Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III; characterization of S-thiolation and dethiolation reactions

Chai, Yoke Chin; Jung, Chul-Ho; Lii, Chong‐Kuei; Ashraf, S. Salman; Hendrich, Suzanne; Wolf, Bernhard; Sies, Helmut; Thomas, James A.

doi:10.1016/0003-9861(91)90295-t

Cited by 110 publications

(74 citation statements)

References 28 publications

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“…By comparison, carbonic anhydrase III is a member of zinc metallo-enzymes and plays an important role in maintaining muscle carbohydrate metabolism as well as the reversible hydration of carbon dioxide (9). Recent studies indicate that, by interacting directly with glutathione, carbonic anyhdrase III participate in the cellular defense against ROS (8). Our current results indicate that both creatine kinase and carbonic anyhdrase III are modified by HNE in control diaphragms but more so in septic rat diaphragms (Figs.…”

Section: Discussionsupporting

confidence: 56%

Modifications of proteins by 4-hydroxy-2-nonenal in the ventilatory muscles of rats

Hussain¹,

Matar²,

Barreiro³

et al. 2006

American Journal of Physiology-Lung Cellular and Molecular Phys

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Although 4-hydroxy-2-nonenal (HNE, a product of lipid peroxidation) is a major cause of oxidative damage inside skeletal muscles, the exact proteins modified by HNE are unknown. We used two-dimensional electrophoresis, immunoblotting, and mass spectrometry to identify selective proteins targeted by HNE inside the diaphragm of rats under two conditions: severe sepsis [induced by E. coli lipopolysaccharides (LPS)] and during strenuous muscle contractions elicited by severe inspiratory resistive loading (IRL). Diaphragm HNE-protein adduct formation (detected with a polyclonal antibody) increased significantly after 1 and 3 h of LPS injection with a return to baseline values thereafter. Similarly, HNE-protein adduct formation inside the diaphragm rose significantly after 6 but not 3 h of IRL. Mass spectrometry analysis of HNE-modified proteins revealed enolase 3b, aldolase and triosephosphate isomerase 1, creatine kinase, carbonic anyhdrase III, aconitase 2, dihydrolipoamide dehydrogenase, and electron transfer flavoprotein-β. Measurements of in vitro enolase activity in the presence of pure HNE revealed that HNE significantly attenuated enolase activity in a dose-dependent fashion, suggesting that HNE-derived modifications have inhibitory effects on enzyme activity. We conclude that lipid peroxidation products may inhibit muscle contractile performance through selective targeting of enzymes involved in glycolysis, energy production as well as CO2 hydration.

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Section: Discussionsupporting

confidence: 56%

Modifications of proteins by 4-hydroxy-2-nonenal in the ventilatory muscles of rats

Hussain¹,

Matar²,

Barreiro³

et al. 2006

American Journal of Physiology-Lung Cellular and Molecular Phys

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“…thiols and sulfhydryl groups of certain cytosolic proteins (S-thiolation). Mixed disulfide formation with GSH (i.e., S-glutathiolation) was found to stimulate certain enzymes and to inhibit others (77)(78)(79)(80). The details of the chemical modification p59 fyn and GSSG remain to be analyzed but may involve the motif CPxxxxxxMxxCW (see Ref.…”

Section: Discussionmentioning

confidence: 99%

Enhancement of T Cell Receptor Signaling by a Mild Oxidative Shift in the Intracellular Thiol Pool

