Role of Peroxiredoxins in Regulating Intracellular Hydrogen Peroxide and Hydrogen Peroxide-induced Apoptosis in Thyroid Cells

Kim, Ho; Lee, Tae‐Hoon; Park, Eun Shin; Suh, Jae Mi; Park, Soo Jung; Chung, Hyo Kyun; Kwon, O‐Yu; Kim, Young Kun; Ro, Heung Kyu; Shong, Minho

doi:10.1074/jbc.275.24.18266

Cited by 197 publications

(130 citation statements)

References 56 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%

“…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: 87%

“…Prx II is important in erythroid cell differentiation [11,26] and protects red blood cell membranes from peroxidation [20,45]. It also regulates signal transduction pathways that directly relate to apoptotic cell death [23,27,28,29,46]. Prx II is thought to protect neuronal cells against destruction by hypoxia and ischaemia [11,47] and tumour cells against X-ray treatment and chemotherapy [48].…”

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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%

mentioning

confidence: 87%

mentioning

confidence: 99%

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Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

et al. 2002

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“…15,16 The 1-Cys PRDX contains only the peroxidatic cysteine, and not a resolving cysteine. 16 Based on the presence of one conserved redox-active cysteine in the NH2 terminus of PRDX6 (C-47), previously known as antioxidant protein 2 (AOP2) 2,3,[17][18][19][20] in contrast to two conserved cysteine residues in the rest of the PRDX family, the Mouse Genomic Nomenclature Committee (MGNC) and Human Gene Nomenclature Committee (HGNC) put this molecule under subgroup 6, now known as PRDX6. 12 H 2 O 2 , a source of oxidative stress, has gained attention recently due to its role as a cellular signaling factor for various cytokines and growth factors, including platelet-derived growth factor (PDGF), insulin-like growth factor (IGF), endothelial-derived growth factor (EGF), tumor necrosis factor a (TNF-a), and transforming growth factor b (TGFb).…”

Section: Introductionmentioning

confidence: 99%

Impaired homeostasis and phenotypic abnormalities in Prdx6−/−mice lens epithelial cells by reactive oxygen species: increased expression and activation of TGFβ

et al. 2005

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PRDX6, a member of the peroxiredoxins (PRDXs) family, is a key player in the removal of reactive oxygen species (ROS). Using targeted inactivation of the Prdx6 gene, we present evidence that the corresponding protein offsets the deleterious effects of ROS on lens epithelial cells (LECs) and regulates gene expression by limiting its levels. PRDX6-depleted LECs displayed phenotypic alterations and elevated a-smooth muscle actin and big-h3 expression (markers for cataractogenesis), indistinguishable from transforming growth factor b (TGFb)-induced changes. Biochemical assays disclosed enhanced levels of ROS, as well as high expression and activation of TGFb1 in Prdx6 À/À LECs. A CAT assay revealed transcriptional repression of lens epithelium-derived growth factor (LEDGF), HSP27, and aB-crystallin promoter activities in these cells. A gel mobility shift assay demonstrated the attenuation of LEDGF binding to heat shock or stress response elements present in these genes. A supply of PRDX6 toPrdx6 À/À LECs reversed these changes. Based on the above data, we propose a rheostat role for PRDX6 in regulating gene expression by controlling the ROS level to maintain cellular homeostasis.

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“…Previously, overexpression of both Prx I and Prx II has been shown to render cells resistant to H 2 O 2 -induced apoptosis. 24,35,36 Our finding of a specific involvement of Prx I in a pathway counteracting the toxic activity of H 2 O 2 is, to our best knowledge, the first report on a specific function of Prx I demonstrated in a loss of function experiment. Why do amino-acid oxidases of Aplysia exhibit tumor specific toxicity?…”

Section: Discussionmentioning

confidence: 76%

Hydrogen peroxide produced by Aplysia ink toxin kills tumor cells independent of apoptosis via peroxiredoxin I sensitive pathways

et al. 2004

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Marine snails of the genus Aplysia possess numerous bioactive substances. We have purified a 60 kDa protein, APIT (Aplysia punctata ink toxin), from the defensive ink of A. punctata that triggers cell death with profound tumor specificity. Tumor cell death induced by APIT is independent of apoptosis but is characterized by the rapid loss of metabolic activity, membrane permeabilization, and shrinkage of nuclei. Proteome analysis of APIT-treated tumor cells indicated a modification of peroxiredoxin I, a cytoplasmic peroxidase involved in the detoxification of peroxides. Interestingly, knockdown of peroxiredoxin I expression by RNA interference sensitized cells for APIT-induced cell death. APIT induced the death of tumor cells via the enzymatic production of H 2 O 2 and catalase completely blocked APITs' activity. Our data suggest that H 2 O 2 induced stress and the modulation of peroxiredoxins might be a promising approach for tumor therapy.

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Role of Peroxiredoxins in Regulating Intracellular Hydrogen Peroxide and Hydrogen Peroxide-induced Apoptosis in Thyroid Cells

Abstract: The abbreviations used are: Prx, Peroxiredoxin; MMI, methimazole; TUNEL, terminal deoxynucleotidyl transferase deoxyuridine triphosphate-biotin nick end-labeling; TSH, thyrotropin; PCR, polymerase chain reaction.

Cited by 197 publications

References 56 publications

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

Oxidative and nitrosative stress induces peroxiredoxins in pancreatic beta cells

Impaired homeostasis and phenotypic abnormalities in Prdx6−/−mice lens epithelial cells by reactive oxygen species: increased expression and activation of TGFβ

Hydrogen peroxide produced by Aplysia ink toxin kills tumor cells independent of apoptosis via peroxiredoxin I sensitive pathways

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