scholarly journals Protein synthesis and growth in the gastrointestinal tract of the young preruminant lamb

1987 ◽  
Vol 58 (1) ◽  
pp. 159-169 ◽  
Author(s):  
D. Attaix ◽  
M. Arnal

1. In Expt 1, fractional synthesis rates (FSR) of tissue protein were measured along the gastrointestinal tract (GIT) of six 1-week-old, milk-fed lambs by using a large amount of L-[3,4(n)-3H]valine.2. In Expt 2, eighteen lambs were used to determine the fractional growth rate (FGR) of gastrointestinal tissue protein.3. FSRMinimum(Min) and FSRMaximum(Max) were calculated assuming plasma or tissue homogenate free valine specific radioactivity was representative of the valine precursor pool for protein synthesis. There were no significant differences between FSR(Min) and FSR(Max) in any gastrointestinal tissue of lambs used in Expt 1 (P > 0.05). FSR gradually and significantly (P > 0.05) increased from the oesophagus (FSR(Max)26.5%/d). reticulo-rumen (30.1%/d), omasum (41.0%/d) and abomasum (56.1%/d) to small intestine (87.5%/d), and then declined significantly (P < 0.05) towards the caecum (45.2%/d) and the colon (38.4%/d). No significant differences were observed between FSR in the duodenum, jejunum or ileum (P > 0.05).4. FGR ranged from 2,6%/d in the oesophagus to 8,7%/d in the omasum. The ratio, FGR:FSR, which reflected the efficiency of protein deposition, was at a maximum in the stomachs and caecum and at a minimum in the small intestine.5. The relative contribution of the oesophagus, stomachs, small intestine and large intestine to GIT protein synthesis was 1, 13, 76 and 10% respectively. The GIT accounted for approximately 11.5% of whole-body protein synthesis.

1989 ◽  
Vol 62 (3) ◽  
pp. 657-671 ◽  
Author(s):  
J. H. Eisemann ◽  
A. C. Hammond ◽  
T. S. Rumsey

The effect of injection with bovine somatotropin (bST) on the fractional rate of protein synthesis (FSR) in tissues of beef steers was studied using a continuous infusion of [1-14C]leucine. Minimum and maximum FSR were calculated from free leucine specific radioactivity (SRA) in plasma or tissue homogenate respectively. Tissue nucleic acid concentrations were also quantified. Tissue samples were obtained from several muscles, sections of the small intestine and liver. In response to bST, both minimum and maximum FSR increased in muscle but not liver or intestinal tissues. Absolute synthesis rate increased in several muscles and small intestine tissues. Treatment with bST increased the relative SRA of protein-bound leucine in muscles compared with liver; increased the amount of protein synthesis per unit empty body-weight (EBW) in most muscles; and increased weight of small intestine relative to EBW, suggesting a differential response between liver and the other tissues measured. Compositional changes in response to bST occurred only in muscles. DNA concentration increased while protein:DNA decreased in the gastrocnemius muscle and RNA:DNA increased in the longissimus dorsi. The maximum percentage contribution of tissue protein synthesis to whole-body protein synthesis was 12·6, 25·7 and 20·5, and 13·0, 29·4 and 25·8 for liver, muscle, and small intestine in placebo-treated and bST-injected steers respectively.


1981 ◽  
Vol 46 (3) ◽  
pp. 409-419 ◽  
Author(s):  
S. R. Davis ◽  
T. N. Barry ◽  
G. A. Hughson

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.


1988 ◽  
Vol 60 (1) ◽  
pp. 77-84 ◽  
Author(s):  
D. Attaix ◽  
E. Aurousseau ◽  
A. Manghebati ◽  
M. Arnal

1. Protein fractional synthesis rate (FSR) was measured in some major tissues and in the whole body of six 1-week-old sucking lambs by a large injection of L-[3H]valine.2. Upper estimates of tissue protein FSR (%/d), assuming that the tissue-homogenate free-valine specific radioactivity defined that of valyl tRNA, were 115.0 in liver, 24.1 in skin, 22.9 in the white M. tensor fasciae latae, 21.6 in the red M. diaphragma and 19–6 in the remainder (exsanguinated whole body without liver and gastrointestinal tract) of lambs.3. Absolute synthesis rates (ASR) of tissue protein were 17, 19 and 42 g/d in the liver, skin and skeletal muscle respectively, and 112 g/d in the remainder. The ASR of whole-body protein, derived from the tissue values, was 146 g/d, i.e. 33 g/d per kg body-weight. The calculated whole-body protein FSR was 23.9 %/d.4. The relative percentage contribution of liver, skin and skeletal muscle to whole-body protein synthesis was 11.7, 13.1, and 29.0.5. We concluded that tissue protein FSR in lambs were in exactly the same decreasing order, from visceral tissues to skeletal muscles, as observed in rats. The ovine FSR estimates and the partitioning of protein synthesis between tissues were in the same range as values recently obtained by flooding-dose experiments in immature rats, piglets, and even in chicks. These findings suggest that inter-species differences are rather limited.


