NADPH-dependent H2O2 generation and peroxidase activity in thyroid particular fraction

Virion, Alain; Michot, Jean–Luc; Dème, Danielle; Kaniewski, Jacques; Pommier, Jacques

doi:10.1016/0303-7207(84)90088-1

Cited by 64 publications

(30 citation statements)

References 27 publications

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“…H 2 O 2 generation by thyrocytes was described by the early 1980s (88,921), and an NADPH oxidase activity was quickly suggested to be the underlying mechanism (605). The discovery of the DUOX enzymes (see above) provided the molecular basis for the thyrocyte ROS generation.…”

Section: Thyroidmentioning

confidence: 99%

The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology

Bedard¹,

Krause²

2007

Physiological Reviews

5,868

117

5,778

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For a long time, superoxide generation by an NADPH oxidase was considered as an oddity only found in professional phagocytes. Over the last years, six homologs of the cytochrome subunit of the phagocyte NADPH oxidase were found: NOX1, NOX3, NOX4, NOX5, DUOX1, and DUOX2. Together with the phagocyte NADPH oxidase itself (NOX2/gp91phox), the homologs are now referred to as the NOX family of NADPH oxidases. These enzymes share the capacity to transport electrons across the plasma membrane and to generate superoxide and other downstream reactive oxygen species (ROS). Activation mechanisms and tissue distribution of the different members of the family are markedly different. The physiological functions of NOX family enzymes include host defense, posttranlational processing of proteins, cellular signaling, regulation of gene expression, and cell differentiation. NOX enzymes also contribute to a wide range of pathological processes. NOX deficiency may lead to immunosuppresion, lack of otoconogenesis, or hypothyroidism. Increased NOX actvity also contributes to a large number or pathologies, in particular cardiovascular diseases and neurodegeneration. This review summarizes the current state of knowledge of the functions of NOX enzymes in physiology and pathology.

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Section: Thyroidmentioning

confidence: 99%

The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology

Bedard¹,

Krause²

2007

Physiological Reviews

5,868

117

5,778

View full text Add to dashboard Cite

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“…H 2 O 2 acts as an electron acceptor in the thyroperoxidase-catalyzed iodination of thyroglobulin that takes place in the follicle lumen at the external side of the apical plasma membrane. At the same membrane surface H 2 O 2 is produced by a Ca 2þ -dependent NADPH oxidase (6,7). The main component of the thyroid NADPH oxidase is a flavoprotein (8), and some of the elements show great similarity to the H 2 O 2 -generating system in leukocytes (9).…”

Section: Introductionmentioning

confidence: 99%

Selenium has a protective role in caspase-3-dependent apoptosis induced by H2O2 in primary cultured pig thyrocytes

Demelash

Karlsson

Nilsson

et al. 2004

European Journal of Endocrinology

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Objective: Hydrogen peroxide (H 2 O 2 ), necessary for thyroid hormonogenesis, is produced at the apical surface of the thyroid follicular epithelium. Excess H 2 O 2 is potentially cytotoxic and may contribute to the development of hypothyroidism, e.g. in severe selenium deficiency. Yet it is unclear how H 2 O 2 contributes to thyroid cell death. Design and methods: H 2 O 2 -induced apoptosis and necrosis were studied in primary cultured pig thyroid cells. Glutathione peroxidase (GPx) activity was altered by culture in low serum with or without selenite substitution. Apoptosis was evaluated by spectrofluorometric measurement of caspase-3-specific substrate cleavage, and by analysis of DNA fragmentation by agarose gel electrophoresis. Necrosis was detected by 51

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“…In the thyrocyte, the hydrogen peroxide necessary for hormone biosynthesis is generated at the apical surface of the cell through a controlled reaction catalyzed by NADPH:O( 2 ) oxidoreductase flavoproteins [3] or simply NADPH oxidases, the dual oxidases DUOX1 and DUOX2. These enzymes are members of the NADPH oxidase (NOX) family of oxidoreductase enzymes, and DUOX1 shares 83% similarity with the DUOX2 gene.…”

Section: Introductionmentioning

confidence: 99%

Role of the NADPH Oxidases DUOX and NOX4 in Thyroid Oxidative Stress

Carvalho

Dupuy

2013

Eur Thyroid J

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Somatic mutations are present at high levels in the rat thyroid gland, indicating that the thyrocyte is under oxidative stress, a state in which cellular oxidant levels are high. The most important class of free radicals, or reactive metabolites, is reactive oxygen species (ROS), such as superoxide anion (O₂^-), hydroxyl radical (OH) and hydrogen peroxide (H₂O₂). The main source of ROS in every cell type seems to be mitochondrial respiration; however, recent data support the idea that NADPH:O(₂) oxidoreductase flavoproteins or simply NADPH oxidases (NOX) are enzymes specialized in controlled ROS generation at the subcellular level. Several decades ago, high concentrations of H₂O₂ were detected at the apical surface of thyrocytes, where thyroid hormone biosynthesis takes place. Only in the last decade has the enzymatic source of H₂O₂ involved in thyroid hormone biosynthesis been well characterized. The cloning of two thyroid genes encoding NADPH oxidases dual oxidases 1 and 2 (DUOX1 and DUOX2) revealed that DUOX2 mutations lead to hereditary hypothyroidism in humans. Recent reports have also described the presence of NOX4 in the thyroid gland and have suggested a pathophysiological role of this member of the NOX family. In the present review, we describe the participation of NADPH oxidases not only in thyroid physiology but also in gland pathophysiology, particularly the involvement of these enzymes in the regulation of thyroid oxidative stress.

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NADPH-dependent H2O2 generation and peroxidase activity in thyroid particular fraction

Cited by 64 publications

References 27 publications

The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology

The NOX Family of ROS-Generating NADPH Oxidases: Physiology and Pathophysiology

Selenium has a protective role in caspase-3-dependent apoptosis induced by H2O2 in primary cultured pig thyrocytes

Role of the NADPH Oxidases DUOX and NOX4 in Thyroid Oxidative Stress

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