The <i>pag</i> gene product, a physiological inhibitor of c‐<i>abl</i> tyrosine kinase, is overexpressed in cells entering S phase and by contact with agents inducing oxidative stress

Prospéri, Marie-Thérèse; Ferbus, Didier; Rouillard, Dany; Goubin, Gérard

doi:10.1016/s0014-5793(98)00057-x

Cited by 48 publications

(30 citation statements)

References 20 publications

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“…3, 4, 5, 6). The different regulation of peroxiredoxins on mRNA and protein level is thought to be dependent on the stress agent and cell type [29,58].…”

Section: Discussionmentioning

confidence: 99%

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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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“…3, 4, 5, 6). The different regulation of peroxiredoxins on mRNA and protein level is thought to be dependent on the stress agent and cell type [29,58].…”

Section: Discussionmentioning

confidence: 99%

“…An up-regulation of peroxiredoxins in response to hydrogen peroxide has been observed in the mouse macrophage cell line RAW [58], and in mouse peritoneal macrophages [30], but not in endothelial cell lines ECV304 [61] and HUVEC [62]. This strongly suggests that induction of peroxiredoxins by stress inducing agents is dependent on cell type.…”

Section: Discussionmentioning

confidence: 99%

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

et al. 2002

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“…Structure details of several Prx family members have been worked out through X-ray crystallography (Choi et al, 1998;Hirotsu et al, 1999;Schroder et al, 2000). The fact that amino acid sequences and antioxidative functions of Prxs are highly conserved through evolution signifies the importance of these enzymes in cell survival (Shau and Kim, 1994;Iwahara et al, 1995;Prospaeri et al, 1998). Park et al recently showed that levels of human Prx-II were associated with resistance of cells to radiation therapy and that Prx-II antisense served as a radiosensitizer (Park et al, 2000).…”

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confidence: 99%

“…Prx-I shares high sequence homology with Prx-II, with similar antioxidative and antiapoptotic functions (for review see Butterfield et al, 1999). However, some activities observed in Prx-I, such as cAbl kinase inhibition (Prospaeri et al, 1998), heme binding (Nakaso et al, 2000), and natural killer enhancement (Sauri et al, 1996), have not been reported for Prx-II. In this study, we sought to determine whether Prx-I could also influence the radiosensitivity of cancer cell lines.…”

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confidence: 99%

Induction of radioprotective peroxiredoxin‐I by ionizing irradiation

Chen

McBride

Iwamoto

et al. 2002

J of Neuroscience Research

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Results of this study indicate a radioprotective effect of peroxiredoxin-I. Peroxiredoxin-I is an antioxidant that scavenges hydroperoxides, whereas reactive oxygen species are the main mediators of ionizing radiation toxicity. We hypothesized that peroxiredoxin-I might be induced by cellular exposure to radiation and act to protect them against its cytotoxic effects. Western blot and Northern blot analyses were used to assess peroxiredoxin-I protein and mRNA expression. Rat C6 glioma cells were engineered to overexpress sense or antisense human peroxiredoxin-I using retroviral vectors. Clonogenic cell survival was used to assess radiosensitivities of the engineered cells. Ionizing radiation induced peroxiredoxin-I protein and mRNA expression in human HT29 colon cancer and rat C6 glioma cells in a dose-and time-dependent manner over a 24 hr period. To determine the effect of peroxiredoxin-I on radiation responses, C6 glioma cells were engineered to overexpress sense or antisense human peroxiredoxin-I. In clonogenic assays, cells overexpressing peroxiredoxin-I were more radioresistant. Cells transduced with antisense peroxiredoxin-I were marginally more sensitive to radiation toxicity. Irradiation can induce peroxiredoxin-I expression, and the increased peroxiredoxin-I may protect cells from further radiation damage. These results suggest that protection by peroxiredoxin-I may play an important role in the survival of glioma and colon cancer cells in patients undergoing radiation therapy.

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“…PRDX 1 belongs to a family of anti-oxidative proteins and is known to be overexpressed when cells are exposed to proliferative signals or oxidative stress (Prosperi et al, 1998). Transgelin-2, a protein of the calponin family, is the second protein whose expression level increased upon differentiation of hNSCs.…”

Section: Human Neuronal Stem Cellsmentioning

confidence: 99%

Mass spectrometry based proteomic analysis of human stem cells: a brief review

Choi

An²,

Kim³

et al. 2007

Exp Mol Med

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Stem cells can give rise to various cell types and are capable of regenerating themselves over multiple cell divisions. Pluripotency and self-renewal potential of stem cells have drawn vast interest from different disciplines, with studies on the molecular properties of stem cells being one example. Current investigations on the molecular basis of stem cells pluripotency and self-renewal entail traditional techniques from chemistry and molecular biology. In this mini review, we discuss progress in stem cell research that employs proteomics approaches. Specifically, we focus on studies on human stem cells from proteomics perspective. To our best knowledge, only the following types of human stem cells have been examined via proteomics analysis: human neuronal stem cells, human mesenchymal stem cells, and human embryonic stem cells. Protein expression serves as biomarkers of stem cells and identification and expression level of such biomarkers are usually determined using two-dimensional electrophoresis coupled mass spectrometry or non-gel based mass spectrometry.

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The pag gene product, a physiological inhibitor of c‐abl tyrosine kinase, is overexpressed in cells entering S phase and by contact with agents inducing oxidative stress

Cited by 48 publications

References 20 publications

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

Induction of radioprotective peroxiredoxin‐I by ionizing irradiation

Mass spectrometry based proteomic analysis of human stem cells: a brief review

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