

“…In contrast, ESR spin trapping using DMPO as a spin trap detects the transient DMPO/protein radical adducts. Unfortunately, only a few protein radicals such as tyrosyl radicals of myoglobin (34) and thiyl radicals of human myoglobin (39,40), hemoglobin (36), and cytochrome c oxidase (35) have been trapped by DMPO and detected by ESR, and even in these cases, high concentrations of proteins had to be used. Therefore, in the detection of protein-derived radicals in biological systems, the sensitive immunochemical detection of protein radical-derived DMPO nitrone adducts is not only complementary to the ESR DMPO spintrapping technique, but a usually superior replacement (37).…”

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confidence: 99%

Protein Radical Formation during Lactoperoxidase-mediated Oxidation of the Suicide Substrate Glutathione

Guo

Detweiler

Mason

2004

Journal of Biological Chemistry

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A novel anti-5,5-dimethyl-1-pyrroline N-oxide (DMPO) polyclonal antiserum that specifically recognizes protein radical-derived DMPO nitrone adducts has been developed. In this study, we employed this new approach, which combines the specificity of spin trapping and the sensitivity of antigen-antibody interactions, to investigate protein radical formation from lactoperoxidase (LPO). When LPO reacted with GSH in the presence of DMPO, we detected an LPO radical-derived DMPO nitrone adduct using enzyme-linked immunosorbent assay and Western blotting. The formation of this nitrone adduct depended on the concentrations of GSH, LPO, and DMPO as well as pH values, and GSH could not be replaced by H 2 O 2 . The level of this nitrone adduct was decreased significantly by azide, catalase, ascorbate, iodide, thiocyanate, phenol, or nitrite. However, its formation was unaffected by chemical modification of free cysteine, tyrosine, and tryptophan residues on LPO. ESR spectra showed that a glutathiyl radical was formed from the LPO/GSH/DMPO system, but no protein radical adduct could be detected by ESR. Its formation was decreased by azide, catalase, ascorbate, iodide, or thiocyanate, whereas phenol or nitrite increased it. GSH caused marked changes in the spectrum of compound II of LPO, indicating that GSH binds to the heme of compound II, whereas phenol or nitrite prevented these changes and reduced compound II back to the native enzyme. GSH also dose-dependently inhibited the peroxidase activity of LPO as determined by measuring 2,2 -azino-bis(3-ethylbenzothiazoline-6-sulfonic acid) oxidation. Taken together, these results demonstrate that the GSH-dependent LPO radical formation is mediated by the glutathiyl radical, possibly via the reaction of the glutathiyl radical with the heme of compound II to form a heme-centered radical trapped by DMPO.

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In vivo thiyl free radical formation from hemoglobin following administration of hydroperoxides

Cited by 92 publications

References 26 publications

S‐Thiolation of human endothelial cell glyceraldehyde‐3‐phosphate dehydrogenase after hydrogen peroxide treatment

S‐Thiolation of human endothelial cell glyceraldehyde‐3‐phosphate dehydrogenase after hydrogen peroxide treatment

A central role for free heme in the pathogenesis of severe malaria: the missing link?

Protein Radical Formation during Lactoperoxidase-mediated Oxidation of the Suicide Substrate Glutathione

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