Level of cottonseed meal but not frequency of feeding regulates whole-body protein synthesis and growth of sheep fed a roughage diet

2009 ◽  
Vol 49 (11) ◽  
pp. 1023
Author(s):  
L. P. Kahn ◽  
Somu B. N. Rao ◽  
J. V. Nolan

An incomplete factorial experiment was conducted to determine the effect of level and frequency of feeding of a protein-rich supplement on the growth and whole-body protein metabolism of young sheep fed a medium quality roughage diet. Cottonseed meal (CSM) was used as the protein supplement and provided at 0, 0.2 or 0.4% liveweight per day at a frequency of 1 or 3 times each week and chopped oaten (0.95) and lucerne (0.05) hay was the roughage. Growth rate more than doubled (P < 0.01) following provision of CSM but there was no advantage of feeding CSM at the highest level. Frequency of feeding CSM did not alter growth rate. Intake of hay was little affected by CSM and as a consequence the food conversion ratio declined (P < 0.01) favourably from 22 : 1 (nil CSM) to 9 : 1 as a result of supplementation. The rate of whole-body protein synthesis increased (P < 0.01) in response to the highest level of CSM with no apparent change in protein degradation, underpinning an increase (P < 0.01) in protein retention. These results highlight the role of protein supplements for promoting growth of young sheep on roughage diets and indicate that these supplements need to be provided only once a week.

2005 ◽  
Vol 80 (1) ◽  
pp. 71-81 ◽  
Author(s):  
Z. Roux

The magnitude of the discrepancy between conventional regression estimates of protein retention efficiency and theoretical estimates of synthesis efficiency indicates a major contribution ascribable to protein turn-over in the generally accepted estimates. As protein turn-over is known to be influenced by diet, feeding level and degree of maturity, this suggests the development of an estimator of protein efficiency that can be adapted for such differences. Therefore, based on generally accepted formulas for growth description, a method of estimating protein retention efficiency was developed which is flexible enough to accommodate different diets, feeding levels and degrees of maturity. Moreover, a formula was derived to convert one type of estimate to the other by regarding constant efficiency as equivalent to variable efficiency at the mid point of the estimation interval. Increase in scientific depth to this descriptive approach is provided by a theoretical consideration of a possible mechanism of hormonal control of protein synthesis and breakdown, ultimately expressed as proportionalities to powers of whole body protein (P). Molecular considerations on cellular synthesis and breakdown indicate a difference between breakdown and synthesis powers equal to (2/9)Q. The factor (2/9) is indicated by an argument based on insulinlike growth factor derived activator diffusion attributes by nucleus and body tissue geometries, whileQis equal to the proportion of nuclei activated by insulin-like growth factor. This proportion is likely to be a function of the concentration of growth factor in the blood. Hence, a linear relationship between intake and blood insulin-like growth factor concentration suggests thatQcan be represented by a scaled transformation of intake, 0 ≤Q≤ 1, such that a value ofQ= 1 represents ad libitum intake on a suitable diet andQ= 0 intake at the maintenance requirement. The quantification of breakdown and synthesis power differences by (2/9)Qleads to kP= {1 + [1 − (P/α)(2/9)Q]−1/6}−1, for turn-over related protein retention efficiency (kP), with α the limit value of P at maturity, so that 0 ≤ (P/α) ≤ 1. Experimental estimates, derived from direct estimates of whole body protein synthesis and breakdown at predetermined levels of intake, are in excellent agreement with the theoretical (2/9)Qin the power associated with (P/α) in kP. Furthermore, conventional multiple regression retention efficiencies satisfactorily approximate the turn-over related retention efficiency that can be calculated at a given level of intake for the mid point of the interval covered by the regression estimates.


1992 ◽  
Vol 68 (2) ◽  
pp. 389-407 ◽  
Author(s):  
Patricia M. Harris ◽  
Pat A. Skene ◽  
Vivien Buchan ◽  
E. Milne ◽  
A. G. Calder ◽  
...  

