scholarly journals Effect of insulin on hind-limb and whole-body leucine and protein metabolism in fed and fasted lambs

1987 ◽  
Vol 58 (3) ◽  
pp. 437-452 ◽  
Author(s):  
V. H. Oddy ◽  
D. B. Lindsay ◽  
P. J. Barker ◽  
A. J. Northrop
Keyword(s):  
Protein Synthesis ◽  
Protein Metabolism ◽  
Hind Limb ◽  
Whole Body ◽  
Limb Muscle ◽  
Body Protein ◽  
Leucine Metabolism ◽  
Hind Limb Muscle ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

1. A combination of isotope-dilution and arterio-venous difference techniques was used to determine rates of leucine metabolism and protein synthesis and degradation in a hind-limb preparation (predominantly muscle) and the whole body of eight lambs fed on milk to appetite and eight lambs fasted from 24 to 48 h.2. Compared with fed lambs, fasted lambs showed decreased rates of protein synthesis in both whole body and hind-limb, and in hind-limb muscle, elevated rates of protein degradation.3. The effects of two rates of insulin infusion on whole-body and hind-limb-muscle leucine metabolism, and in turn on protein metabolism, were determined. Insulin had no significant effect on leucine flux or oxidation (and hence protein synthesis and degradation) in whole-body or hind-limb muscle of fed lambs. In fasted lambs insulin progressively reduced arterial leucine concentration and whole-body leucine flux and oxidation, indicating a reduction in both protein synthesis and degradation. Insulin reduced the rate of leucine efflux from hind-limb muscle, which was followed by a reduction in leucine uptake. Insulin increased hind-limb-muscle glucose uptake in both fed and fasted lambs.4. On the basis that hind-limb muscle was representative of skeletal muscle in general, we estimated that muscle accounted for the same percentage (about 27) of whole-body protein synthesis in both fed and fasted lambs. This percentage was unaffected by infusion of insulin, although the absolute rates differed in fed and fasted lambs.

Human protein metabolism: its measurement and regulation

2002 ◽  
Vol 283 (6) ◽  
pp. E1105-E1112 ◽  
Author(s):  
Zhenqi Liu ◽  
Eugene J. Barrett
Keyword(s):  
Protein Synthesis ◽  
Whole Body ◽  
Body Protein ◽  
Architectural Support ◽  
Protein Mass ◽  
Protein Pool ◽  
Tracer Kinetic ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

The body's protein mass not only provides architectural support for cells but also serves vital roles in maintaining their function and survival. The whole body protein pool, as well as that of individual tissues, is determined by the balance between the processes of protein synthesis and degradation. These in turn are regulated by interactions among hormonal, nutritional, neural, inflammatory, and other influences. Prolonged changes in either the synthetic or degradative processes (or both) that cause protein wasting increase morbidity and mortality. The application of tracer kinetic methods, combined with measurements of the activity of components of the cellular signaling pathways involved in protein synthesis and degradation, affords new insights into the regulation of both protein synthesis and breakdown in vivo. These insights, including those from studies of insulin, insulin-like growth factor I, growth hormone, and amino acid-mediated regulation of muscle and whole body protein turnover, provide opportunities to develop and test therapeutic approaches with promise to minimize or prevent these adverse health consequences.

scholarly journals Contribution of whole-body protein synthesis to basal metabolism in layer and broiler chickens

1987 ◽  
Vol 57 (2) ◽  
pp. 269-277 ◽  
Author(s):  
T. Muramatsu ◽  
Y. Aoyagi ◽  
J. Okumura ◽  
I. Tasaki
Keyword(s):  
Protein Synthesis ◽  
Broiler Chickens ◽  
Whole Body ◽  
Synthesis Rate ◽  
Body Protein ◽  
Fractional Synthesis Rate ◽  
Degradation Rates ◽  
Fractional Synthesis ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

1. The effect of starvation on whole-body protein synthesis and on the contribution of protein synthesis to basal metabolic rate was investigated in young chickens (Expt 1). Strain differences between layer and broiler chickens in whole-body protein synthesis and degradation rates were examined when the birds were starved (Expt 2).2. In Expt 1, 15-d-old White Leghorn male chickens were used, while in Expt 2 Hubbard (broiler) and White Leghorn (layer) male chickens at 14 d of age were used. They were starved for 4 d, and heat production was determined by carcass analysis after 2 and 4 d of starvation. Whole-body protein synthesis rates were measured on 0, 2 and 4 d of starvation (Expt 1), and on 0 and 4 d of starvation (Expt 2).3. The results showed that starving reduced whole-body protein synthesis in terms of fractional synthesis rate and the amount synthesized. Whole-body protein degradation was increased by starvation both in terms of fractional synthesis rate and the amount degraded on a per kg body-weight basis.4. Reduced fractional synthesis rate of protein in the whole body was accounted for by reductions in both protein synthesis per unit RNA and RNA:protein ratio.5. In the fed state, whole-body protein synthesis and degradation rates, whether expressed as fractional rates or amounts per unit body-weight, tended to be higher in layer than in broiler chickens. In the starved state, the difference in the rate of protein synthesis between the two strains virtually disappeared, while the degradation rates were higher in layer than in broiler birds.6. Based on the assumed value of 3.56 kJ/g protein synthesized (Waterlow et al. 1978), the heat associated with whole-body protein synthesis in the starved state was calculated to range from 14 to 17% of the basal metabolic rate with no strain difference between layer and broiler chickens.

