Thioredoxin and glutaredoxin system proteins—immunolocalization in the rat central nervous system

Aon-Bertolino, Maria Laura; Romero, Juan Ignacio; Galeano, Pablo; Holubiec, Mariana; Badorrey, Maria Sol; Saraceno, Gustavo Ezequiel; Hanschmann, Eva-Maria; Lillig, Christopher Horst; Capani, Francisco

doi:10.1016/j.bbagen.2010.06.011

Cited by 69 publications

(81 citation statements)

References 64 publications

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“…Moreover, neuronal cells bear relatively weak antioxidant defense due to reduced expression of antioxidants with high levels of phospholipids, which are highly sensitive to oxidative modification (18,50). The protective activity of Prdx6 has been documented in neuronal cells (3,29). Most of the antioxidant proteins including Prdx6 reside in cytosol to remove ROS enzymatically.…”

Section: Discussionmentioning

confidence: 99%

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Delivery of a protein transduction domain-mediated Prdx6 protein ameliorates oxidative stress-induced injury in human and mouse neuronal cells

Singh

Chhunchha

Fatma

et al. 2016

American Journal of Physiology-Cell Physiology

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Section: Discussionmentioning

confidence: 99%

“…Prdxs are distributed in the normal mammalian brain (29). Aon-Bertolino et al (3) reported a relatively intense Prdx6 staining in the hippocampus of the rat brain (34). These qualities make Prdx6 an ideal molecule for therapeutic use.…”

mentioning

confidence: 99%

Delivery of a protein transduction domain-mediated Prdx6 protein ameliorates oxidative stress-induced injury in human and mouse neuronal cells

Singh

Chhunchha

Fatma

et al. 2016

American Journal of Physiology-Cell Physiology

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“…This is not to imply that all tissues respond both qualitatively and quantitatively in a similar way to the same exercise stimulus. In fact, the expression of many redox proteins has proved to be highly cell, tissue, organ and species specific (Aon-Bertolino et al, 2011;Dammeyer and Arner, 2011;Godoy et al, 2011 the literature (Liu et al, 2000;Dyson et al, 2011). Nevertheless, it is evident that metabolic perturbations after virtually every type of exercise lead to alterations in redox homeostasis.…”

Section: Effects Of Very Short Duration Exercise On Redox Homeostasismentioning

confidence: 99%

Redox biology of exercise: an integrative and comparative consideration of some overlooked issues

Nikolaidis

Kyparos

Spanou

et al. 2012

Journal of Experimental Biology

122

138

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SummaryThe central aim of this review is to address the highly multidisciplinary topic of redox biology as related to exercise using an integrative and comparative approach rather than focusing on blood, skeletal muscle or humans. An attempt is also made to redefine ʻoxidative stressʼ as well as to introduce the term ʻalterations in redox homeostasisʼ to describe changes in redox homeostasis indicating oxidative stress, reductive stress or both. The literature analysis shows that the effects of non-muscledamaging exercise and muscle-damaging exercise on redox homeostasis are completely different. Non-muscle-damaging exercise induces alterations in redox homeostasis that last a few hours post exercise, whereas muscle-damaging exercise causes alterations in redox homeostasis that may persist for and/or appear several days post exercise. Both exhaustive maximal exercise lasting only 30s and isometric exercise lasting 1-3min (the latter activating in addition a small muscle mass) induce systemic oxidative stress. With the necessary modifications, exercise is capable of inducing redox homeostasis alterations in all fluids, cells, tissues and organs studied so far, irrespective of strains and species. More importantly, ʻexercise-induced oxidative stressʼ is not an ʻoddityʼ associated with a particular type of exercise, tissue or species. Rather, oxidative stress constitutes a ubiquitous fundamental biological response to the alteration of redox homeostasis imposed by exercise. The hormesis concept could provide an interpretative framework to reconcile differences that emerge among studies in the field of exercise redox biology. Integrative and comparative approaches can help determine the interactions of key redox responses at multiple levels of biological organization.Key words: antioxidant, biomarker, eccentric, free radical, training. THE JOURNAL OF EXPERIMENTAL BIOLOGY 1616The ʻgoodʼ (antioxidants), the ʻbadʼ (reactive species) and the ʻuglyʼ (oxidative stress) 1 The distinction drawn in the section heading is schematically used to parody the popular manichaeistic view that antioxidants are considered 'useful' entities, reactive species are considered 'harmful' entities and oxidative stress is considered a 'negative' state. Certainly, the reality is much more complicated and antioxidants, reactive species and oxidative stress can serve both useful and detrimental roles, which are dependent on the biological context (within an organism), which in turn are greatly dependent on the environmental context (outside an organism). AntioxidantsAdmittedly, to define the term 'antioxidant' is a difficult task. In this paper, antioxidant is defined as any mechanism, structure and/or substance that delays, prevents or removes oxidative modifications to a target molecule (Halliwell and Gutteridge, 2007;Pamplona and Costantini, 2011). Antioxidants can be complex molecules such as the superoxide dismutases and peroxiredoxins, or simpler ones such as uric acid and glutathione (Gutteridge and Halliwell, 2010). They can be broa...

