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1-Cys Peroxiredoxin Overexpression Protects Cells against Phospholipid Peroxidation-Mediated Membrane Damage

Manevich, Yefim ; Sweitzer, Tom ; Pak, Jhang Ho ; Feinstein, Sheldon I. ; Muzykantov, Vladimir ; Fisher, Aron B.

Proceedings of the National Academy of Sciences - PNAS, 2002-09, Vol.99 (18), p.11599-11604 [Periódico revisado por pares]

United States: National Academy of Sciences

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  • Título:
    1-Cys Peroxiredoxin Overexpression Protects Cells against Phospholipid Peroxidation-Mediated Membrane Damage
  • Autor: Manevich, Yefim ; Sweitzer, Tom ; Pak, Jhang Ho ; Feinstein, Sheldon I. ; Muzykantov, Vladimir ; Fisher, Aron B.
  • Assuntos: 3T3 cells ; Amino Acid Sequence ; Animals ; Annexins ; Antioxidants ; Base Sequence ; Biochemistry ; Biological Sciences ; Cell lines ; Cell membranes ; Cells, Cultured ; Cytoprotection ; DNA Primers ; Enzymes ; Fluorescence ; Lipid Peroxidation ; Lipids ; Lungs ; Membranes ; Molecular Sequence Data ; Oxidative Stress ; Peroxidases - chemistry ; Peroxidases - metabolism ; Peroxiredoxins ; Phospholipids ; Phospholipids - metabolism ; Pretreatment ; Rats ; Thiobarbituric Acid Reactive Substances - metabolism
  • É parte de: Proceedings of the National Academy of Sciences - PNAS, 2002-09, Vol.99 (18), p.11599-11604
  • Notas: ObjectType-Article-1
    SourceType-Scholarly Journals-1
    ObjectType-Feature-2
    content type line 23
    Communicated by Robert E. Forster, University of Pennsylvania School of Medicine, Philadelphia, PA
    To whom reprint requests should be addressed. E-mail: abf@mail.med.upenn.edu.
  • Descrição: 1-Cys peroxiredoxin (1-cysPrx) is a novel antioxidant enzyme able to reduce phospholipid hydroperoxides in vitro by using glutathione as a reductant. This enzyme is widely expressed and is enriched in lungs. A fusion protein of green fluorescent protein with 1-cysPrx was stably expressed in a lung-derived cell line (NCl-H441) lacking endogenous enzyme. Overexpressing cells (C17 or C48) degraded H2O 2and t-butylhydroperoxide more rapidly and showed decreased sensitivity to oxidant stress as measured by51Cr release. On exposure to$^\bullet OH$generated by Cu2+-ascorbate (Asc), overexpressing cells compared with H441 showed less increase in thiobarbituric acid-reactive substance and phosphatidylcholine hydroperoxide content. This effect was reversed by depletion of cellular glutathione. Diphenyl-1-pyrenoylphosphonium fluorescence, used as a real-time probe of membrane phospholipid peroxidation, increased immediately on exposure to Cu2+-Asc and was abolished by preincubation of cells with Trolox (a soluble vitamin E) or Tempol (a radical scavenger). The rate of diphenyl-1-pyrenoylphosphonium fluorescence increase with Cu2+-Asc exposure was markedly attenuated in C17 and C48 cells as compared with H441. Annexin V-Cy3 was used to detect phosphatidylserine translocation from the inner to outer leaflet of the plasma membrane. Cu2+-Asc treatment induced phosphatidylserine translocation within 2 h in H441 cells but none was observed in C48 cells up to 24 h. These results indicate that 1-cysPrx can scavenge peroxides but in addition can reduce peroxidized membrane phospholipids. Thus, the enzyme can protect cells against oxidant-induced plasma membrane damage, thereby playing an important role in cellular defense against oxidant stress.
  • Editor: United States: National Academy of Sciences
  • Idioma: Inglês
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  • Realização: ABCD-USP USP   Logos de Redes Sociais: Freepik

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