scholarly journals Early Growth and Protein-Energy Metabolism in Chicken Lines Divergently Selected on Ultimate pH

2021 ◽  
Vol 12 ◽  
Author(s):  
Sonia Métayer-Coustard ◽  
Sophie Tesseraud ◽  
Christophe Praud ◽  
David Royer ◽  
Thierry Bordeau ◽  
...  
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Content ◽  
Muscle Growth ◽  
Breast Meat ◽  
Muscle Glycogen Content ◽  
Protein Energy ◽  
Breast Meat Yield ◽  
Lower Plasma Glucose ◽  
Slaughter Age

In chickens, a divergent selection on the Pectoralis major pHu allowed the creation of the pHu+ and pHu− lines, which represent a unique model for studying the biological control of carbohydrate storage in muscle. The present study aimed to describe the early mechanisms involved in the establishment of pHu+ and pHu− phenotypes. At hatching, pHu+ chicks were slightly heavier but exhibited lower plasma glucose and triglyceride and higher uric acid. After 5 days, pHu+ chicks exhibited higher breast meat yield compared to pHu− while their body weight was no different. At both ages, in vivo muscle glycogen content was lower in pHu+ than in pHu− muscles. The lower ability of pHu+ chicks to store carbohydrate in their muscle was associated with the increased expression of SLC2A1 and SLC2A3 genes coding glucose transporters 1 and 3, and of CS and LDHα coding key enzymes of oxidative and glycolytic pathways, respectively. Reduced muscle glycogen content at hatching of the pHu+ was concomitant with higher activation by phosphorylation of S6 kinase 1/ribosomal protein S6 pathway, known to activate protein synthesis in chicken muscle. In conclusion, differences observed in muscle at slaughter age in the pHu+ and pHu− lines are already present at hatching. They are associated with several changes related to both carbohydrate and protein metabolism, which are likely to affect their ability to use eggs or exogenous nutrients for muscle growth or energy storage.

Influence of preexercise muscle glycogen content on transcriptional activity of metabolic and myogenic genes in well-trained humans

2007 ◽  
Vol 102 (4) ◽  
pp. 1604-1611 ◽  
Author(s):  
Emmanuel G. Churchley ◽  
Vernon G. Coffey ◽  
David J. Pedersen ◽  
Anthony Shield ◽  
Kate A. Carey ◽  
...  
Keyword(s):  
Resistance Training ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Muscle Growth ◽  
Early Response ◽  
Mrna Abundance ◽  
Basal Transcription ◽  
Muscle Glycogen Content ◽  
Single Bout ◽  
Heavy Resistance Training

To determine whether preexercise muscle glycogen content influences the transcription of several early-response genes involved in the regulation of muscle growth, seven male strength-trained subjects performed one-legged cycling exercise to exhaustion to lower muscle glycogen levels (Low) in one leg compared with the leg with normal muscle glycogen (Norm) and then the following day completed a unilateral bout of resistance training (RT). Muscle biopsies from both legs were taken at rest, immediately after RT, and after 3 h of recovery. Resting glycogen content was higher in the control leg (Norm leg) than in the Low leg (435 ± 87 vs. 193 ± 29 mmol/kg dry wt; P < 0.01). RT decreased glycogen content in both legs ( P < 0.05), but postexercise values remained significantly higher in the Norm than the Low leg (312 ± 129 vs. 102 ± 34 mmol/kg dry wt; P < 0.01). GLUT4 (3-fold; P < 0.01) and glycogenin mRNA abundance (2.5-fold; not significant) were elevated at rest in the Norm leg, but such differences were abolished after exercise. Preexercise mRNA abundance of atrogenes was also higher in the Norm compared with the Low leg [atrogin: ∼14-fold, P < 0.01; RING (really interesting novel gene) finger: ∼3-fold, P < 0.05] but decreased for atrogin in Norm following RT ( P < 0.05). There were no differences in the mRNA abundance of myogenic regulatory factors and IGF-I in the Norm compared with the Low leg. Our results demonstrate that 1) low muscle glycogen content has variable effects on the basal transcription of select metabolic and myogenic genes at rest, and 2) any differences in basal transcription are completely abolished after a single bout of heavy resistance training. We conclude that commencing resistance exercise with low muscle glycogen does not enhance the activity of genes implicated in promoting hypertrophy.