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“…However, the role of GRX1 in other experimental models of PD has not been studied in detail. Recent studies have demonstrated that GRX1 is expressed at lower levels in the substantia nigra and striatum compared to the hippocampus and cerebral cortex (3,7). Human dopaminergic SK-N-SH cells express very low levels of GRX1, which, as shown here, can be increased by stable expression or adenoviral gene delivery (Figs.…”

Section: Grx1 Protects Against Experimental Pdmentioning

confidence: 86%

Glutaredoxin 1 Protects Dopaminergic Cells by Increased Protein Glutathionylation in Experimental Parkinson's Disease

Rodríguez-Rocha

Garcia

Zavala-Flores

et al. 2012

Antioxidants & Redox Signaling

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Aims: Chronic exposure to environmental toxicants, such as paraquat, has been suggested as a risk factor for Parkinson's disease (PD). Although dopaminergic cell death in PD is associated with oxidative damage, the molecular mechanisms involved remain elusive. Glutaredoxins (GRXs) utilize the reducing power of glutathione to modulate redox-dependent signaling pathways by protein glutathionylation. We aimed to determine the role of GRX1 and protein glutathionylation in dopaminergic cell death. Results: In dopaminergic cells, toxicity induced by paraquat or 6-hydroxydopamine (6-OHDA) was inhibited by GRX1 overexpression, while its knockdown sensitized cells to paraquat-induced cell death. Dopaminergic cell death was paralleled by protein deglutathionylation, and this was reversed by GRX1. Mass spectrometry analysis of immunoprecipitated glutathionylated proteins identified the actin binding flightless-1 homolog protein (FLI-I) and the RalBP1-associated Eps domain-containing protein 2 (REPS2/POB1) as targets of glutathionylation in dopaminergic cells. Paraquat induced the degradation of FLI-I and REPS2 proteins, which corresponded with the activation of caspase 3 and cell death progression. GRX1 overexpression reduced both the degradation and deglutathionylation of FLI-I and REPS2, while stable overexpression of REPS2 reduced paraquat toxicity. A decrease in glutathionylated proteins and REPS2 levels was also observed in the substantia nigra of mice treated with paraquat. Innovation: We have identified novel protein targets of glutathionylation in dopaminergic cells and demonstrated the protective role of GRX1-mediated protein glutathionylation against paraquat-induced toxicity. Conclusions: These results demonstrate a protective role for GRX1 and increased protein glutathionylation in dopaminergic cell death induced by paraquat, and identify a novel protective role for REPS2.

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Thioredoxin and glutaredoxin system proteins—immunolocalization in the rat central nervous system

Cited by 69 publications

References 64 publications

Delivery of a protein transduction domain-mediated Prdx6 protein ameliorates oxidative stress-induced injury in human and mouse neuronal cells

Delivery of a protein transduction domain-mediated Prdx6 protein ameliorates oxidative stress-induced injury in human and mouse neuronal cells

Redox biology of exercise: an integrative and comparative consideration of some overlooked issues

Glutaredoxin 1 Protects Dopaminergic Cells by Increased Protein Glutathionylation in Experimental Parkinson's Disease

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