Oxidative Stress Contributes to Cytoskeletal Protein Degradation of Esox lucius through Activation of Mitochondrial Apoptosis during Postmortem Storage.

Abstract

This study investigated the role of oxidative stress in the mitochondrial apoptotic pathways and structural protein degradation of fish during postmortem storage by measuring oxidative stress levels, mitochondrial antioxidant enzyme activity, mitochondrial dysfunction, apoptotic factors, and structural protein degradation (n = 3). The results revealed that reactive oxygen species (ROS) increased gradually within the first 12 h and then decreased (p < 0.05) in mitochondria. Lipid peroxidation was increased, and superoxide dismutase, catalase, and glutathione peroxidase activities were decreased in mitochondria (p < 0.05). Furthermore, oxidative stress induced mitochondrial membrane opening, mitochondrial swelling, as well as the depolarization of mitochondrial potential. This led to an increase in the release of cytochrome c from mitochondria and caspase-3 activation. Ultimately, oxidative stress promoted small protein degradation (troponin-T and desmin) and induced myofibril susceptibility to proteolysis. These observations confirmed that oxidative stress mediated the activation of mitochondrial apoptotic factors-promoted protein degradation, initiating the deterioration of fish muscle through the mitochondrial apoptotic pathway.