Peroxynitrite oxidizes erythrocyte membrane band 3 protein and diminishes its anion transport capacity
| Autor: | Gloria Celedón, Gustavo González, Eduardo Lissi, Jose A. Pino |
|---|---|
| Rok vydání: | 2007 |
| Předmět: |
Anions
Erythrocytes Inorganic chemistry Oxidative phosphorylation Biochemistry Catechin Hemoglobins chemistry.chemical_compound Anion Exchange Protein 1 Erythrocyte Peroxynitrous Acid Nitration medicine Humans Band 3 Cell damage Ion Transport Nitrates biology Band 3 Anion Transport Protein General Medicine Oxidants medicine.disease Acetylcysteine Membrane chemistry biology.protein Biophysics Tyrosine Oxidation-Reduction Peroxynitrite Cysteine |
| Zdroj: | Free Radical Research. 41:316-323 |
| ISSN: | 1029-2470 1071-5762 |
| DOI: | 10.1080/10715760601090305 |
| Popis: | We describe an altered membrane band 3 protein-mediated anion transport in erythrocytes exposed to peroxynitrite, and relate the loss of anion transport to cell damage and to band 3 oxidative modifications. We found that peroxynitrite down-regulate anion transport in a dose dependent relation (100-300 micromoles/l). Hemoglobin oxidation was found at all peroxynitrite concentrations studied. A dose-dependent band 3 protein crosslinking and tyrosine nitration were also observed. Band 3 protein modifications were concomitant with a decrease in transport activity. ( - )-Epicatechin avoids band 3 protein nitration but barely affects its transport capacity, suggesting that both processes are unrelated. N-acetyl cysteine partially reverted the loss of band 3 transport capacity. It is concluded that peroxynitrite promotes a decrease in anion transport that is partially due to the reversible oxidation of band 3 cysteine residues. Additionally, band 3 tyrosine nitration seems not to be relevant for the loss of its anion transport capacity. |
| Databáze: | OpenAIRE |
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