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Title:
Inhibition of arachidonate metabolism in human epidermoid carcinoma A431 cells overexpressing phospholipid hydroperoxide glutathione peroxidase | Journal of Biomedical Science
Description:
Phospholipid hydroperoxide glutathione peroxidase (PHGPx), a selenium-dependent glutathione peroxidase, can interact with lipophilic substrates, including phospholipid hydroperoxides, fatty acid hydroperoxides and cholesterol hydroperoxides, and can reduce them to hydroxide compounds. It also seems to be a major regulator of lipid oxygenation in human epidermoid carcinoma A431 cells. In order to study the functional role of PHGPx in the regulation of 12-lipoxygenase and cyclooxygenase, cDNA of PHGPx was inserted into pcDNA3.1/His, and a plasmid designated as S4 with the His-tag sequence inserted between PHGPx and its 3′-untranslated region was constructed. A number of stable transfectants of A431 cells that could express the tag-PHGPx were generated using plasmid S4. Using an intact cell assay system, the metabolism of arachidonic acid to prostaglandin E2 significantly decreased in stable transfectants of overexpressing PHGPx compared to that in a vector control cell line. If the intact cell assay was carried out in the presence of 13-hydroperoxyoctadecadienoic acid as a stimulator of lipid peroxidation, formation of 12-hydroxyeicosatetraenoic acid from arachidonic acid also significantly decreased in stable transfectants of overexpressing PHGPx compared to that in a vector control cell line, indicating that PHGPx could downregulate the 12-lipoxygenase activity in cells. These results support the hypothesis that PHGPx plays a pivotal role in the regulation of arachidonate metabolism in A431 cells.
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Keywords {🔍}
google, scholar, glutathione, peroxidase, phospholipid, hydroperoxide, cells, article, lipoxygenase, biol, chem, chang, phgpx, lipid, human, huang, chen, cell, access, privacy, cookies, content, journal, acid, cdna, publish, search, metabolism, epidermoid, carcinoma, overexpressing, hydroperoxides, activity, biochem, expression, cloning, ursini, data, information, log, research, science, arachidonate, functional, role, regulation, cyclooxygenase, sequence, stable, transfectants,
Topics {✒️}
selenium-dependent glutathione peroxidase month download article/chapter membrane-damaging lipid peroxidation therapy-resistant state related subjects �enzymatic’ lipid peroxidation 138 sheng-li road overexpressing phgpx compared including phospholipid hydroperoxides cancer cells intact cell assay full article pdf privacy choices/manage cookies hydroperoxide-reducing activity glutathione peroxidase rbl-2h3 cells cold spring harbor a431 cells check access instant access chang wc lipid peroxidation european economic area point mutations define aug initiator codon folin phenol reagent article chen human plasma fatty acid hydroperoxides conditions privacy policy september 2002 volume 9 translation start sites prostaglandin d2 synthesis lipid oxygenation microsomal 12-lipoxygenase activity accepting optional cookies journal finder publish article journal mouse cdna sequence reduced glutathione tag sequence inserted article log chen cj oxygenation products article cite significantly decreased rat platelets esworthy rs chu ff mutant enzyme
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headline:Inhibition of arachidonate metabolism in human epidermoid carcinoma A431 cells overexpressing phospholipid hydroperoxide glutathione peroxidase
description:Phospholipid hydroperoxide glutathione peroxidase (PHGPx), a selenium-dependent glutathione peroxidase, can interact with lipophilic substrates, including phospholipid hydroperoxides, fatty acid hydroperoxides and cholesterol hydroperoxides, and can reduce them to hydroxide compounds. It also seems to be a major regulator of lipid oxygenation in human epidermoid carcinoma A431 cells. In order to study the functional role of PHGPx in the regulation of 12-lipoxygenase and cyclooxygenase, cDNA of PHGPx was inserted into pcDNA3.1/His, and a plasmid designated as S4 with the His-tag sequence inserted between PHGPx and its 3′-untranslated region was constructed. A number of stable transfectants of A431 cells that could express the tag-PHGPx were generated using plasmid S4. Using an intact cell assay system, the metabolism of arachidonic acid to prostaglandin E2 significantly decreased in stable transfectants of overexpressing PHGPx compared to that in a vector control cell line. If the intact cell assay was carried out in the presence of 13-hydroperoxyoctadecadienoic acid as a stimulator of lipid peroxidation, formation of 12-hydroxyeicosatetraenoic acid from arachidonic acid also significantly decreased in stable transfectants of overexpressing PHGPx compared to that in a vector control cell line, indicating that PHGPx could downregulate the 12-lipoxygenase activity in cells. These results support the hypothesis that PHGPx plays a pivotal role in the regulation of arachidonate metabolism in A431 cells.
datePublished:
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Phospholipid hydroperoxide glutathione peroxidase
Cyclooxygenase
12-Lipoxygenase
A431 cells
Biomedicine
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headline:Inhibition of arachidonate metabolism in human epidermoid carcinoma A431 cells overexpressing phospholipid hydroperoxide glutathione peroxidase
description:Phospholipid hydroperoxide glutathione peroxidase (PHGPx), a selenium-dependent glutathione peroxidase, can interact with lipophilic substrates, including phospholipid hydroperoxides, fatty acid hydroperoxides and cholesterol hydroperoxides, and can reduce them to hydroxide compounds. It also seems to be a major regulator of lipid oxygenation in human epidermoid carcinoma A431 cells. In order to study the functional role of PHGPx in the regulation of 12-lipoxygenase and cyclooxygenase, cDNA of PHGPx was inserted into pcDNA3.1/His, and a plasmid designated as S4 with the His-tag sequence inserted between PHGPx and its 3′-untranslated region was constructed. A number of stable transfectants of A431 cells that could express the tag-PHGPx were generated using plasmid S4. Using an intact cell assay system, the metabolism of arachidonic acid to prostaglandin E2 significantly decreased in stable transfectants of overexpressing PHGPx compared to that in a vector control cell line. If the intact cell assay was carried out in the presence of 13-hydroperoxyoctadecadienoic acid as a stimulator of lipid peroxidation, formation of 12-hydroxyeicosatetraenoic acid from arachidonic acid also significantly decreased in stable transfectants of overexpressing PHGPx compared to that in a vector control cell line, indicating that PHGPx could downregulate the 12-lipoxygenase activity in cells. These results support the hypothesis that PHGPx plays a pivotal role in the regulation of arachidonate metabolism in A431 cells.
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