One- and Two-Electron Oxidation of Reduced Glutathione by Peroxidases

Harman, Laura S.; Carver, D K; Schreiber, Jörg; Mason, Ronald P.

doi:10.1007/978-1-4684-5134-4_47

Biological Reactive Intermediates III

1986

DOI: 10.1007/978-1-4684-5134-4_47

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One- and Two-Electron Oxidation of Reduced Glutathione by Peroxidases

Laura S. Harman

D K Carver²,

Jörg Schreiber³

et al.

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Cited by 34 publications

References 6 publications

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Zur Biochemie der Thiolgruppe: Bedeutung des Glutathions

Sies

1989

Naturwissenschaften

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Glutathione (GSH) comprises the bulk of the pool of free thiol groups in biological systems. Since its first description as philothione 100 years ago, there have been repeated surprises in discoveries of novel functions. Just recently the important role of thioethers with products of the lipoxygenase reaction, i.e., the leukotrienes, was revealed as mediator of physiological and pathophysiological processes. Another major function resides in detoxication, GSH being cosubstrate in the GSH-peroxidase reaction for the reduction of hydroperoxides in the defense against oxidative stress. Interest also focuses on reactions of glutathionyl radicals in protection by thiols against DNA damage resulting from ionizing radiation.

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Zur Biochemie der Thiolgruppe: Bedeutung des Glutathions

Sies

1989

Naturwissenschaften

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The acrolein cytotoxicity and cytoprotective action of α-tocopherol

1992

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The influence of acrolein on hepatocytes and the effect of alpha-tocopherol on acrolein cytotoxicity were investigated using primary cultured rat hepatocytes. Hepatocellular injury was dependent on both acrolein concentration in medium and on duration of exposure. Treatment of hepatocytes with 100 microM acrolein resulted in a marked loss of cellular glutathione (GSH) within 15 min, gradual accumulation of cellular lipid peroxide (LPO) and subsequent lactate dehydrogenase (LDH) leakage in the medium from 3 hr after exposure to acrolein. Cellular GSH peroxidase (GSH-Px) activity at 2 hr was significantly decreased. Electron microscopic examination on hepatocytes at 8 hr revealed a marked swelling of mitochondria and ruptures of the plasma membrane. Simultaneous treatment with 100 microM acrolein and 20 microM alpha-tocopherol did not prevent the loss of cellular GSH, though it prevented the LPO accumulation and the LDH leakage. The decrease of cellular GSH-Px activity with acrolein treatment was not mitigated by co-treatment with alpha-tocopherol. Ultrastructural alterations of hepatocytes induced by acrolein were minimized by co-treatment with alpha-tocopherol. In conclusion, acute loss of GSH and GSH-Px may increase cellular LPO and lead to hepatocellular injury, though suppression of cellular LPO accumulation by alpha-tocopherol can prevent the hepatocellular injury, even under condition of lack of GSH and GSH-Px.

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Lipoxygenase - a versatile biocatalyst for biotransformation of endobiotics and xenobiotics

Kulkarni¹

2001

CMLS, Cell. Mol. Life Sci.

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Lipoxygenase, a member of the arachidonate cascade enzymes, dioxygenates polyenoic fatty acids to finally yield products with profound and distinct biological activity. This review summarizes the available evidence for another role played by lipoxygenases in the metabolism of endobiotics and xenobiotics. Although other mechanisms exist, a direct hydrogen abstraction by the enzyme and the peroxyl radical-dependent chemical oxidation appear to be central to the co-oxidase activity of lipoxygenases. Besides polyunsaturated fatty acids, H2O2, fatty acid hydroperoxides, and synthetic organic hydroperoxides support the lipoxygenase-catalyzed xenobiotic oxidation. The major reactions documented thus far include oxidation, epoxidation, hydroxylation, sulfoxidation, desulfuration, dearylation, and N-dealkylation. It is noteworthy that lipoxygenases are also capable of glutathione conjugation of certain xenobiotics. The enzyme system appears to be inducible following exposure to chemicals. Lipoxygenases are inhibited by a large number of chemicals, some of which also serve as co-substrates. Available data suggest that lipoxygenases contribute to in vivo metabolism of xenobiotics in mammals.

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One- and Two-Electron Oxidation of Reduced Glutathione by Peroxidases

Cited by 34 publications

References 6 publications

Zur Biochemie der Thiolgruppe: Bedeutung des Glutathions

Zur Biochemie der Thiolgruppe: Bedeutung des Glutathions

The acrolein cytotoxicity and cytoprotective action of α-tocopherol

Lipoxygenase - a versatile biocatalyst for biotransformation of endobiotics and xenobiotics

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