AMP-activated protein kinase (AMPK) α2 subunit mediates glycolysis in postmortem skeletal muscle

Liang, Junfang; Yang, Qiyuan; Zhu, Mei‐Jun; Jin, Yufeng; Du, Min

doi:10.1016/j.meatsci.2013.05.025

Cited by 23 publications

(11 citation statements)

References 51 publications

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“…In this study, we obtained four times the activity of AMPK in the carcasses with normal muscle pH compared to those with high muscle pH, without variation in time. These results would indicate that this enzyme participates actively in the postmortem early glycolysis, in a similar way to that observed in AMPK knockout mice for 2-alpha way (Liang et al, 2013), which show reduced glycogen content, postmortem pH decline and the lactate generation. Many kinetic effects occurring in enzymes such as AMPK are altered by pre and postmortem factors that are still unknown, so further studies are needed in this regard (Ferguson & Gerrard, 2014).…”

Section: Muscle Enzyme Activities According To Ph Categorization and supporting

confidence: 74%

“…This situation is different in cattle, since it has been demonstrated that the GDE activity in cattle is lower than in pigs, measured in L. dorsi (Ylä-Ajos, Ruusunen, & Puolanne, 2006). Also, according to the results obtained by Du et al (2005) and Liang, Yang, Zhuc, Jina, and Du (2013) on AMPK knockout mice, using also mice with β-adrenergic blockers and subjected to exercise, when compared with normal rats, AMPK would participate from the start of the postmortem anaerobic glycolysis and would have direct effect on the final muscle pH 24 (higher) in AMPK knockout mice subjected to exercise. Other authors argue that activated AMPK can impact glycolysis in two ways.…”

Section: Muscle Enzyme Activities According To Ph Categorization and mentioning

confidence: 95%

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Glycolytic potential and activity of adenosine monophosphate kinase (AMPK), glycogen phosphorylase (GP) and glycogen debranching enzyme (GDE) in steer carcasses with normal (<5.8) or high (>5.9) 24h pH determined in M. longissimus dorsi

et al. 2015

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Section: Muscle Enzyme Activities According To Ph Categorization and supporting

confidence: 74%

Section: Muscle Enzyme Activities According To Ph Categorization and mentioning

confidence: 95%

Glycolytic potential and activity of adenosine monophosphate kinase (AMPK), glycogen phosphorylase (GP) and glycogen debranching enzyme (GDE) in steer carcasses with normal (<5.8) or high (>5.9) 24h pH determined in M. longissimus dorsi

et al. 2015

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“…AMPK is well-known a serine/threonine kinase and a heterotrimeric protein complex consisting α, β, and γ subunits that play a key role in cellular energy homeostasis as well as one of a major regulator of post-mortem glycolysis in porcine muscle [31, 32]. Rapid alteration of AMPKα2 protein expression has been reported that was almost disappeared within 24 h post-mortem in mouse muscle [33]. We demonstrated that the expressions of GS, GSK-3β, and AMPKα were rapidly degraded within 24–36 h post-mortem and disappeared completely 48 h post-mortem (Fig 1).…”

Section: Discussionmentioning

confidence: 99%

Degradation of Kidney and Psoas Muscle Proteins as Indicators of Post-Mortem Interval in a Rat Model, with Use of Lateral Flow Technology

et al. 2016

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We investigated potential protein markers of post-mortem interval (PMI) using rat kidney and psoas muscle. Tissue samples were taken at 12 h intervals for up to 96 h after death by suffocation. Expression levels of eight soluble proteins were analyzed by Western blotting. Degradation patterns of selected proteins were clearly divided into three groups: short-term, mid-term, and long-term PMI markers based on the half maximum intensity of intact protein expression. In kidney, glycogen synthase (GS) and glycogen synthase kinase-3β were degraded completely within 48 h making them short-term PMI markers. AMP-activated protein kinase α, caspase 3 and GS were short-term PMI markers in psoas muscle. Glyceraldehyde 3-phosphate dehydrogenase (GAPDH) was a mid-term PMI marker in both tissues. Expression levels of the typical long-term PMI markers, p53 and β-catenin, were constant for at least 96 h post-mortem in both tissues. The degradation patterns of GS and caspase-3 were verified by immunohistochemistry in both tissues. GAPDH was chosen as a test PMI protein to perform a lateral flow assay (LFA). The presence of recombinant GAPDH was clearly detected in LFA and quantified in a concentration-dependent manner. These results suggest that LFA might be used to estimate PMI at a crime scene.

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“…Energy metabolism, especially glycolysis, is an important way of these changes. These changes directly affect the quality of meat, such as pH, water retention, color, and tenderness (Liang, Yang, Zhu, Jin, & Du, ; Sambandam & Lopaschuk, ). The degree of energy metabolism and pH drop after slaughter affects the quality characteristics of meat (Men, Deng, Tao, Qi, & Xiu, ; Scheffler, Kasten, England, Scheffler, & Gerrard, ).…”

Section: Introductionmentioning

confidence: 99%

Study on the effect of CaMKKβ‐mediated AMPK activation on the glycolysis and the quality of different altitude postmortem bovineslongissimusmuscle

et al. 2019

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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.

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AMP-activated protein kinase (AMPK) α2 subunit mediates glycolysis in postmortem skeletal muscle

Cited by 23 publications

References 51 publications

Glycolytic potential and activity of adenosine monophosphate kinase (AMPK), glycogen phosphorylase (GP) and glycogen debranching enzyme (GDE) in steer carcasses with normal (<5.8) or high (>5.9) 24h pH determined in M. longissimus dorsi

Glycolytic potential and activity of adenosine monophosphate kinase (AMPK), glycogen phosphorylase (GP) and glycogen debranching enzyme (GDE) in steer carcasses with normal (<5.8) or high (>5.9) 24h pH determined in M. longissimus dorsi

Degradation of Kidney and Psoas Muscle Proteins as Indicators of Post-Mortem Interval in a Rat Model, with Use of Lateral Flow Technology

Study on the effect of CaMKKβ‐mediated AMPK activation on the glycolysis and the quality of different altitude postmortem bovineslongissimusmuscle

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