Early events in erythroid differentiation: accumulation of the acidic peroxidoxin (PRP/TSA/NKEF-B)

Rabilloud, Thierry; Berthier, R; Vincon, Mathilde; Ferbus, Didier; Goubin, Gérard; Lawrence, Jean‐Jacques

doi:10.1042/bj3120699

Cited by 62 publications

(40 citation statements)

References 33 publications

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“…Lower cysteine oxidation states have also been described for another peroxiredoxin (1-Cys peroxiredoxin), but here again, only in vitro (36). From our study, it appears that this form is encountered in vivo after even a moderate oxidative stress and is constitutively present in normal erythrocytes (37). It must be mentioned, however, that our analysis takes place under reducing conditions, so that lower oxidation states of peroxiredoxins (e.g.…”

Section: Discussionmentioning

confidence: 87%

Proteomics Analysis of Cellular Response to Oxidative Stress

Rabilloud¹,

Heller²,

Gasnier³

et al. 2002

Journal of Biological Chemistry

351

122

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The proteomics analysis reported here shows that a major cellular response to oxidative stress is the modification of several peroxiredoxins. An acidic form of the peroxiredoxins appeared to be systematically increased under oxidative stress conditions. Peroxiredoxins are enzymes catalyzing the destruction of peroxides. In doing so, a reactive cysteine in the peroxiredoxin active site is weakly oxidized (disulfide or sulfenic acid) by the destroyed peroxides. Cellular thiols (e.g. thioredoxin) are used to regenerate the peroxiredoxins to their active state. Tandem mass spectrometry was carried out to characterize the modified form of the protein produced in vivo by oxidative stress. The cysteine present in the active site was shown to be oxidized into cysteic acid, leading to an inactivated form of peroxiredoxin. This strongly suggested that peroxiredoxins behave as a dam upon oxidative stress, being both important peroxidedestroying enzymes and peroxide targets. Results obtained in a primary culture of Leydig cells challenged with tumor necrosis factor ␣ suggested that this oxidized/native balance of peroxiredoxin 2 may play an active role in resistance or susceptibility to tumor necrosis factor ␣-induced apoptosis.

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Section: Discussionmentioning

confidence: 87%

Proteomics Analysis of Cellular Response to Oxidative Stress

Rabilloud¹,

Heller²,

Gasnier³

et al. 2002

Journal of Biological Chemistry

351

122

View full text Add to dashboard Cite

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“…Prx2 counteracts the nuclear factor B pathway (57), which is required for DC maturation (60). It was therefore not surprising to find low levels of Prx2 in mature DCs and, more generally, low levels of Prx2 in the monocyte-DC lineage compared with other hematopoietic lineages (62).…”

Section: Discussionmentioning

confidence: 99%

High Expression of Antioxidant Proteins in Dendritic Cells

Rivollier

Perrin-Cocon

Luche

et al. 2006

Molecular & Cellular Proteomics

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Dendritic cells (DCs) display the unique ability to activate naive T cells and to initiate primary T cell responses revealed in DC-T cell alloreactions. DCs frequently operate under stress conditions. Oxidative stress enhances the production of inflammatory cytokines by DCs. We performed a proteomic analysis to see which major changes occur, at the protein expression level, during DC differentiation and maturation. Comparative two-dimensional gel analysis of the monocyte, immature DC, and mature DC stages was performed. Manganese superoxide dismutase (Mn-SOD) reached 0.7% of the gel-displayed proteins at the mature DC stage. This important amount of Mn-SOD is a primary antioxidant defense system against superoxide radicals, but its product, H 2 O 2 , is also deleterious for cells. Peroxiredoxin (Prx) enzymes play an important role in eliminating such peroxide. Prx1 expression level continuously increased during DC differentiation and maturation, whereas Prx6 continuously decreased, and Prx2 peaked at the immature DC stage. As a consequence, DCs were more resistant than monocytes to apoptosis induced by high amounts of oxidized low density lipoproteins containing toxic organic peroxides and hydrogen peroxide. Furthermore DC-stimulated T cells produced high levels of receptor activator of nuclear factor B ligand, a chemotactic and survival factor for monocytes and DCs. This study provides insights into the original ability of DCs to express very high levels of antioxidant enzymes such as Mn-SOD and Prx1, to detoxify oxidized low density lipoproteins, and to induce high levels of receptor activator of nuclear factor B ligand by the T cells they activate and further emphasizes the role that DCs

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“…Prx enzymes have been identified in association with various cellular functions apparently unrelated to peroxidase activity. Several lines of evidence support the concept that peroxiredoxins can influence cell proliferation and differentiation, immunological defence, receptor signalling and apoptosis [10,23,26,27,28,29]. This is reflected by the numerous synonyms used.…”

mentioning

confidence: 89%

“…It is also named thiol-specific antioxidant (TSA) [38,39], protector protein (PRP) [11,26], human natural killer cell-enhancing factor-B (NKEF-B) [33,41,40], calpromotin [19,42,43] and torin [44]. Prx II is important in erythroid cell differentiation [11,26] and protects red blood cell membranes from peroxidation [20,45].…”

mentioning

confidence: 99%

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

et al. 2002

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Aims/hypothesis. Insulin-producing beta cells are destroyed by oxidative and nitrosative stress during the pathogenesis of Type I (insulin-dependent) diabetes mellitus. These cells are more sensitive than others due to their deficiency of well known antioxidant enzymes like superoxide dismutase, glutathione peroxidase and catalase. However the peroxiredoxins discovered in the past decade form a large family of highly conserved thioredoxin-dependent peroxide reductases, which are present in most tissues. We investigated whether peroxiredoxins I and II are present in pancreatic beta cells and if they are inducible by oxidative and nitrosative stress. Methods. To detect these enzymes in insulin-producing beta cells we used semiquantitative RT-PCR, western blots and immunohistochemistry. The expression of peroxiredoxins I and II was analysed after treatment with cytokines, hydrogen peroxide, alloxan or streptozotocin in the rat insulinoma cells INS-1 using RT-PCR and western blots. Results. We show that peroxiredoxins I and II are present in the cytoplasm of pancreatic islet cells as well as in insulinoma cell lines βTC6-F7 and INS-1. Peroxiredoxins I and II were up-regulated by all stress agents used. Conclusion/interpretation. Beta cells, undersupplied with well characterized antioxidant enzymes, possess an additional antioxidant system which is inducible by oxidative as well as nitrosative stress. [Diabetologia (2002) 45:867-876]

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Early events in erythroid differentiation: accumulation of the acidic peroxidoxin (PRP/TSA/NKEF-B)

Cited by 62 publications

References 33 publications

Proteomics Analysis of Cellular Response to Oxidative Stress

Proteomics Analysis of Cellular Response to Oxidative Stress

High Expression of Antioxidant Proteins in Dendritic Cells

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

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