scholarly journals Incorporating turnover in estimates of protein retention efficiency for different body tissues

2006 ◽  
Vol 95 (2) ◽  
pp. 246-254 ◽  
Author(s):  
C. Z. Roux
Keyword(s):  
Protein Synthesis ◽  
Growth Factor ◽  
Whole Body ◽  
Muscle Fibres ◽  
Retention Efficiency ◽  
Tissue Protein ◽  
Protein Retention ◽  
Body Tissues ◽  
Breakdown Rates ◽  
The Relationship

Formulated in terms of protein synthesis (PS) and protein retention (PR), a definition of turnover-related protein retention efficiency (kP) allows the expression kP=[1+(PS/PR)/6]−1, 6 representing the ratio of the energy equivalent of protein to the cost of synthesis. By combining plausible hormonal and cellular control mechanisms of protein (P) growth, it is possible to derive (PS/PR)=[Q{(P/α)−(4/9)Y−1}]−1+1, allowing the calculation of kPby substitution. The symbol α represents the limit value of protein growth, while the term 4/9 derives from the power in the relationship between the concentration of growth factor-related activator in the nucleus and cell volume (cv). Y is the power in the relationship between cv and total tissue protein, and Q represents the proportion of growth factor-activated nuclei in a tissue. The proportion Q can be estimated from simple functions of intake rates or blood growth factor concentrations. Estimates of Y are derived from histological considerations or calculated from experimental observations; Y=1 for multinucleated skeletal muscle fibres and Y=1/3, 1/2, 1/6 on average for mononucleated cell tissues, skin or bone and viscera, respectively. To apply kPto the whole body, an average value of Y=1/2 can be taken. Experimental observations on tissue protein synthesis and breakdown rates yield direct estimates of kPin satisfactory agreement with comparable theoretical predictions.

Incorporating turn-over in whole body protein retention ef.ciency in pigs

2005 ◽  
Vol 80 (1) ◽  
pp. 71-81 ◽  
Author(s):  
Z. Roux
Keyword(s):  
Protein Synthesis ◽  
Growth Factor ◽  
Hormonal Control ◽  
Whole Body ◽  
Insulin Like Growth Factor ◽  
Retention Efficiency ◽  
Body Protein ◽  
Protein Retention ◽  
Limit Value ◽  
Turn Over

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.

Combined ingestion of protein and free leucine with carbohydrate increases postexercise muscle protein synthesis in vivo in male subjects

2005 ◽  
Vol 288 (4) ◽  
pp. E645-E653 ◽  
Author(s):  
René Koopman ◽  
Anton J. M. Wagenmakers ◽  
Ralph J. F. Manders ◽  
Antoine H. G. Zorenc ◽  
Joan M. G. Senden ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Whole Body ◽  
Vastus Lateralis Muscle ◽  
Protein Balance ◽  
Body Protein ◽  
Breakdown Rates ◽  
Postexercise Recovery ◽  
Male Subjects

The present study was designed to determine postexercise muscle protein synthesis and whole body protein balance following the combined ingestion of carbohydrate with or without protein and/or free leucine. Eight male subjects were randomly assigned to three trials in which they consumed drinks containing either carbohydrate (CHO), carbohydrate and protein (CHO+PRO), or carbohydrate, protein, and free leucine (CHO+PRO+Leu) following 45 min of resistance exercise. A primed, continuous infusion of l-[ ring-13C6]phenylalanine was applied, with blood samples and muscle biopsies collected to assess fractional synthetic rate (FSR) in the vastus lateralis muscle as well as whole body protein turnover during 6 h of postexercise recovery. Plasma insulin response was higher in the CHO+PRO+Leu compared with the CHO and CHO+PRO trials (+240 ± 19% and +77 ± 11%, respectively, P < 0.05). Whole body protein breakdown rates were lower, and whole body protein synthesis rates were higher, in the CHO+PRO and CHO+PRO+Leu trials compared with the CHO trial ( P < 0.05). Addition of leucine in the CHO+PRO+Leu trial resulted in a lower protein oxidation rate compared with the CHO+PRO trial. Protein balance was negative during recovery in the CHO trial but positive in the CHO+PRO and CHO+PRO+Leu trials. In the CHO+PRO+Leu trial, whole body net protein balance was significantly greater compared with values observed in the CHO+PRO and CHO trials ( P < 0.05). Mixed muscle FSR, measured over a 6-h period of postexercise recovery, was significantly greater in the CHO+PRO+Leu trial compared with the CHO trial (0.095 ± 0.006 vs. 0.061 ± 0.008%/h, respectively, P < 0.05), with intermediate values observed in the CHO+PRO trial (0.0820 ± 0.0104%/h). We conclude that coingestion of protein and leucine stimulates muscle protein synthesis and optimizes whole body protein balance compared with the intake of carbohydrate only.

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
Keyword(s):  
Growth Rate ◽  
Protein Synthesis ◽  
Cottonseed Meal ◽  
Whole Body ◽  
Body Protein ◽  
Protein Supplements ◽  
Protein Retention ◽  
Medium Quality ◽  
Protein Rich

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.

