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.

Interactions of deoxynivalenol and lipopolysaccharides on tissue protein synthesis in pigs

2013 ◽  
Vol 6 (2) ◽  
pp. 185-197 ◽  
Author(s):  
K. Kullik ◽  
B. Brosig ◽  
S. Kersten ◽  
H. Valenta ◽  
A.-K. Diesing ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Small Intestine ◽  
Control Diet ◽  
Live Weight ◽  
The Body ◽  
Tissue Protein ◽  
Fusarium Toxin ◽  
Synthesis Parameters ◽  
Tissue Protein Synthesis

Possible interactions between the Fusarium toxin deoxynivalenol and lipopolysaccharides on in vivo protein synthesis were investigated in selected porcine tissues. A total of 36 male castrated pigs (initial weight of 26 kg) were used. 24 pigs were fed a control diet and 12 a Fusarium-contaminated diet (chronic oral deoxynivalenol, 3.1 mg/kg diet) for 37 days. Tissue protein synthesis was measured in pigs fed control diet after intravenous infusion of deoxynivalenol (100 µg/kg live weight/h), lipopolysaccharides (7.5 µg/kg live weight/h) or a combination of both compounds on the day of the measurements, while six pigs from the chronic oral deoxynivalenol group were intravenously treated with lipopolysaccharides (7.5 µg/kg live weight/h). Deoxynivalenol challenge alone failed to alter protein synthesis parameters. Fractional protein synthesis rates were exclusively reduced in liver, spleen and small intestine of lipopolysaccharides-treated pigs. Intravenous deoxynivalenol co-exposure enhanced the impacts of lipopolysaccharides on protein synthesis parameters in the spleen and the small intestine to some extent, while a chronic oral pre-exposure with deoxynivalenol relieved its effects in the spleen. Whether these interactions occur in other tissues and under other study conditions, especially toxin doses and route of entry into the body, needs to be examined further.

scholarly journals Dietary lysine deficiency greatly affects muscle and liver protein turnover in growing chickens

1996 ◽  
Vol 75 (6) ◽  
pp. 853-865 ◽  
Author(s):  
S. Tesseraud ◽  
R. Peresson ◽  
J. Lopes ◽  
A.M. Chagneau
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Pectoralis Major Muscle ◽  
Pectoralis Major ◽  
Translational Efficiency ◽  
Liver Protein ◽  
Deficient Diet ◽  
Principal Mechanism ◽  
Tissue Protein

We analysed the respective influences of age and lysine deficiency on skeletal muscle and liver protein turnover. Growing male broilers were fed ad libirum on isoenergetic diets containing 2OO g crude protein/kg which varied in their lysine content (7·7 or 10·1 g/kg). Fractional rates of protein synthesis (FSR) were measured in vivo in the liver and the pectoralis major muscle of 2-, 3- and 4-week-old chickens (flooding dose of l-[143H]phenylalanine). Fractional rates of proteolysis (FBR) were estimated for the same tissues as the difference between synthesis and growth. Over the 2-week period liver FSR and FBR were unchanged, whereas muscle FSR decreased with age. This developmental decline was related to the lower capacity for protein synthesis (Cs) without any modifications of the translational efficiency. Whatever the age, lysine deficiency resulted in significant decreases in body weight, tissue protein content and tissue protein deposition, apparently because of reduced amounts of proteins synthesized. We recorded a difference in the response of the two tissues to lysine deficiency, the pectoralis major being more sensitive than the liver. When comparing birds of the same age, liver FSR and FBR were not modified by the diet, where as muscle FSR, Cs and FBR were higher in chicks fed on a lysinc-deficient diet than in the controls. Conversely, when chicks of similar weights were compared, the main effect of the dietary deficiency was an increase in muscle FBR. The results suggest that lysine deficiency not only delayed chick development so that protein turnover was affected, but also induced greater changes in metabolism. Thus, the principal mechanism whereby muscle mass decreased appeared to be a change in FBR.

Conditions that alter rates of tissue protein synthesis in vivo

1980 ◽  
Vol 8 (3) ◽  
pp. 283-285 ◽  
Author(s):  
MARGARET A. McNURLAN ◽  
VIRGINIA M. PAIN ◽  
PETER J. GARLICK
Keyword(s):  
Protein Synthesis ◽  
Tissue Protein ◽  
Tissue Protein Synthesis

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.