Protein metabolism in lambs from lines divergently selected for weaning weight

1995 ◽  
Vol 124 (1) ◽  
pp. 129-137 ◽  
Author(s):  
V. H. Oddy ◽  
P. A. Speck ◽  
H. M. Warren ◽  
P. C. Wynn
Keyword(s):  
Food Intake ◽  
Protein Degradation ◽  
Protein Metabolism ◽  
Hind Limb ◽  
Rate Of Change ◽  
Whole Body ◽  
Limb Muscle ◽  
Weaning Weight ◽  
Hind Limb Muscle ◽  
Selection For

SUMMARYThe physiological consequences of selection for weaning weight were investigated using 14-month-old castrated male Merino lambs from lines selected for (W +) and against (W – ) weight at weaning for over 10 generations. The selection experiment commenced in 1953 and was conducted at Trangie, NSW, Australia. Lambs from these lines now differ by 42% in weight at weaning and maturity, and have a proportionately similar composition of protein, fat and ash in their bodies at similar stages of maturity. In the whole body, there were no apparent between-strain differences in protein synthesis, but W + lambs had lower (P < 0·05) rates of phenylalanine oxidation than W – lambs. In hind limb muscle, protein metabolism of W + lambs was more responsive to food intake than in W – lambs. In particular, the rate of change of protein degradation differed (P < 0·05) between the lines in response to food intake per unit liveweight with protein degradation decreasing with increased feed intake in W + lambs. W + lambs had lower (P < 0·05) rates of blood flow to, and used less (P < 0·05) oxygen per kg hind limb muscle than W— lambs. Endocrine differences between the lines included increased (P < 0·05) plasma insulin-like growth factor-I (IGF-1) concentration in W + compared to W— lambs and, from regression analysis, an indication that there was a higher (P < 0·01) response in hind limb protein gain to insulin in the W + lambs.These results suggest that selection for weaning weight has altered the dynamics of protein metabolism in lambs, principally through alterations in protein breakdown in muscle. Moreover, they suggest that there are associated genetic differences in endocrine control of protein metabolism which involve insulin and possibly IGF-I.

scholarly journals New perspectives in the control of body protein metabolism

2012 ◽  
Vol 108 (S2) ◽  
pp. S94-S104 ◽  
Author(s):  
Margaret A. McNurlan
Keyword(s):  
Protein Synthesis ◽  
Translational Control ◽  
Protein Metabolism ◽  
Gene Activation ◽  
Mrna Translation ◽  
Body Protein ◽  
Control Body ◽  
Long Term Impact ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

Recent advances in elucidating the mechanisms that control body protein synthesis and degradation both expand and complicate our understanding of how these processes are regulated. This review presents an introduction to the multiple regulatory systems involved, emphasizing the number of potential controls. These include gene transcription, gene activation or suppression, activation or suppression of mRNA translation and activation or suppression of signaling pathways. The complexity of these interacting controls presents a challenge to our understanding of the overall coordinated regulation of protein synthesis and degradation and its response to any particular stimulus. Specific examples are used to illustrate regulatory mechanisms, including the ways in which protein metabolism is regulated by the amino acid leucine. In addition to regulation associated with gene expression and post-translational control, the expanding field of epigenetics adds another layer of complexity, including trans-generational responses to nutrient intake, highlighting the potential for long-term impact of nutritional experience on the metabolism of subsequent generations.