Enhancement of tumor proteolysis by TNF-alpha: correlation of in vivo isotope estimates with growth

1991 ◽  
Vol 261 (1) ◽  
pp. R106-R116
Author(s):  
N. W. Istfan ◽  
P. R. Ling ◽  
G. L. Blackburn ◽  
B. R. Bistrian
Keyword(s):  
Protein Synthesis ◽  
Protein Metabolism ◽  
Whole Body ◽  
Independent Effect ◽  
Yoshida Sarcoma ◽  
Protein Breakdown ◽  
Body Protein ◽  
Breakdown Rates ◽  
Made In

To evaluate the accuracy of in vivo estimates of protein synthesis and breakdown, measurements of plasma and tissue leucine kinetics were made in rat tumor tissues at different conditions of growth by use of constant intravenous infusion of [14C]leucine. These measurements were made in Yoshida sarcoma tumors on days 10 and 13 after implantation, with and without tumor necrosis factor (TNF) infusion and on day 10 in Walker-256 carcinosarcoma. Expressed as micromoles of leucine per gram tissue, tumor protein breakdown increased (P less than 0.01) from 0.32 +/- 0.02 to 0.52 +/- 0.09 (SE) mumol/h, with progress of the Yoshida sarcoma tumor between days 10 and 13 after implantation. Similarly, TNF increased tumor proteolysis on day 10 (0.43 +/- 0.03 mumol.h-1.g-1, P less than 0.05 vs. day 10 control) but not on day 13 after implantation of the Yoshida tumor. Estimates of growth derived from the difference between protein synthesis and breakdown rates were not statistically different from those based on actual tumor volume changes in both tumor models. However, estimates of “whole body” protein metabolism (plasma leucine flux) were not affected either by tumor aging or by treatment with TNF. This study shows that in vivo estimates of tissue protein metabolism based on our [14C]leucine constant infusion model closely reflect the growth characteristic of that tissue. A cytotoxic perfusion-independent effect for intravenous TNF on growing tumor tissue is demonstrable as increased protein breakdown. Furthermore, the commonly used concept of whole body protein metabolism, derived solely from tracer dilution in plasma, is an oversimplification.

Incorporating turn-over in whole body protein retention efficiency in cattle and sheep

2005 ◽  
Vol 80 (3) ◽  
pp. 345-351 ◽  
Author(s):  
C. Z. Roux
Keyword(s):  
Multiple Regression ◽  
General Rule ◽  
The Body ◽  
Whole Body ◽  
Regression Estimate ◽  
Retention Efficiency ◽  
Body Protein ◽  
Protein Retention ◽  
Limit Value ◽  
Turn Over

AbstractIn pigs the quantification of breakdown and synthesis by powers of body protein led to the estimation of turn-over related protein retention efficiency by the equation kP= {1 + [1 − (P/α)(2/9)Q]−1/6}−1, with α the limit value of whole body protein (P) maturity, so that 0 ≤(P/α)≤1. The factor 2/9 is derived from diffusion attributes indicated by cell and nucleus geometries α and Q represents a scaled transformation of intake, 0 ≤ Q ≤ 1, such that a value of Q = 1 may represent ad libitum intake and Q = 0 the intake at the maintenance requirement. Published observations on finishing steers provide estimates of whole body protein synthesis and breakdown at pre-determined levels of intake in confirmation of the theoretical (2/9)Q power associated with (P/α) inkP. Further confirmation of the (2/9)Q power in cattle follows from satisfactory agreement between an estimate of conventional multiple regression retention efficiency and the turn-over related retention efficiency calculated at the given level of intake, for the mid point of the body mass interval covered by the regression estimate. In addition, a simulation experiment on cattle from the literature gives power estimates of protein breakdown and synthesis in general agreement with those accepted for pigs. Examples on both fine and coarse diets are employed to suggest a general rule for prediction on diets causing submaximal efficiency due to suboptimal intakes.In sheep, evidence derived from estimates of conventional multiple regression efficiencies suggests that the rule (a-b) = (2/9) Q for the calculation ofkPshould be reserved for the description of compensatory growth. Protein retention efficiency for ordinary growth should be described by an adaptation of the rule derived for suboptimal intakes.

scholarly journals Comparative metabolism of L-methionine, DL-methionine and DL-2-hydroxy 4-methylthiobutanoic acid by broiler chicks

1985 ◽  
Vol 54 (3) ◽  
pp. 621-633 ◽  
Author(s):  
C. Linda Saunderson
Keyword(s):  
Protein Synthesis ◽  
Tissue Distribution ◽  
Broiler Chicks ◽  
Tissue Protein ◽  
Body Tissues ◽  
Comparative Metabolism ◽  
Liver And Kidney

