Oxidative stress responses in older men during endurance training and detraining

Purpose: Aging is associated with increased oxidative stress, whereas systematic exercise training has been shown to improve quality of life and functional performance of the aged. This study aimed to evaluate responses of selected markers of oxidative stress and antioxidant status in inactive older men during endurance training and detraining. Methods: Nineteen older men (65-78 yr) were randomly assigned into either a control (C, N = 8) or an endurance-training (ET, N = 11, three training sessions per week, 16 wk, walking/jogging at 50-80% of HRmax) group. Before, immediately posttraining, and after 4 months of detraining, subjects performed a progressive diagnostic treadmill test to exhaustion (GXT). Plasma samples, collected before and immediately post-GXT, were analyzed for malondialdehyde (MDA) and 3-nitrotyrosine (3-NT) levels, total antioxidant capacity (TAC), and glutathione peroxidase activity (GPX). Results: ET caused a 40% increase in running time and a 20% increase in maximal oxygen consumption (VO2max) (P < 0.05). ET lowered MDA (9% at rest, P < 0.01; and 16% postexercise, P < 0.05) and 3-NT levels (20% postexercise, P < 0.05), whereas it increased TAC (6% at rest, P < 0.01; and 14% postexercise, P < 0.05) and GPX (12% postexercise, P < 0.05). However, detraining abolished these adaptations. Conclusions: ET may attenuate basal and exercise-induced lipid peroxidation and increase protection against oxidative stress by increasing TAC and GPX activity. However, training cessation may reverse these training-induced adaptations

Membrane-Bound Alpha Synuclein Clusters Induce Impaired Lipid Diffusion and Increased Lipid Packing

The aggregation of membrane-bound α-synuclein (αS) into oligomers and/or amyloid fibrils has been suggested to cause membrane damage in in vitro model phospholipid membrane systems and in vivo. In this study, we investigate how αS interactions that precede the formation of well-defined aggregates influence physical membrane properties. Using three truncated variants of αS with different aggregation propensities and comparable phospholipid membrane binding affinities we show, using fluorescence recovery after photobleaching (FRAP) and fluorescence anisotropy measurements, that formation of αS clusters on supported lipid bilayers (SLBs) impairs lateral lipid diffusion and increases lipid packing beneath the αS clusters. Formation of protein clusters starts immediately after monomer addition. The magnitudes of the changes in effective lipid diffusion and lipid order increase with the protein cluster size. Our results show that the combination of inter-αS and αS-membrane interactions can drive the formation of more ordered lipid domains. Considering the functional involvement of membrane micro-domains in biological membranes, αS-induced domain formation may be relevant for alternative disease mechanisms