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


2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Shuangyao Wang ◽  
Chris G. Carter ◽  
Quinn P. Fitzgibbon ◽  
Basseer M. Codabaccus ◽  
Gregory G. Smith

AbstractThis is the first study in an aquatic ectotherm to combine a stoichiometric bioenergetic approach with an endpoint stochastic model to explore dietary macronutrient content. The combination of measuring respiratory gas (O2 and CO2) exchange, nitrogenous (ammonia and urea) excretion, specific dynamic action (SDA), metabolic energy substrate use, and whole-body protein synthesis in spiny lobster, Sagmariasus verreauxi, was examined in relation to dietary protein. Three isoenergetic feeds were formulated with varying crude protein: 40%, 50% and 60%, corresponding to CP40, CP50 and CP60 treatments, respectively. Total CO2 and ammonia excretion, SDA magnitude and coefficient, and protein synthesis in the CP60 treatment were higher compared to the CP40 treatment. These differences demonstrate dietary protein influences post-prandial energy metabolism. Metabolic use of each major energy substrate varied at different post-prandial times, indicating suitable amounts of high-quality protein with major non-protein energy-yielding nutrients, lipid and carbohydrate, are critical for lobsters. The average contribution of protein oxidation was lowest in the CP50 treatment, suggesting mechanisms underlying the most efficient retention of dietary protein and suitable dietary inclusion. This study advances understanding of how deficient and surplus dietary protein affects energy metabolism and provides approaches for fine-scale feed evaluation to support sustainable aquaculture.


1990 ◽  
Vol 52 (3) ◽  
pp. 509-514 ◽  
Author(s):  
C A Stuart ◽  
R E Shangraw ◽  
E J Peters ◽  
R R Wolfe

Author(s):  
Jorn Trommelen ◽  
Andrew M. Holwerda ◽  
Philippe J. M. Pinckaers ◽  
Luc J. C. van Loon

All human tissues are in a constant state of remodelling, regulated by the balance between tissue protein synthesis and breakdown rates. It has been well-established that protein ingestion stimulates skeletal muscle and whole-body protein synthesis. Stable isotope-labelled amino acid methodologies are commonly applied to assess the various aspects of protein metabolism in vivo in human subjects. However, to achieve a more comprehensive assessment of post-prandial protein handling in vivo in human subjects, intravenous stable isotope-labelled amino acid infusions can be combined with the ingestion of intrinsically labelled protein and the collection of blood and muscle tissue samples. The combined application of ingesting intrinsically labelled protein with continuous intravenous stable isotope-labelled amino acid infusion allows the simultaneous assessment of protein digestion and amino acid absorption kinetics (e.g. release of dietary protein-derived amino acids into the circulation), whole-body protein metabolism (whole-body protein synthesis, breakdown and oxidation rates and net protein balance) and skeletal muscle metabolism (muscle protein fractional synthesis rates and dietary protein-derived amino acid incorporation into muscle protein). The purpose of this review is to provide an overview of the various aspects of post-prandial protein handling and metabolism with a focus on insights obtained from studies that have applied intrinsically labelled protein under a variety of conditions in different populations.


1992 ◽  
Vol 122 (11) ◽  
pp. 2167-2173 ◽  
Author(s):  
Christiane Obled ◽  
Maurice Arnal

1997 ◽  
Vol 128 (2) ◽  
pp. 233-246 ◽  
Author(s):  
S. A. NEUTZE ◽  
J. M. GOODEN ◽  
V. H. ODDY

