Role of beta-adrenoceptor signaling and AMP-activated protein kinase in glycolysis of postmortem skeletal muscle.
Postmortem glycolysis is directly linked to the incidences of PSE (pale, soft, and exudative) and DFD (dark, firm, and dry) meats, which cause significant economic loss to the meat industry. However, mechanisms controlling postmortem glycolysis are unclear. The objective of this study was to determine the role of beta-adrenoceptor signaling and AMP-activated protein kinase (AMPK) in postmortem glycolysis. Eighteen 2 month old C57BL/6J female mice were randomly separated into three groups. Group I received an intraperitoneal injection of saline solution only and served as the control; group II received a saline injection and then were forced to swim for 1 min; and group III received an injection of propranolol (1 mg/kg) in saline. In addition, six C57BL/6J female AMPK knockout mice were assigned to group IV, which received a saline injection and were forced to swim for 1 min. The longissimus dorsi muscle was sampled at 0, 1, and 24 h postmortem for pH and enzyme activity measurements. The objective is to elucidate the roles of beta-adrenoceptor signaling and AMPK in the glycolysis of postmortem muscle. Results showed that AMPK activity had a major role in determining the ultimate muscle pH, with an ultimate pH for control mice of 6.16 and AMPK knockout mice of 6.48. The beta-adrenoceptor signaling is essential for initial rapid glycolysis. Blocking beta-adrenoceptor signaling prevented the initial pH decline induced by stress. Activation of beta-adrenoceptor signaling due to preslaughter stress activates glycogen phosphorylase, resulting in a rapid glycolysis shortly after slaughter. On the other hand, the activation of AMPK is important for maintaining the activity of glycogen phosphorylase and pyruvate kinase, leading to a sustained glycolysis and a low ultimate pH.
Du
Min
M
Department of Animal Science, University of Wyoming, Laramie, Wyoming 82071, USA. mindu@uwyo.edu
Shen
Qingwu W
QW
Zhu
Mei J
MJ
D055372:AMP-Activated Protein Kinases; D000818:Animals; D005260:Female; D024981:Glycogen Phosphorylase / Q000378:metabolism; D006019:Glycolysis; D006863:Hydrogen-Ion Concentration; D051379:Mice; D008810:Mice, Inbred C57BL; D018345:Mice, Knockout; D009097:Multienzyme Complexes / Q000172:deficiency / Q000502:physiology*; D018482:Muscle, Skeletal / Q000502:physiology*; D011180:Postmortem Changes; D017346:Protein Serine-Threonine Kinases / Q000172:deficiency / Q000502:physiology*; D011770:Pyruvate Kinase / Q000378:metabolism; D011943:Receptors, Adrenergic, beta / Q000502:physiology*; D015398:Signal Transduction
D009097:Multienzyme Complexes; D011943:Receptors, Adrenergic, beta; D024981:Glycogen Phosphorylase; D011770:Pyruvate Kinase; D017346:Protein Serine-Threonine Kinases; D055372:AMP-Activated Protein Kinases