Phenylarsine oxide inhibits ex vivo HIV-1 expression
| Autor: | Sylvie Legrand-Poels, M. Best-Belpomme, Monique Vuillaume, Neso Sojic, M. Edeas, Christian Amatore, A. Lindenbaum, Jacques Piette, Stéphane Arbault |
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| Rok vydání: | 1997 |
| Předmět: |
Lipopolysaccharides
Lipopolysaccharide HIV Core Protein p24 Protein tyrosine phosphatase Biology Virus Replication Peripheral blood mononuclear cell Arsenicals Monocytes Cell Line chemistry.chemical_compound Humans Phenylarsine oxide Enzyme Inhibitors Pharmacology Protein Tyrosine Phosphatase Non-Receptor Type 1 Tumor Necrosis Factor-alpha NF-kappa B General Medicine Hydrogen Peroxide Virology Molecular biology Oxidative Stress chemistry Cell culture Phorbol HIV-1 Tetradecanoylphorbol Acetate Tumor necrosis factor alpha Protein Tyrosine Phosphatases Ex vivo |
| Zdroj: | Biomedicinepharmacotherapy = Biomedecinepharmacotherapie. 51(10) |
| ISSN: | 0753-3322 |
| Popis: | Summary Phenylarsine oxide (PAO), which is described as an inhibitor of tyrosine phosphatase activity, inhibits H2O2 release from human peripheral blood mononuclear cells (PBMCs) as measured by electrochemistry. Since human immunodeficiency virus type 1 (HIV-1) replication is known to be favored under oxidative stress conditions, ex vivo experiments using uninfected PBMCs, primary monocytes or a latently infected promonocytic U1 cell line show that HIV-1 replication and reactivation, monitored by p24 antigen measurement, are inhibited by PAO in a time- and concentration-dependent manner. These observations can be linked with the inhibition of NF-κB activation when uninfected monocytes are induced by either tumor necrosis factor alpha (TNF-α), phorbol 12-myristate 13-acetate (PMA) or lipopolysaccharide (LPS). |
| Databáze: | OpenAIRE |
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