A major locus (RN) affecting muscle glycogen content is located on pig Chromosome 15

Pre-slaughter stress may decrease muscle glycogen content, a key element for a suitable low ultimate pH and prevention of dark-cutting meat. Body temperature monitoring is a tool used in research on animal stress, as an indicator of stress events. Possible relationships between body temperature of sheep and post-mortem muscle glycogen were investigated in this study. Body temperature was measured with intravaginal loggers inserted into each animal at 3 days pre-slaughter, to record body temperature every 3 min over a period of 3 days. Blood samples were collected from each animal at exsanguination for measurement of glucose and lactic acid concentrations. The muscle content of glycogen and lactic acid were determined in samples of M. longissimus collected at the level of the 13th rib, at 1 h post-slaughter. A plot of body temperature versus time showed a rise in body temperature from all animals during events such as mustering, loading onto the truck, unloading at the abattoir, during pre-slaughter handling and at slaughter. Pearson’s correlation coefficients were determined between (1) the main temperature increments occurring between farm and slaughter; and (2) post-slaughter muscle glycogen and lactate levels. A significant negative correlation was detected between elevation in core body temperature due to physical stress of sheep and muscle glycogen levels at slaughter. A low correlation was detected between body temperature and blood glucose or lactate concentrations. Further research should examine the relationship between core body temperature and meat quality in order to better understand the complex relationship between animal stress and meat quality.

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Progressive increase in human skeletal muscle AMPKα2 activity and ACC phosphorylation during exercise

AJP Endocrinology and Metabolism ◽

10.1152/ajpendo.00101.2001 ◽

2002 ◽

Vol 282 (3) ◽

pp. E688-E694 ◽

Cited By ~ 95

Author(s):

T. J. Stephens ◽

Z.-P. Chen ◽

B. J. Canny ◽

B. J. Michell ◽

B. E. Kemp ◽

...

Keyword(s):

Skeletal Muscle ◽

Muscle Glycogen ◽

Human Skeletal Muscle ◽

Glycogen Content ◽

Vastus Lateralis ◽

Moderate Intensity ◽

Moderate Intensity Exercise ◽

Western Blots ◽

Muscle Glycogen Content ◽

Muscle Creatine

The effect of prolonged moderate-intensity exercise on human skeletal muscle AMP-activated protein kinase (AMPK)α1 and -α2 activity and acetyl-CoA carboxylase (ACCβ) and neuronal nitric oxide synthase (nNOSμ) phosphorylation was investigated. Seven active healthy individuals cycled for 30 min at a workload requiring 62.8 ± 1.3% of peak O2consumption (V˙o 2 peak) with muscle biopsies obtained from the vastus lateralis at rest and at 5 and 30 min of exercise. AMPKα1 activity was not altered by exercise; however, AMPKα2 activity was significantly ( P < 0.05) elevated after 5 min (∼2-fold), and further elevated ( P < 0.05) after 30 min (∼3-fold) of exercise. ACCβ phosphorylation was increased ( P < 0.05) after 5 min (∼18-fold compared with rest) and increased ( P< 0.05) further after 30 min of exercise (∼36-fold compared with rest). Increases in AMPKα2 activity were significantly correlated with both increases in ACCβ phosphorylation and reductions in muscle glycogen content. Fat oxidation tended ( P = 0.058) to increase progressively during exercise. Muscle creatine phosphate was lower ( P < 0.05), and muscle creatine, calculated free AMP, and free AMP-to-ATP ratio were higher ( P < 0.05) at both 5 and 30 min of exercise compared with those at rest. At 30 min of exercise, the values of these metabolites were not significantly different from those at 5 min of exercise. Phosphorylation of nNOSμ was variable, and despite the mean doubling with exercise, statistically significance was not achieved ( P = 0.304). Western blots indicated that AMPKα2 was associated with both nNOSμ and ACCβ consistent with them both being substrates of AMPKα2 in vivo. In conclusion, AMPKα2 activity and ACCβ phosphorylation increase progressively during moderate exercise at ∼60% of V˙o 2 peak in humans, with these responses more closely coupled to muscle glycogen content than muscle AMP/ATP ratio.

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