Protein synthesis in pulmonary arteries from rats exposed to hyperoxia

1993 ◽  
Vol 264 (1) ◽  
pp. L74-L79
Author(s):  
W. S. Stirewalt ◽  
J. T. Coflesky ◽  
L. H. Young ◽  
J. N. Evans
Keyword(s):  
Protein Synthesis ◽  
Soluble Protein ◽  
Growth Response ◽  
Pulmonary Arteries ◽  
Protein Fractions ◽  
Tissue Protein ◽  
Fractional Rate ◽  
Fractional Synthesis

These studies were undertaken to determine the relationship of early changes in the synthesis rates and contents of collagen, elastin, and soluble tissue protein of pulmonary arteries in rats exposed chronically to normobaric hyperoxia. The growth response of pulmonary arteries was characterized by proportionate increases in the contents of the three protein fractions after 7 days (130% of control) and 21 days (194% of control) of exposure. Fractional rates of protein synthesis were assessed both in vivo and in vitro with the use of several radiolabeled amino acids as tracers to minimize uncertainties of the relationships of the specific radioactivities of measured amino acid pools and the precursors for the proteins fractions. Values for fractional synthesis rates of collagen, elastin, and soluble protein in vitro in pulmonary arteries isolated from control rats were 2.2, 1.6, and 19%/day, respectively. Rates of synthesis of collagen and soluble protein in vitro were approximately 20% lower than that determined in control rats in vivo. The fractional synthesis rates of the three protein fractions in isolated arteries from experimental rats were unchanged after 1 day of hyperoxic exposure, decreased marginally after 3 days, and markedly increased after 7 days. At this time the absolute increments in the fractional synthesis rates of collagen (+4.7%/day) and elastin (+5.0%/day) were less than that of soluble tissue protein (+16%/day) and were more comparable to the accumulation rate of proteins in the tissue. The disproportionate increment in the fractional rate of soluble protein synthesis suggests that the fractional rate of degradation of soluble protein was also increased during the growth response in this model of hypertension.

Intrauterine growth restriction does not alter response of protein synthesis to feeding in newborn pigs

1997 ◽  
Vol 272 (5) ◽  
pp. E877-E884 ◽  
Author(s):  
T. A. Davis ◽  
M. L. Fiorotto ◽  
D. G. Burrin ◽  
W. G. Pond ◽  
H. V. Nguyen
Keyword(s):  
Protein Synthesis ◽  
Intrauterine Growth Restriction ◽  
Plasma Insulin ◽  
Growth Restriction ◽  
Tissue Protein ◽  
Intrauterine Growth ◽  
Igf I ◽  
Tissue Protein Synthesis ◽  
Newborn Pigs

This study aimed to determine the effect of intrauterine growth restriction (IUGR) on the acute response of tissue protein synthesis to feeding in newborn pigs. Newborn pigs of sows fed either control or protein-restricted diets throughout gestation were designated C or IUGR, respectively. Both groups were either fasted for 9 h after birth or fed hourly 30 ml colostrum/kg body wt for 2.75 h after a 6-h fast. Fractional rates of tissue protein synthesis (Ks) were measured in vivo with a flooding dose of L-[4-3H]phenylalanine. Birth weight was reduced by 33% in IUGR pigs. IUGR had no effect on Ks in skeletal muscles, heart, liver, jejunum, or pancreas. Feeding stimulated tissue Ks similarly in C and IUGR pigs. Fasting plasma insulin concentrations and their rise with feeding were unaffected by IUGR. Plasma insulin-like growth factor I (IGF-I) concentrations were reduced by 42% in IUGR pigs and were not altered by feeding in either IUGR or C pigs. There were positive nonlinear relationships between tissue Ks and circulating concentrations of insulin. The results indicate that, in newborn pigs, tissue Ks are unaffected by IUGR, despite reduced plasma IGF-I concentrations. The efficiency with which nutrients stimulate tissue Ks is also not altered by IUGR, perhaps because the rise in plasma insulin concentrations with feeding is unaffected by IUGR.

Whole-body and tissue protein synthesis during brief and prolonged fasting in the rat

1991 ◽  
Vol 81 (5) ◽  
pp. 611-619 ◽  
Author(s):  
Yves Cherel ◽  
Didier Attaix ◽  
Danuta Rosolowska-Huszcz ◽  
Rajae Belkhou ◽  
Jean-Patrice Robin ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Skeletal Muscles ◽  
Whole Body ◽  
Protein Loss ◽  
Body Protein ◽  
Tissue Protein ◽  
Control Value ◽  
Tissue Protein Synthesis ◽  
Fractional Synthesis