Hehner

Breitkreutz

Shubinsky

et al. 2000

The Journal of Immunology

148

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Exposure of T cells to the macrophage products hydrogen peroxide (HP) or l-lactate (LAC) was previously shown to enhance IL-2 production and to modulate glutathione (GSH) status. We now found that 50 μM HP and 30 mM LAC enhanced strongly the transcription from the IL-2 promoter in Jurkat T cells after stimulation with anti-CD28 together with or without anti-CD3 but not with anti-CD3 Abs alone. Therefore, we used anti-CD3 plus anti-CD28-stimulated cells to investigate the effect of the GSH reductase inhibitor 1,3-bis(2-chloroethyl)-1-nitrosourea (BCNU) on the signal cascade. BCNU enhanced the transcription to a similar extent as HP or LAC. Lowering the intracellular GSH/GSH disulfide ratio by BCNU, HP, or NO resulted in all cases in the fulminant enhancement of Jun-N-terminal kinase and p38 mitogen-activated protein kinase but not extracellular signal-regulated kinase 1/2. Jun-N-terminal kinase and NF-κB activation was enhanced through pathways involving Rac, Vav1, PKCΘ, p56lck, p59fyn, and IκB kinases. In a cell-free system, the autophosphorylation of rFyn was stimulated by GSH disulfide but not by HP. These findings suggest that the oxidation of the cellular thiol pool may play a role as an amplifying mechanism for TCR/CD3 signals in immune responses.

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“…Modification of cysteine residues with GSH has been reported for many enzymes such as carbonic anhydrase [13] and fatty acid synthetase [14]. Such glutathionylation usually decreases enzyme activities but enhances them in some cases, for example with fructose 1,6-bisphosphatase [48,49].…”

Section: Discussionmentioning

confidence: 99%

“…Modification of cysteine residues with GSH has been reported for many enzymes, such as carbonic anhydrase [13] and fatty acid synthetase [14], and the amounts of glutathionylated forms may be increased in response Abbreviations used : HHR, Hirosaki hairless rat ; SD, Sprague-Dawley ; GST, glutathione transferase ; NEM, N-ethylmaleimide ; CDNB, 1-chloro-2,4-dinitrobenzene ; DDPM, N- (4-dimethylamino-3,5-dinitrophenyl)maleimide ; DPCC, diphenylcarbamyl chloride ; TFA, trifluoroacetic acid ; MALDI-TOF, matrix-assisted laser desorption-ionization-time-of-flight ; DTT, dithiothreitol, RT-PCR, reverse transcriptase PCR. 1 To whom correspondence should be addressed (e-mail tsuchida!cc.hirosaki-u.ac.jp).…”

Section: Introductionmentioning

confidence: 99%

Polymorphism of the glutathione transferase subunit 3 in Sprague–Dawley rats involves a reactive cysteine residue

Kumano

Kimura

Hayakari

et al. 2000

Biochemical Journal

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Comparison of Hirosaki hairless rat (HHR) and SpragueDawley (SD) rat liver glutathione transferase (GST) subunits by HPLC revealed differences in subunit 3 ; a new peak was detected in HHR GSTs and this was tentatively named X. By chromatofocusing, the HHR GST form composed of peak X and SD rat GST 3-3 were eluted at pH 8.8 and 9.1 respectively. The former was more sensitive to the SH reagent N-ethylmaleimide (NEM) than the latter. GSSG treatment of peak X resulted in a shift of retention time (peak Y) by HPLC analysis. However, such conversion was not observed for the SD rat GST 3-3 following GSSG or dithiothreitol (DTT) treatment. Peak Y exhibited m\z values of 26091.9 and 26125.4 by matrix-assisted laser-desorption ionization-time-of-flight MS, higher than those of peak X by 304-307, equivalent to the molecular-mass value of GSH. On treatment with DTT, peak Y was converted into peak X, with release of a substance with HPLC-characteristics of GSH. This substance was confirmed to be GSH by liquid chromatography\ MS. These results thus indicated peak Y to be a glutathionylated form of peak X. Quantification revealed the release of

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Identification of an abundant S-thiolated rat liver protein as carbonic anhydrase III; characterization of S-thiolation and dethiolation reactions

Cited by 110 publications

References 28 publications

Modifications of proteins by 4-hydroxy-2-nonenal in the ventilatory muscles of rats

Modifications of proteins by 4-hydroxy-2-nonenal in the ventilatory muscles of rats

Enhancement of T Cell Receptor Signaling by a Mild Oxidative Shift in the Intracellular Thiol Pool

Polymorphism of the glutathione transferase subunit 3 in Sprague–Dawley rats involves a reactive cysteine residue

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