Cellular Glutathione Peroxidase as a Predominant Scavenger of Hydroperoxyeicosatetraenoic Acids in Rabbit Alveolar Macrophages.

Chiba, Nobuyoshi; Imai, Hideki; Narashima, Kazuki; Arai, Masayoshi; Oshima, Genichiro; Kunimoto, Manabu; Nakagawa, Yasuhito

doi:10.1248/bpb.22.1047

Cited by 15 publications

(8 citation statements)

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“…The regulation of hydroperoxide metabolism and control of leukotriene metabolism are clearly very important functions of GPX-4 located in both mitochondria and the cytosol. In addition, in some circulating granulocytes there is evidence that GPX-1 also has important functions in the control of leukotriene metabolism [97].…”

Section: Gpx-4 Functionsmentioning

confidence: 99%

The glutathione peroxidases

Arthur¹

2001

CMLS, Cell. Mol. Life Sci.

774

497

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There are several proteins in mammalian animals. Additionally, cellular glutathione peroxidase knockout mice have been used to investigate the funccells that can metabolize hydrogen peroxide and lipid hydroperoxides. These proteins include four selenium-tions of this protein. From this work it is clear that the selenoperoxidases are involved in cell antioxidant syscontaining glutathione peroxidases that are found in tems. However, they also have more subtle functions different cell fractions and tissues of the body. This in ensuring the regulation and formation of arachareview considers the structure and distribution of the selenoperoxidases and how this relates to their biologi-donic acid metabolites that are derived from hydroperoxide intermediates. The range of biological processes, cal function. The functions of the selenoperoxidases were originally studied in systems where their activity which are potentially dependent on optimal selenoperwas manipulated by changing dietary selenium levels. oxidase activity in mammals, emphasises the imporMore recently, molecular techniques have allowed tance of achieving adequate selenium intake in the overexpression of selenoperoxidases in cell lines and diet.

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Section: Gpx-4 Functionsmentioning

confidence: 99%

The glutathione peroxidases

Arthur¹

2001

CMLS, Cell. Mol. Life Sci.

774

497

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“…Arachidonic acid is converted to prostaglandins and thromboxanes by cyclooxygenase (prostaglandin endoperoxide synthase); leukotrienes via 5-HPETE by 5-lipoxygenase; to lipoxins via 15-HPETE by 15-lipoxygenase; and 12-HPETE by 12-lipoxygenase (24). 5-HPETE can be reduced by lipid peroxidases such as glutathione peroxidase to 5-HETE (25,26), which is finally oxidized to 5-oxo-ETE by 5(S)-hydroxyeicosanoid-specific dehydrogenase (27). Eicosanoid receptors recognizing prostaglandins D 2 , E 2 , and F 2␣ ; prostacyclin; thromboxane A 2 ; and leukotriene B 4 ; respectively, have been cloned and vigorously analyzed because of the importance of their implicated biological functions such as inflammation, blood clotting, and control of vascular tone (11,24,28).…”

Section: Fig 5 Effect Of 5-oxo-ete On Forskolin-stimulated Camp Promentioning

confidence: 99%

Identification of a Novel Human Eicosanoid Receptor Coupled to Gi/o

Hosoi¹,

Koguchi²,

Sugikawa

et al. 2002

Journal of Biological Chemistry

147

137

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We have conducted an in silico data base search for and cloned a novel G-protein-coupled receptor (GPCR) named TG1019. Dot and Northern blotting analyses showed that transcripts of the novel GPCR were expressed in various tissues except brain, and the expression was more intense in liver, kidney, peripheral leukocyte, lung, and spleen than in other tissues. By GTP␥S binding assay using the TG1019-G␣ i1 -protein fusion expressed in insect cells, eicosanoids, and polyunsaturated fatty acids such as 5-oxo-6E,8Z,11Z,14Z-eicosatetraenoic acid (5-oxo-ETE), 5(S)-hydroperoxy-6E,8Z, 11Z,14Z-eicosatetraenoic acid, and arachidonic acid were identified to exhibit agonistic activities against TG1019. 5-oxo-ETE was the most potent to enhance the specific binding by 6-fold at a maximum effect dose of submicromolar to micromolar order with an ED 50 value of 5.7 nM. Conversely, polyunsaturated fatty acids such as docosahexaenoic acid and eicosapentaenoic acid showed antagonistic activities against TG1019. In Chinese hamster ovary cells transiently expressing TG1019, the forskolin-stimulated production of cAMP was inhibited up to ϳ70% by 5-oxo-ETE, with an IC 50 value of 33 nM. This inhibition was sensitive to pretreatment of the cells with pertussis toxin.

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“…nitrogen and redissolved in chloroform. Total hydroperoxide was quantified by the methylcarbamoylmethylene method [22] with PC hydroperoxide that had been prepared previously as a standard. Lipid phosphorus was estimated as described previously [23].…”

Section: Preparation Of Cl-ooh and Hydroxycardiolipin (Cl-oh)mentioning

confidence: 99%

Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis

Nomura

Imai

Koumura

et al. 2000

Biochemical Journal

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271

179

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Cytochrome c (cyt. c) is a proapoptotic factor that binds preferentially to cardiolipin (CL), a mitochondrial lipid, but not to cardiolipin hydroperoxide (CL-OOH). Cyt. c that had bound to CL liposomes was liberated on peroxidation of the liposomes by a radical. The generation of CL-OOH in mitochondria occurred before the release of cyt. c in rat basophile leukaemia (RBL)2H3 cells that had been induced to undergo apoptosis by exposure to hypoglycaemia with 2-deoxyglucose (2DG). The amount of cyt. c bound to CL prepared from the mitochondria of 2DG-treated cells was lower than that of untreated cells. The release of cyt. c was completely suppressed when the production of CL-OOH in mitochondria was inhibited by the overexpression of mitochondrial phospholipid hydroperoxide glutathione peroxidase (PHGPx). The fluorescence from CL-labelling dye (10-N-nonyl Acridine Orange) decreased on the induction of apoptosis by 2DG. However, no decrease in fluorescence was observed in PHGPx-overexpressing cells. Cyt. c was released from mitochondria that had been isolated from control cells on peroxidation by t-butylhydroperoxide, but no similar liberation of cyt. c from mitochondria isolated from mitochondrial PHGPx-overexpressing cells was observed. These findings suggest that the generation of CL-OOH in mitochondria might be a primary event that triggers the release of cyt. c from mitochondria in the apoptotic process in which mitochondrial PHGPx participates as an anti-apoptotic factor by preventing the formation of CL-OOH.

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Cellular Glutathione Peroxidase as a Predominant Scavenger of Hydroperoxyeicosatetraenoic Acids in Rabbit Alveolar Macrophages.

Cited by 15 publications

References 1 publication

The glutathione peroxidases

The glutathione peroxidases

Identification of a Novel Human Eicosanoid Receptor Coupled to Gi/o

Mitochondrial phospholipid hydroperoxide glutathione peroxidase inhibits the release of cytochrome c from mitochondria by suppressing the peroxidation of cardiolipin in hypoglycaemia-induced apoptosis

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