Evidence that erythrocytes are highly susceptible to exercise oxidative stress: FT-IR spectrometric studies at the molecular level

Authors

  • Cyril Petibois,

    Corresponding author
    1. CNRS UMR 5084, CNAB, Groupe de Chimie Bio-Organique, 33076 Bordeaux, Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux, France
    2. Faculté des Sciences du Sport et de l'Education Physique, Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux, France
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  • Gérard Déléris

    1. CNRS UMR 5084, CNAB, Groupe de Chimie Bio-Organique, 33076 Bordeaux, Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux, France
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Corresponding author. CNRS UMR 5084, CNAB, Groupe de Chimie Bio-Organique, 33076 Bordeaux, Université Victor Segalen Bordeaux 2, 146 rue Léo Saignat, 33076 Bordeaux, France. Tel./fax: +33 5 57 57 10 02. cyril.petibois@u-bordeaux2.fr

Abstract

We tested the hypothesis that usual exercise oxidative stress strongly affects erythrocytes viability. A 120-min physical exercise with progressive intensity was used as a model of oxidative stress. FT-IR spectrometry was used to determine structural changes in erythrocyte contents (phospholipids, proteins, lactate, and glucose) from blood samples taken every 20 min. Carbonyl formation from amino acid residues (P = 0.03) and hemoglobin unfolding (P = 0.01) could be identified as main protein denaturation markers during oxidative stress. Higher unsaturation level (P = 0.001) in phospholipids fatty acyl chains were also observed while VO2 increased (P < 0.05). The increase in lactacidosis affected primarily hemoglobin unfolding (P = 0.02). Finally, two distinct cellular events occurred during oxidative stress: 1—phospholipids peroxidation correlated to VO2, but lactacidosis and hemoconcentration remained secondary factors; 2—hemoglobin denaturation was mainly observed through unfolding and carbonylation, and lactacidosis and hemoconcentration were important contributing factors.

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