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LINK . SPRINGER . COM {}

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We are analyzing https://link.springer.com/article/10.1007/bf02256540.

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.
Website Age:
28 years and 1 months (reg. 1997-05-29).

Matching Content Categories {📚}

  • Science
  • Education
  • Telecommunications

Content Management System {📝}

What CMS is link.springer.com built with?

Custom-built

No common CMS systems were detected on Link.springer.com, and no known web development framework was identified.

Traffic Estimate {📈}

What is the average monthly size of link.springer.com audience?

🌠 Phenomenal Traffic: 5M - 10M visitors per month


Based on our best estimate, this website will receive around 8,170,236 visitors per month in the current month.

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How Does Link.springer.com Make Money? {💸}

We're unsure how the site profits.

Not all websites are made for profit; some exist to inform or educate users. Or any other reason why people make websites. And this might be the case. Link.springer.com might be plotting its profit, but the way they're doing it isn't detectable yet.

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

Schema {🗺️}

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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:
         dateModified:
         pageStart:453
         pageEnd:459
         sameAs:https://doi.org/10.1007/BF02256540
         keywords:
            Phospholipid hydroperoxide glutathione peroxidase
            Cyclooxygenase
            12-Lipoxygenase
            A431 cells
            Biomedicine
            general
         image:
         isPartOf:
            name:Journal of Biomedical Science
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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:
      dateModified:
      pageStart:453
      pageEnd:459
      sameAs:https://doi.org/10.1007/BF02256540
      keywords:
         Phospholipid hydroperoxide glutathione peroxidase
         Cyclooxygenase
         12-Lipoxygenase
         A431 cells
         Biomedicine
         general
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         name:Journal of Biomedical Science
         issn:
            1423-0127
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                  name:National Cheng Kung University
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                     name:Department Medical Technology, College of Medicine, National Cheng Kung University, Tainan, Taiwan, ROC
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            name:Wen-Chang Chang
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            name:National Cheng Kung University
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               name:Department of Pharmacology College of Medicine, National Cheng Kung University, Tainan, Taiwan (ROC)
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External Links {🔗}(53)

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