1. Little information is currently available on protein turnover during chronic protein loss situations. We have thus measured the whole-body and tissue protein fractional synthesis rates (ks), the whole-body fractional protein degradation rate (kd), the capacity for protein synthesis (Cs) and the efficiency of protein synthesis (kRNA) in vivo in fed and fasted (1, 5 and about 9 days) 400 g rats. 2. One day of starvation resulted in a reduced ks and an increased kd in the whole body. ks was selectively depressed in skeletal muscles, mainly owing to a reduced kRNA, and was not modified in heart, liver and skin. The contribution of skin to whole-body protein synthesis increased by 39%. 3. During the phase of protein sparing (5 days of fasting), kd in the whole body decreased below the control fed level. ks in skeletal muscles was sustained because kRNA was restored to 82–98% of the control value. 4. Rats were in a protein-wasting phase after 9 days of starvation. kd in the whole body did not increase and was actually 78% of the value observed in fed animals. By contrast, ks in the whole body and tissues decreased to 14–34% of the control values, owing to reductions in both Cs and kRNA. Whatever the duration of the fast, the contribution of the skin to whole-body protein synthesis largely exceeded that of skeletal muscle. 5. The present findings suggest that the main goal in the treatment of chronic protein loss should be to sustain protein synthesis. Our data also emphasize the importance of skin in whole-body protein synthesis in fasting and possibly in other protein loss situations.

scholarly journals Occurrence of ornithine decarboxylase and polyamines in cartilage

1977 ◽  
Vol 162 (2) ◽  
pp. 347-350 ◽  
Author(s):  
P D Conroy ◽  
D M Simms ◽  
J J Pointon
Keyword(s):  
Chick Embryo ◽  
Ornithine Decarboxylase ◽  
Costal Cartilage ◽  
Decarboxylase Activity ◽  
Ph Optimum ◽  
Tissue Protein ◽  
Ornithine Decarboxylase Activity ◽  
Body Tissues ◽  
Human Foetuses

The activity of ornithine decarboxylase was investigated in cartilage from chick embryos, rabbits, rats and human foetuses. The enzyme activity in these cartilages was of the same order as the detected in other body tissues. Ornithine decarboxylase activity in chick-embryo cartilage and liver was the same when compared on the basis of total soluble tissue protein. The cartilage enzyme exhibited a pH optimum of 6.5 and a Km for ornithine of 0.16mM. Ornithine decarboxylase activity in chick-embryo pelvic leaflets was maintained at the value in vivo for up to 22h when the isolated tissue was incubated in a modified Waymouth's medium (MB 752/1) at 37 degrees C. After addition of cycloheximide to the incubation medium, ornithine decarboxylase activity declined, with a half-life of 40 min. The concentrations of the polyamines spermidine and spermine in chick-embryo pelvic cartilage and rabbit costal cartilage were of the same order as the concentrations detected in other tissues.

scholarly journals The effects of fasting or hypoxia on rates of protein synthesis in vivo in subcellular fractions of rat heart and gastrocnemius muscle

1989 ◽  
Vol 257 (2) ◽  
pp. 519-527 ◽  
Author(s):  
V R Preedy ◽  
P H Sugden
Keyword(s):  
Protein Synthesis ◽  
Subcellular Fractions ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Tissue Protein ◽  
Moderate Hypoxia ◽  
Hypoxic Conditions ◽  
Rate Ratios ◽  
H Protein

We measured rates of protein synthesis in vivo in subcellular fractions (soluble, myofibrillar and stromal fractions) of the heart and the gastrocnemius from rats after fasting or under hypoxic conditions (i.e. atmospheres containing 5% or 10% O2). Such interventions are known to inhibit protein synthesis under some circumstances. The recovery of tissue protein after fractionation was 80-100%. The proportions of protein present in the soluble and stromal fractions were different in the two muscles. The rates of protein synthesis in the myofibrillar and stromal fractions were less than those for total mixed tissue protein, whereas the rate for soluble protein was greater. Both fasting and moderate hypoxia (10% O2 for 24 h) inhibited protein synthesis in the gastrocnemius. In this tissue, the synthesis of the myofibrillar fraction was apparently the most sensitive to inhibition, and this resulted in some significant increases in the soluble-fraction/myofibrillar-fraction protein-synthesis rate ratios. In the heart, fasting inhibited protein synthesis, but moderate hypoxia (10% O2 for 24 h) did not. The rate of protein synthesis in the cardiac myofibrillar fraction was again more sensitive to fasting than were the rates in the other fractions, but it was not as sensitive as that in the gastrocnemius. Under severely hypoxic conditions (5% O2 for 1 or 2 h), protein synthesis was decreased in all fractions in both tissues. These results suggest that the rates of protein synthesis in these relatively crude subcellular fractions vary.

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