Influence of the β-adrenergic agonist cimaterol on body composition and whole body synthesis and degradation of protein in growing lambs

1992 ◽  
Vol 72 (3) ◽  
pp. 569-587 ◽  
Author(s):  
W. R. Caine ◽  
G. W. Mathison
Keyword(s):  
Body Composition ◽  
Protein Synthesis ◽  
Protein Turnover ◽  
Whole Body ◽  
Body Protein ◽  
Feeding Level ◽  
Intake Level ◽  
Psoas Major ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation

A study was undertaken to determine the effect of dietary cimaterol at low (1.1 × maintenance (M)) followed by high (2.2 × M) feed intake on body composition and protein metabolism in growing lambs fed alfalfa pellets. Control (n = 5), cimaterol I (n = 5) and cimaterol II (n = 4) lambs received rations containing cimaterol at 0, 10.9 and 0 mg kg−1 of dietary dry matter (DM) at 1.1 × M and 0, 10.9 and 10.9 mg kg−1 DM at 2.2 × M intake, respectively. On day 22 at each feeding level, whole-body protein turnover was determined as estimated from 6-h continuous infusions of 1-[14C]-leucine. Longissimus dorsi areas (P = 0.03) and the weights of psoas major, gastrocnemius (P < 0.01) and semitendinosus (P = 0.06) muscles were increased in lambs fed cimaterol throughout the experiment. There was an increase in leucine irreversible loss (P = 0.006), whole body protein synthesis (P = 0.004) and accretion (P = 0.001) at the high compared to low intake. At the low intake, protein accretion was increased (P < 0.1) from 63 g d−1 in control lambs to 94 g d−1 in cimaterol-treated lambs. No difference could be detected in whole-body protein accretion in the lambs at the high feeding level. It was concluded that cimaterol-fed lambs had higher accretion of protein in muscles than control lambs and that increases in protein accretion due to cimaterol could be detected by the radioleucine method at the low-intake level but not at the high-intake level. Large differences in estimates for protein accretion obtained from leucine metabolism, nitrogen balance and liveweight gain data suggest that refinements in techniques for estimating whole-body protein synthesis and degradation are needed. Key words: Cimaterol, lambs, protein turnover, leucine, intake, amino acids

scholarly journals Effect of food intake on hind-limb and whole-body protein metabolism in young growing sheep: chronic studies based on arterio-venous techniques

1992 ◽  
Vol 68 (2) ◽  
pp. 389-407 ◽  
Author(s):  
Patricia M. Harris ◽  
Pat A. Skene ◽  
Vivien Buchan ◽  
E. Milne ◽  
A. G. Calder ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Metabolism ◽  
Hind Limb ◽  
Live Weight ◽  
Whole Body ◽  
Acid Oxidation ◽  
Protein Loss ◽  
Body Protein ◽  
Protein Retention

Whole-body protein synthesis, estimated by the irreversible loss rate procedure, and hind-leg protein metabolism determined by arterio-venous techniques were monitored in response to three nutritional conditions (approximately 0.6, 12 and 1.8 x energy maintenance (M)) in ten wether lambs (33 kg average live weight). In all lambs and treatments measurements were based on radiolabelled phenylalanine, but the terminal procedures (five at 0.6 x M and five at 1.8 x M) also included infusion of [1-13C]leucine; this permitted comparison of amino acids catabolized (leucine) and non-metabolized (phenylalanine) by the hind-limb tissues. Whole-body protein synthesis increased with intake and the relationship with energy expenditure was slightly lower than that reported previously for pigs and cattle. The efficiency of protein retention: protein synthesis did not exceed 0.25 between the two intake extremes. Effects of intake on amino acid oxidation were similar to those observed for cattle. Hind-limb protein synthesis also increased significantly (P < 0.001) in response to intake. Estimates of protein gain, from net uptake values, indicated that the tissues made a greater proportional contribution to total protein retention above M and to protein loss below M, emphasizing the role played by muscle tissue in providing mobile protein stores. The rates of protein synthesis calculated depended on the selection of precursor (blood) metabolite, but rates based on leucine always exceeded those based on phenylalanine when precursor from the same pool was selected. The incremental efficiency of protein retained: protein synthesis was apparently unity between 0.6 and 1.2 x M but 0.3 from 1.2 to 1.8 x M. Blood flow through the iliac artery was also proportional to intake. Leucine and oxo-acid catabolism to carbon dioxide increased with intake such that the metabolic fate of the amino acid was distributed in the proportion 2:1 between protein gain and oxidation. The rates of oxidation were only 1–3% the reported capacity of the rate-limiting dehydrogenase enzyme in muscle, but sufficient enzyme activity resides in the hind-limb adipose tissue to account for such catabolism

Responses of whole body protein synthesis and degradation to plantain herb in sheep exposed to heat

2008 ◽  
Vol 62 (3) ◽  
pp. 219-229 ◽  
Author(s):  
Mohammad Al-Mamun ◽  
Yuki Hanai ◽  
Chizuru Tanaka ◽  
Yoshifumi Tamura ◽  
Hiroaki Sano
Keyword(s):  
Protein Synthesis ◽  
Whole Body ◽  
Body Protein ◽  
Protein Synthesis And Degradation ◽  
Synthesis And Degradation
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