1980 ◽  
Vol 43 (3) ◽  
pp. 491-502 ◽  
Author(s):  
G. E. Lobley ◽  
Vivien Milne ◽  
Joan M. Lovie ◽  
P. J. Reeds ◽  
K. Pennie

The daily rates of synthesis of protein by the whole body and by the individual tissues were determined in two Hereford × Friesian heifers (236 kg and 263 kg live weight), and a dry Friesian cow (628 kg live weight).The rate of whole-body protein synthesis (g protein/d) was estimated from the total flux through the blood of [3H]leucine and [3H]tyrosine following infusion at a constant rate for 8 h.The fractional rates of protein synthesis (ks) in the tissues (g synthesized/d per g tissue protein) were obtained after slaughter of the animals at the end of the infusion period. The fractional rate of protein synthesis was calculated assuming that the specific radioactivity of free tyrosine in either the blood (to giveks, b) or the tissue homogenate (to giveks, h) defined closely the specific radioactivity of the amino acid precursor for protein synthesis. Total protein synthesis (As, borAs, h; g/d) in an individual tissue was calculated as the product ofks, b) (orks, h) × protein content.Based on the total leucine flux, i.e. without correction for oxidation, 1.6 kg protein were synthesized daily in the heifers; for the cow this value was 2.0 kg/d.The sum of the daily total synthesis in the major tissues (muscle+bone+brain, gastrointestinal tract (GIT), liver, hide) gave values of 1.4–1.9 kg/d based onAs, b, and 2.2–3.0 kg/d based onAs, h.The percentage contributions of the individual tissues to the total protein synthesis were similar in all three animals, for example based onAs, hmuscle was 12–16; carcass (muscle+bone+brain) 32–33; GIT 38–46; liver 7–8; skin 14–21%.The contribution of muscle to total synthesis estimated from the leucine flux was 19–22%; this value is in agreement with those calculated on the same basis for other species.The energy cost of protein synthesis was estimated to account for a maximum of 30% of heat production.


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.


1980 ◽  
Vol 186 (1) ◽  
pp. 381-383 ◽  
Author(s):  
M A McNurlan ◽  
P J Garlick

The rate of protein synthesis was assessed in liver, stomach, small and large intestine and in the whole body of rats by injection of 100 mumol of [14C]leucine/100 g body wt. In each of the tissues turnover was very rapid, so that taken together they accounted for 43% of the protein synthesized by the whole animal.


1989 ◽  
Vol 257 (5) ◽  
pp. E639-E646 ◽  
Author(s):  
C. Obled ◽  
F. Barre ◽  
D. J. Millward ◽  
M. Arnal

These studies were undertaken to determine to what extent constant infusion measurements and plasma sampling could provide sensible answers for rates of whole body protein turnover and also which amino acid would be the most representative probe of whole body protein turnover. Whole body protein synthesis rates were estimated in 70-g rats with L-[U-14C]threonine, L-[U-14C]lysine, L-[U-14C]tyrosine, L-[U-14C]phenylalanine, and L-[1-14C]leucine by either simultaneous tracer infusion of four amino acids or by injections of large quantities of 14C-labeled amino acids. In the infusion experiment, indirect estimates of whole body protein turnover based on free amino acid specific radioactivity and stochastic modeling were compared with direct measurement of the incorporation of the tracer into proteins. These two methods of analysis provided similar results for each amino acid, although in each case fractional synthesis rates were lower (by between 26 and 63%) when calculations were based on plasma rather than tissue specific radioactivity. With the flooding-dose method, whole body fractional protein synthesis rates were 41.4, 25.6, 31.1, and 31.4% with threonine, lysine, phenylalanine, and leucine, respectively. These values were similar to those obtained by the continuous infusion method using tissue specific radioactivity for threonine and lysine. For leucine, however, the flooding-dose method provided an intermediate value between the two estimates derived either from the plasma or the tissue specific radioactivity in the infusion method.(ABSTRACT TRUNCATED AT 250 WORDS)


1984 ◽  
Vol 52 (2) ◽  
pp. 359-369 ◽  
Author(s):  
A. L. Schaefer ◽  
C. R. Krishnamurti

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.


2003 ◽  
Vol 284 (5) ◽  
pp. E1037-E1042 ◽  
Author(s):  
Paolo Tessari ◽  
Edward Kiwanuka ◽  
Michela Zanetti ◽  
Rocco Barazzoni

Whether phenylalanine-tyrosine (Phe-Tyr) tracers yield estimates of postprandial protein synthesis comparable to those of the widely used leucine (Leu) tracer is unclear. We measured Leu oxidation (Ox), Phe hydroxylation (Hy), and their disposal into whole body protein synthesis before and after the administration of a mixed meal (62 kJ/kg body wt, 22% of energy as protein), over 4 h in healthy subjects. Both plasma and intracellular precursor pools were used. The amino acid data were extrapolated to body protein by assuming a fixed ratio of Leu to Phe in the proteins. In the postabsorptive state, whole body protein synthesis (expressed as mg · kg−1 · min−1) was similar between Leu and Phe-Tyr tracers irrespective of the precursor pool used. After the meal, Leu Ox, Phe Hy, and body protein synthesis increased ( P ≤ 0.01 vs. basal). With the use of intracellular precursor pools, the increase of protein synthesis with Phe-Tyr (+0.51 ±0.21 mg · kg−1 · min−1) and Leu tracers (+0.57 ± 0.14) were similar ( P = not significant). In contrast, with plasma pools the increase of protein synthesis was more than twofold greater with Phe-Tyr (+1.17 ± 0.19 mg · kg−1 · min−1) than that with Leu (0.50 ± 0.13 mg · kg−1 · min−1, P < 0.01). Direct correlations were found between Leu and Ox [using both plasma and intracellular pools ( r ≤ 0.65, P ≤ 0.01)] but not between Phe and either plasma or intracellular Hy. In conclusion, 1) Phe-Tyr and Leu tracers yield comparable estimates of body protein synthesis postprandially, provided that intracellular precursor pools are used; 2) both Leu Ox and Phe Hy are stimulated by a mixed meal; 3) Phe does not correlate with Hy, which might be better related to the (unknown) portal Phe.


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