1. Metabolism, in broiler chicks, of DL-2-hydroxy 4-methylthiobutanoic acid (DL-HMB), DL-methionine and L-methionine was compared in vivo using 14C-labelled tracers.2. The distribution of L-[1-14C]methionine and DL-[1-14C]HMB in the major body tissues was examined for a period of 120 min after administration.3. The relative oxidation (14CO2, exhaled), excretion and incorporation into tissue protein of L-[l-14C]methionine, DL-[l-14C]methionine and DL-[1-14C]HMB were measured in fed birds.4. Tissue distribution of L-[1-14C]methionine and DL-[1-14C]HMB differed during 60–90 min following administration.5. The production of 14CO2, from each of the tracers was similar but excretion of 14C-labelled material was very different with the greatest excretion from DL-[1-14C]HMB and the least from L[1-14C]methionine.6. The incorporation of 14C into tissue proteins varied with the tracer given and the tissue examined. Liver and kidney had equivalent incorporation from each of the tracers while other tissues examined showed lower incorporation from DL-[1-14C]methionine and DL-[1-14C]HMB.7. The results show that DL-HMB, D-methionine and L-methionine are metabolized differently in vivo and that they are excreted in differing proportions. There is also a difference in the ability of each to act as a precursor for protein synthesis in tissues other than liver.

scholarly journals Protein synthesis in tissues of growing lambs

1981 ◽  
Vol 46 (3) ◽  
pp. 409-419 ◽  
Author(s):  
S. R. Davis ◽  
T. N. Barry ◽  
G. A. Hughson
Keyword(s):  
Protein Synthesis ◽  
Cardiac Muscle ◽  
Specific Radioactivity ◽  
Biceps Femoris ◽  
Whole Body ◽  
Tissue Homogenate ◽  
Body Protein ◽  
Tissue Protein ◽  
Biceps Femoris Muscle ◽  
Plasma Leucine

1. The fractional rate of protein synthesis (FSR) in tissues of nine growing lambs (4–5 months of age) was estimated following continuous infusion of L-[4,5–3H]leucine for a period of 7 h. Minimum and upper estimates of FSR were obtained assuming that the specific radioactivity (SRA) of leucine in blood plasma and tissue homogenate respectively defined that of leucyl tRNA.2. Mean upper estimates of tissue protein FSR (/d) were skin 0·35, longissimus dorsi muscle 0·05, biceps femoris muscle 0·04, liver 0·54, rumen 0·79, cardiac muscle 0·09. Minimum estimates of tissue protein FSR ranged from 0·03 (muscle) to 0·15 (liver).3. Plasma leucine flux was closely related to body protein content and dietary leucine absorption (r 0·94).4. The rate of whole-body protein synthesis (WBS) derived from plasma leucine flux corrected for oxidation and localized recycling of leucine into protein was similar to that calculated from the sum of daily protein synthesis in individual tissues using the upper estimate of FSR, i.e. 610 g/d v. 581 g/d.5. The estimate of WBS derived from plasma leucine flux directly (241 g/d) was similar to that calculated from the sum of minimum estimates of daily protein synthesis in individual tissues (214 g/d).6. The ratio, intracellular leucine SRA:plasma leucine SRA tended to increase with increasing dietary leucine absorption in all tissues although these factors were only significantly correlated (P < 0·05) in cardiac muscle, skin and rumen. Such relationships suggest an increased exchange of plasma leucine with intracellular leucine with increased food intake.7. It was estimated that the energy cost of protein synthesis accounted for approximately 42% of daily heat production.

scholarly journals Whole body and tissue fractional protein synthesis in the ovine fetusin utero

1984 ◽  
Vol 52 (2) ◽  
pp. 359-369 ◽  
Author(s):  
A. L. Schaefer ◽  
C. R. Krishnamurti
Keyword(s):  
Protein Synthesis ◽  
Activity Ratio ◽  
Specific Activity ◽  
Whole Body ◽  
Absolute Rate ◽  
Body Protein ◽  
Tissue Protein ◽  
Fractional Rate ◽  
Tyrosine Concentration

1. Whole-body and tissue fractional protein synthesis rates were determined in chronically-catheterized ovine fetuses at 120–130 d of gestation following an 8 h continuous infusion of L-[U-14C]-or L-[2, 3, 5, 6-3H]tyrosine.2. From the net utilization of tyrosine by the fetus, corrected for apparent oxidation, and tyrosine concentration in the fetal carcass protein, whole-body protein synthesis was estimated to be 63 g/d per kg.3. Following 8 h of infusion of labelled tyrosine the ewes were killed and fetal tissues were removed for the determination of tyrosine specific activity. The fractional rate of protein synthesis (k3) was calculated from the specific activity ratio, protein bound: intracellular free tyrosine. Tissue k, values for the liver, kidney, lungs, brain, skeletal muscle and small intestine were 78, 45, 65, 37, 26 and 93% /d respectively.4. The absolute rate of synthesis was calculated by multiplying the tissue protein content by k2. Muscles, gastrointestinal tract, liver and lungs contributed approximately 20.5, 20.5, 14.4 and 9.4% respectively to whole- body protein synthesis.5. The efficiency of protein synthesis as expressed by the RNA activity was higher in liver, lung and brain followed by kidney, skeletal and cardiac muscle.

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