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Selenium-Dependent Glutathione Peroxidase and Eicosanoid Production

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Biochemistry of Arachidonic Acid Metabolism

Part of the book series: Prostaglandins, Leukotrienes, and Cancer ((PLAC,volume 1))

Abstract

In 1971, Lands et al. (1) reported that a functioning glutathione peroxidase (GSHPx, EC 1.11.1.9) system inhibited two dioxygenases, prostaglandin (PG) synthase from sheep vesicular glands and soybean lipoxygenase, suggesting that product activation is an important feature in the mechanism for both enzymes. These initial experiments were followed by a series of studies (See Chapters 1 and 2 this book and Ref. 2) which demonstrated the peroxide requirement for activation and maintenance of the catalytic function of PG synthase in vitro. The synthase is inhibited at peroxide concentrations 1 μmole/1 or greater. This property of duality, stimulation at low and inhibition at high concentrations, has led to the hypothesis that “peroxide tone” can regulate the production of eicosanoids, oxygenated metabolites of arachidonic acid (20: 4). The provocative question that arises from these enzymatic studies is “Does GSHPx function as a modulator of dioxygenases by regulating the hydroperoxide level within the cell?” A survey of the literature indicates that evidence is accumulating to support a positive response to this query and it is this evidence which is the subject of this chapter.

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© 1985 Martinus Nijhoff Publishing, Boston

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Schoene, N.W. (1985). Selenium-Dependent Glutathione Peroxidase and Eicosanoid Production. In: Lands, W.E.M. (eds) Biochemistry of Arachidonic Acid Metabolism. Prostaglandins, Leukotrienes, and Cancer, vol 1. Springer, Boston, MA. https://doi.org/10.1007/978-1-4613-2597-0_8

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  • DOI: https://doi.org/10.1007/978-1-4613-2597-0_8

  • Publisher Name: Springer, Boston, MA

  • Print ISBN: 978-1-4612-9627-0

  • Online ISBN: 978-1-4613-2597-0

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