Protein S-Thiolation and Regulation of Microsomal Glutathione Transferase Activity by the Glutathione Redox Couple

Dafré, Alcir Luiz; Sies, Helmut; Akerboom, Theodorus P.M.

doi:10.1006/abbi.1996.0344

Cited by 63 publications

(33 citation statements)

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“…S-glutathionylation can inactivate the catalytic function of many proteins such as transcription factors NF-κB and NF-1 [59,60], protein tyrosine phosphatase 1B (PTP-1B) [61,62], protein kinase C-α [63], etc. However, the activities of a number of other proteins, such as HIV-1 protease, glutathione S-transferase, and Ras, are enhanced by Sglutathionylation [64][65][66]. In certain cases, the altered protein function due to Sglutathionylation has been shown to play a role in regulation of cell physiology.…”

Section: Discussionmentioning

confidence: 99%

Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia

Xiong

et al. 2007

Free Radical Biology and Medicine

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To understand the physiological function of glutaredoxin, a thiotransferase catalyzing the reduction of mixed disulfides of protein and glutathione (protein-SSG), we generated a line of knockout mice deficient in the cytosolic glutaredoxin 1 (Grx1). To our surprise, mice deficient in Grx1 were not more susceptible to acute oxidative insults in models of heart and lung injury induced by ischemia/ reperfusion and hyperoxia, respectively; suggesting that changes in S-glutathionylation status of cytosolic proteins are not the major cause of such tissue injury. On the other hand, mouse embryonic fibroblasts (MEFs) isolated from Grx1-deficient mice displayed an increased vulnerability to diquat and paraquat, but they were not more susceptible to cell death induced by hydrogen peroxide (H 2 O 2 ) and diamide. A deficiency in Grx1 also sensitized MEFs to protein S-glutathionylation in response to H 2 O 2 treatment and retarded deglatuthionylation of the S-glutathionylated proteins, especially evident for an unspecified protein of approximately 44 kDa. Additional experiments showed that MEFs lacking Grx1 were more tolerant to apoptosis induced by tumor necrosis factor α plus actinomycin D. These findings suggest that different oxidants may damage the cells via distinct mechanisms in which Grx1-dependent de-glutathionylation may or may not be protective, and Grx1 may exert its function on specific target proteins.

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Section: Discussionmentioning

confidence: 99%

Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia

Xiong

et al. 2007

Free Radical Biology and Medicine

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“…It was observed that a seleno-organic compound reacts very efficiently with peroxynitrite Sies & Masumoto, 1997) and that seleno-organic compounds, such as selenomethionine or selenocystine, protect against peroxynitrite-induced DNA strand breaks (Roussyn, Briviba, Masumoto & Sies, 1996) or against nitration reactions (Briviba, Roussyn, Sharov & Sies, 1996 Another topic addressed is the modification of proteins by mixed disulphide formation with glutathione, called glutathiolation (see Thomas & Sies, 1991). Dafre, Sies & Akerboom (1996) examined the properties of protein S-thiolation and regulation of microsomal glutathione transferase activity by the glutathione redox couple.…”

Section: Recent Topics Of Interestmentioning

confidence: 99%

Oxidative stress: oxidants and antioxidants

Sies¹

1997

Experimental Physiology

3,284

2,188

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Itistitlitfi /-Ph siol/ugi schie Chie,nie 1, Hei/i(-ItiiH eliie-t-L iIiVe-sit(it Doisscldo,!, Postf0chi 101007, 1)-40001 1)isse)ld)o1f Gef cermainy (NlANNS C RIPT RECEIN'ED 2X 0('TT()BER 19)6, ACCEPTEL) 2' NONOENIBER 1996) SUMMARYAn imbalanice between oxidants and antioxidaints in favour of the oxidants, potentially leading to damage, is termed 'oxidative stress'. Oxidants are formed as a normal product of aerobic metabolism but can be produced at elevated rates under pathophysiological conditions. Antioxidant defense involves several strategies, both enzymatic and non-enzymatic. In the lipid phase, tocopherols and carotenes as well as oxy-carotenoids are of' interest, (as are vitamin A and ubiquinols. In the aqueous phase, there aI-C ascorbate, glutathione and other com-pounds. In addition to the cytosol, the nuclear and mitochondrial matrices and extracellular fluids are protected. Overall, these low molecular miass antioxidant molecules .add significantly to the defense provided by the enzym-es superoxide dismuta.se, catalcase and glutathione peroxidases. INTRO D) U CT IONAn imbalance betweeni oxidants and antioxida.nts in favour of the oxxidants, potentially leading to damage, is termed 'oxidative stress' (Sies, 1985(Sies, , 1986(Sies, , 1991 (see Sies, 1993(see Sies, , 1995

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“…Early data demonstrating protein S-glutathiolation were largely derived from the exposure of cells to toxic levels of oxidants or activation of an inflammatory response from neutrophils (141), macrophages (961), and monocytes (764). Such studies readily demonstrated a number of S-glutathiolated proteins that spanned a broad range of cellular functions including metabolism (glyceraldehyde-3-phosphate dehydrogenase and creatine kinase) (164,764), the cytoskeleton (actin) (141), and antioxidant protection (SOD and glutathione transferase) (180,812) to name a few. For a more complete list of S-glutathiolated proteins, readers are directed to an excellent review (490).…”

Section: Targets For Rns In Cellular Signalingmentioning

confidence: 99%

Role of Oxidative Modifications in Atherosclerosis

Stocker¹,

Keaney²

2004

Physiological Reviews

2,248

1,756

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This review focuses on the role of oxidative processes in atherosclerosis and its resultant cardiovascular events. There is now a consensus that atherosclerosis represents a state of heightened oxidative stress characterized by lipid and protein oxidation in the vascular wall. The oxidative modification hypothesis of atherosclerosis predicts that low-density lipoprotein (LDL) oxidation is an early event in atherosclerosis and that oxidized LDL contributes to atherogenesis. In support of this hypothesis, oxidized LDL can support foam cell formation in vitro, the lipid in human lesions is substantially oxidized, there is evidence for the presence of oxidized LDL in vivo, oxidized LDL has a number of potentially proatherogenic activities, and several structurally unrelated antioxidants inhibit atherosclerosis in animals. An emerging consensus also underscores the importance in vascular disease of oxidative events in addition to LDL oxidation. These include the production of reactive oxygen and nitrogen species by vascular cells, as well as oxidative modifications contributing to important clinical manifestations of coronary artery disease such as endothelial dysfunction and plaque disruption. Despite these abundant data however, fundamental problems remain with implicating oxidative modification as a (requisite) pathophysiologically important cause for atherosclerosis. These include the poor performance of antioxidant strategies in limiting either atherosclerosis or cardiovascular events from atherosclerosis, and observations in animals that suggest dissociation between atherosclerosis and lipoprotein oxidation. Indeed, it remains to be established that oxidative events are a cause rather than an injurious response to atherogenesis. In this context, inflammation needs to be considered as a primary process of atherosclerosis, and oxidative stress as a secondary event. To address this issue, we have proposed an “oxidative response to inflammation” model as a means of reconciling the response-to-injury and oxidative modification hypotheses of atherosclerosis.

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Protein S-Thiolation and Regulation of Microsomal Glutathione Transferase Activity by the Glutathione Redox Couple

Cited by 63 publications

References 0 publications

Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia

Targeted disruption of the glutaredoxin 1 gene does not sensitize adult mice to tissue injury induced by ischemia/reperfusion and hyperoxia

Oxidative stress: oxidants and antioxidants

Role of Oxidative Modifications in Atherosclerosis

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