RESUMO
UNLABELLED: Tapering can be an effective way of enhancing performance after a period of intensive training, but the mechanisms for this ergogenic effect are unclear. It was hypothesized that overload training will increase oxidative stress through an accumulative effect of repeated high-intensity exercise, whereas tapering will improve the antioxidant defense system and alleviate oxidative stress. PURPOSE: To study the oxidative stress response to overload training and tapering. METHODS: A group of eight well-trained male endurance athletes (30+/-6 yr; 73+/-13 kg; 64+/-6 mL.kg.min) performed two 4-wk periods of training in a crossover design. Each period included a 2-wk build-up phase followed either by 2 wk of training at the same load (control) or by a week with a 40% increase in training load (overload) preceding a week with a 60% reduction in training load (taper). Performance was monitored through weekly 15-min cycling time trials preceded by a 45-min preload at 70% Wmax. Blood samples were taken before and after the time trials and analyzed for oxidatively modified heme (OxHm), methemoglobin (metHb), and glutathione redox status. RESULTS: Cycling time trials induced significant postexercise increases in levels of OxHm (+3.8%; P<0.001) and oxidized glutathione (GSSG: +13.9%; P<0.05) and decreases in metHb (-12.1%; P<0.001), reduced glutathione (GSH: -14.4%; P<0.001), and GSH/GSSG (-29.7%; P<0.001). Tapering was shown to significantly increase performance (+4.9%; P<0.05). Training modifications did not influence resting levels or exercise-induced changes of markers of oxidative stress. CONCLUSION: A short period of tapered training improves performance but does not seem to be associated with substantial changes in exercise-induced oxidative stress.
Assuntos
Estresse Oxidativo/fisiologia , Esforço Físico , Antioxidantes , Estudos Cross-Over , Teste de Esforço , Glutationa , Humanos , Masculino , Reino UnidoRESUMO
Although assays for the most popular markers of exercise-induced oxidative stress may experience methodological flaws, there is sufficient credible evidence to suggest that exercise is accompanied by an increased generation of free radicals, resulting in a measurable degree of oxidative modifications to various molecules. However, the mechanisms responsible are unclear. A common assumption that increased mitochondrial oxygen consumption leads per se to increased reactive oxygen species (ROS) production is not supported by in vitro and in vivo data. The specific contributions of other systems (xanthine oxidase, inflammation, haem protein auto-oxidation) are poorly characterised. It has been demonstrated that ROS have the capacity to contribute to the development of muscle fatigue in situ, but there is still a lack of convincing direct evidence that ROS impair exercise performance in vivo in humans. It remains unclear whether exercise-induced oxidative modifications have little significance, induce harmful oxidative damage, or are an integral part of redox regulation. It is clear that ROS play important roles in numerous physiological processes at rest; however, the detailed physiological functions of ROS in exercise remain to be elucidated.
Assuntos
Exercício Físico/fisiologia , Peroxidação de Lipídeos/fisiologia , Estresse Oxidativo/fisiologia , Animais , Feminino , Radicais Livres/análise , Nível de Saúde , Humanos , Masculino , Consumo de Oxigênio/fisiologia , Condicionamento Físico Animal , Sensibilidade e EspecificidadeRESUMO
Free radical formation in heme proteins is recognised as a factor in mediating the toxicity of peroxides in oxidative stress. As well as initiating free radical damage, heme proteins damage themselves. Under extreme conditions, where oxidative stress and low pH coincide (e.g., myoglobin in the kidney following rhabdomyolysis and hemoglobin in the CSF subsequent to subarachnoid hemorrhage), peroxide can induce covalent heme to protein cross-linking. In this paper we show that, even at neutral pH, the heme in hemoglobin is covalently modified by oxidation. The product, which we term OxHm, is a "green heme" iron chlorin with a distinct optical spectrum. OxHm formation can be quantitatively prevented by reductants of ferryl iron, e.g., ascorbate. We have developed a simple, robust, and reproducible HPLC assay to study the extent of OxHm formation in the red cell in vivo. We show that hemoglobin is oxidatively damaged even in normal blood; approximately 1 in 2,000 heme groups exist as OxHm in the steady state. We used a simple model (physical exercise) to demonstrate that OxHm increases significantly during acute oxidative stress. The exercise-induced increase is short-lived, suggesting the existence of an active mechanism for repairing or removing the damaged heme proteins.