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This study investigated the effect of lysosomal iron involvement in the mechanism of mitochondrial apoptosis on bovine muscle protein degradation during postmortem aging. Six crossbred cattle were studied to evaluate intracellular reactive oxygen species (ROS), antioxidant enzyme activity, lysosomal membrane stability, mitochondrial dysfunction-induced apoptosis, desmin and troponin-T degradation in both control and iron chelator desferrioxamine (DFO) groups. Results showed that lysosomal iron induced ROS accumulation and lysosomal membrane destabilization by decreasing the antioxidant enzyme activity (P 0.05). Subsequently, lysosomal dysfunction mediated by iron increased mitochondrial membrane permeability and decreased mitochondrial membrane potential, thereby enhancing Bid and cytochrome c release and caspase-9/-3 activation (P 0.05). Ultimately, lysosomal iron mediated lysosomal-mitochondrial apoptosis increased the postmortem bovine muscle desmin and troponin-T degradation (P 0.05). The results indicated that lysosomal iron contributes to postmortem meat tenderization through the lysosomal-mitochondrial dysfunction-induced apoptosis pathway.

This study investigated the apoptosis pathway mediated by apoptosis-inducing factors (AIF) and internal factors that influence the release of AIF. The results indicated that the AIF expression was decreased in mitochondria and increased in nucleus (P < 0.05). However, no significant differences were observed in the AIF expression in mitochondria with caspase inhibitor treatment. The optical density of nucleus and mitochondrial swelling was significant increased (P < 0.05). Reactive oxygen species (ROS) fell gradually within the first 6 h and increased in the next 24 h. Calpain I activity was decreased, Ca2+ concentration, cathepsin B and D activities was increased (P < 0.05). The results demonstrated that AIF-mediated caspase-dependent pathway was a new mitochondrial apoptosis pathway and that mitochondrial swelling, ROS content, Ca2+ concentration, calpain I, cathepsin B and cathepsin D activities are the key influencing factors in apoptosis in postmortem bovine muscle.

This study investigated the activity of adenosine monophosphate-activated protein kinase (AMPK), glycolysis, and meat quality index in three altitude bovines during postmortem aging process. Local cattle (altitude:1,500 m), Gannan yak (3,000 m), and Yushu yak (4,500 m) postmortem Longissimus Dorsi (LD) muscle were used. Results indicated that CaCl2 significantly increased the AMPK activity by increasing the calcium-regulated protein kinase kinase (CaMKKβ) activity. Besides, AMPK activation enhanced the activity of lactate dehydrogenase (LDH) and Ca2+ -ATPase and accelerated the rate of muscle maturation during postmortem aging. Moreover, the expression of HIF-1, PRKAA2, and GLUT4 genes in high-altitude Yushu yak was higher than that of low-altitude bovines. CaCl2 activates AMPK by activating CaMKKβ cascade and accelerates postmortem glycolysis affecting the intramuscular environment, color, and muscle protein degradation to accelerate postmortem muscle maturation, suggesting that AMPK has essential effects on postmortem muscle glycolysis and quality, and can regulate muscle quality by regulating postmortem muscle AMPK activity. PRACTICAL APPLICATIONS: Insufficient postmortem glycolysis usually leads to DFD (dark, firm, and dry) meat. Beef have relatively high incidences of DFD meat, which has an unattractive dark color and causes significant loss to the meat industry. Therefore, AMPK, which can regulate postmortem glycolysis to affect meat quality, is a valid research target.