This study used an experimental model, described in a companion paper, to examine the effects of feed intake on protein turnover in the small intestine of lambs. Ten male castrate lambs (∼ 10 months old) were offered, via continuous feeders, either 400 (n = 5) or 1200 (n = 5) g/day lucerne chaff, and mean experimental liveweights were 28 and 33 kg respectively. All lambs were prepared with catheters in the cranial mesenteric vein (CMV), femoral artery (FA), jugular vein and abomasum, and a blood flow probe around the CMV. Cr-EDTA (0·139 mg Cr/ml, ∼ 0·2 ml/min) was infused abomasally for 24 h and L-[2,6-3H]phenylalanine (Phe) (420±9·35 μCi into the abomasum) and L-[U-14C]phenylalanine (49·6±3·59 μCi into the jugular vein) were also infused during the last 8 h. Blood from the CMV and FA was sampled during the isotope infusions. At the end of infusions, lambs were killed and tissue (n = 4) and digesta (n = 2) samples removed from the small intestine (SI) of each animal. Transfers of labelled and unlabelled Phe were measured between SI tissue, its lumen and blood, enabling both fractional and absolute rates of protein synthesis and gain to be estimated.Total SI mass increased significantly with feed intake (P < 0·05), although not on a liveweight basis. Fractional rates of protein gain in the SI tended to increase (P = 0·12) with feed intake; these rates were −16·2 (±13·7) and 23·3 (±15·2) % per day in lambs offered 400 and 1200 g/day respectively. Mean protein synthesis and fractional synthesis rates (FSR), calculated from the mean retention of 14C and 3H in SI tissue, were both positively affected by feed intake (0·01 < P < 0·05). The choice of free Phe pool for estimating precursor specific radioactivity (SRA) for protein synthesis had a major effect on FSR. Assuming that tissue free Phe SRA represented precursor SRA, mean FSR were 81 (±15) and 145 (±24) % per day in lambs offered 400 and 1200 g/day respectively. Corresponding estimates for free Phe SRA in the FA and CMV were 28 (±2·9) and 42 (±3·5) % per day on 400 g/day, and 61 (±2·9) and 94 (±6·0) on 1200 g/day. The correct value for protein synthesis was therefore in doubt, although indirect evidence suggested that blood SRA (either FA or CMV) may be closest to true precursor SRA. This evidence included (i) comparison with flooding dose estimates of FSR, (ii) comparison of 3H[ratio ]14C Phe SRA in free Phe pools with this ratio in SI protein, and (iii) the proportion of SI energy use associated with protein synthesis.Using the experimental model, the proportion of small intestinal protein synthesis exported was estimated as 0·13–0·27 (depending on the choice of precursor) and was unaffected by feed intake. The contribution of the small intestine to whole body protein synthesis tended to be higher in lambs offered 1200 g/day (0·21) than in those offered 400 g/day (0·13). The data obtained in this study suggested a role for the small intestine in modulating amino acid supply with changes in feed intake. At high intake (1200 g/day), the small intestine increases in mass and CMV uptake of amino acids is less than absorption from the lumen, while at low intake (400 g/day), this organ loses mass and CMV uptake of amino acids exceeds that absorbed. The implications of these findings are discussed.


1985 ◽  
Vol 226 (1) ◽  
pp. 37-42 ◽  
Author(s):  
J J Pomposelli ◽  
J D Palombo ◽  
K J Hamawy ◽  
B R Bistrian ◽  
G L Blackburn ◽  
...  

Previous studies have reported that use of a flooding dose of radiolabelled amino acid is a more precise technique than the constant infusion of tracer quantities for determining rates of protein synthesis in rapidly turning-over tissues in the rat. However, there has been little direct investigation comparing different methods under comparable conditions. Initially, 12 healthy male Sprague-Dawley rats, weighing approx. 100 g, were randomized to receive either a bolus intravenous injection of 100 mumol of L-leucine (containing 30 microCi of [1-14C]leucine)/100 g body wt., or a continuous 2 h tracer infusion of [14C]leucine. In the second phase of the experiment, 12 additional rats were intravenously injected with 1 × 10(8) colony-forming units of Pseudomonas aeruginosa and 16 h later randomized to receive one of two infusions described above. Total protein synthesis as well as fractional synthesis rates were determined in liver, rectus muscle and whole body. Synthesis rates measured in liver, muscle and whole body were significantly higher in bacteraemic rats than in healthy rats. The flooding-dose methodology gave significantly higher estimates of protein synthesis in the liver, skeletal muscle and whole body than did the continuous-infusion method using direct measurement of the acid-soluble fraction from the respective tissue. Indirect estimates of whole-body protein synthesis based on plasma enrichments and stochastic modelling gave the lowest values.


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