Study on the effect of CaMKKβ-mediated AMPK activation on the glycolysis and the quality of different altitude postmortem bovines longissimus 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.