Variations in chicken breast meat quality: implications of struggle and muscle glycogen content at death

2005 ◽  
Vol 46 (5) ◽  
pp. 572-579 ◽  
Author(s):  
C. Berri ◽  
M. Debut ◽  
V. Santé-Lhoutellier ◽  
C. Arnould ◽  
B. Boutten ◽  
...  
Keyword(s):  
Meat Quality ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Chicken Breast ◽  
Breast Meat ◽  
Muscle Glycogen Content ◽  
Chicken Breast Meat

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

1996 ◽  
Vol 7 (1) ◽  
pp. 52-54 ◽  
Author(s):  
P. Mariani ◽  
K. Lundström ◽  
U. Gustafsson ◽  
A. -C. Enfält ◽  
R. K. Juneja ◽  
...  
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Content ◽  
Chromosome 15 ◽  
Major Locus ◽  
Muscle Glycogen Content

Insulin promotes glycogen synthesis in the absence of GSK3 phosphorylation in skeletal muscle

2008 ◽  
Vol 294 (1) ◽  
pp. E28-E35 ◽  
Author(s):  
Michale Bouskila ◽  
Michael F. Hirshman ◽  
Jørgen Jensen ◽  
Laurie J. Goodyear ◽  
Kei Sakamoto
Keyword(s):  
Skeletal Muscle ◽  
Glucose Uptake ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Glycogen Synthase ◽  
Glycogen Synthesis ◽  
Wild Type ◽  
Muscle Glycogen Synthesis ◽  
Mutant Forms

Insulin promotes dephosphorylation and activation of glycogen synthase (GS) by inactivating glycogen synthase kinase (GSK) 3 through phosphorylation. Insulin also promotes glucose uptake and glucose 6-phosphate (G-6- P) production, which allosterically activates GS. The relative importance of these two regulatory mechanisms in the activation of GS in vivo is unknown. The aim of this study was to investigate if dephosphorylation of GS mediated via GSK3 is required for normal glycogen synthesis in skeletal muscle with insulin. We employed GSK3 knockin mice in which wild-type GSK3α and -β genes are replaced with mutant forms (GSK3α/βS21A/S21A/S9A/S9A), which are nonresponsive to insulin. Although insulin failed to promote dephosphorylation and activation of GS in GSK3α/βS21A/S21A/S9A/S9Amice, glycogen content in different muscles from these mice was similar compared with wild-type mice. Basal and epinephrine-stimulated activity of muscle glycogen phosphorylase was comparable between wild-type and GSK3 knockin mice. Incubation of isolated soleus muscle in Krebs buffer containing 5.5 mM glucose in the presence or absence of insulin revealed that the levels of G-6- P, the rate of [14C]glucose incorporation into glycogen, and an increase in total glycogen content were similar between wild-type and GSK3 knockin mice. Injection of glucose containing 2-deoxy-[3H]glucose and [14C]glucose also resulted in similar rates of muscle glucose uptake and glycogen synthesis in vivo between wild-type and GSK3 knockin mice. These results suggest that insulin-mediated inhibition of GSK3 is not a rate-limiting step in muscle glycogen synthesis in mice. This suggests that allosteric regulation of GS by G-6- P may play a key role in insulin-stimulated muscle glycogen synthesis in vivo.

1047 Effects of Training and Testosterone on Muscle Glycogen Content In Streptozotocin-Induced Diabelic Female Rats

1993 ◽  
Vol 25 (Supplement) ◽  
pp. S186
Author(s):  
H. A. Kolzer ◽  
E. van Breda ◽  
P. Geurlen ◽  
H. Kuipers ◽  
J. F.C. Glatz
Keyword(s):  
Muscle Glycogen ◽  
Glycogen Content ◽  
Female Rats ◽  
Muscle Glycogen Content

scholarly journals Relationship between changes in core body temperature in lambs and post-slaughter muscle glycogen content and dark-cutting

2014 ◽  
Vol 54 (4) ◽  
pp. 459 ◽  
Author(s):  
D. G. Pighin ◽  
W. Brown ◽  
D. M. Ferguson ◽  
A. D. Fisher ◽  
R. D. Warner
Keyword(s):  
Lactic Acid ◽  
Body Temperature ◽  
Meat Quality ◽  
Muscle Glycogen ◽  
Glycogen Content ◽  
Core Body Temperature ◽  
Correlation Coefficients ◽  
Significant Negative Correlation ◽  
Muscle Glycogen Content ◽  
Core Body

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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