Anaesthetic Agents and Their Effect on Tissue Protein Synthesis in the Rat

1989 ◽  
Vol 77 (6) ◽  
pp. 651-655 ◽  
Author(s):  
S. D. Heys ◽  
A. C. Norton ◽  
C. R. Dundas ◽  
O. Eremin ◽  
K. Ferguson ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Young Male ◽  
Male Rats ◽  
Liver Protein ◽  
Arterial Blood Gas ◽  
Anaesthetic Agents ◽  
Arterial Blood ◽  
Tissue Protein Synthesis

1. Rates of protein synthesis were measured, in vivo, in lung, liver, heart and skeletal muscle of young male rats. Groups of rats were exposed for 1 h duration to one of the following anaesthetic regimens: 1.4% halothane, 2.2% halothane, 1.4% halothane in 66% nitrous oxide, intravenous pentobarbitone (20 mg/kg) and intravenous midazolam (18 mg/kg) combined with fentanyl (2 μg/kg). Fractional rates of protein synthesis were determined by injecting [3H]phenylalanine (150 μmol/100 g body weight) 2. Liver protein synthesis was depressed significantly by all regimens, except midazolam/fentanyl, by up to 37.7% of control values. Lung protein synthesis was significantly reduced by all the anaesthetic agents by up to 30% of control rates 3. The effects of the anaesthetic agents on skeletal muscle and heart were small and not statistically significant 4. There was no evidence of ventilatory depression as manifested by changes in arterial blood gas partial pressures of CO2 and O2, except in the group treated with 2.2% halothane.

scholarly journals Acute IGF-I infusion stimulates protein synthesis in skeletal muscle and other tissues of neonatal pigs

2002 ◽  
Vol 283 (4) ◽  
pp. E638-E647 ◽  
Author(s):  
Teresa A. Davis ◽  
Marta L. Fiorotto ◽  
Douglas G. Burrin ◽  
Rhonda C. Vann ◽  
Peter J. Reeds ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Cardiac Muscle ◽  
Liver Protein ◽  
Tissue Protein ◽  
Neonatal Pigs ◽  
Igf I ◽  
Tissue Protein Synthesis ◽  
Insulin Replacement

Studies have shown that protein synthesis in skeletal muscle of neonatal pigs is uniquely sensitive to a physiological rise in both insulin and amino acids. Protein synthesis in cardiac muscle, skin, and spleen is responsive to insulin but not amino acid stimulation, whereas in the liver, protein synthesis responds to amino acids but not insulin. To determine the response of protein synthesis to insulin-like growth factor I (IGF-I) in this model, overnight-fasted 7- and 26-day-old pigs were infused with IGF-I (0, 20, or 50 μg · kg−1 · h−1) to achieve levels within the physiological range, while amino acids and glucose were clamped at fasting levels. Because IGF-I infusion lowers circulating insulin levels, an additional group of high-dose IGF-I-infused pigs was also provided replacement insulin (10 ng · kg−0.66 · min−1). Tissue protein synthesis was measured using a flooding dose ofl-[4-3H]phenylalanine. In 7-day-old pigs, low-dose IGF-I increased protein synthesis by 25–60% in various skeletal muscles as well as in cardiac muscle (+38%), skin (+24%), and spleen (+32%). The higher dose of IGF-I elicited no further increase in protein synthesis above that found with the low IGF-I dose. Insulin replacement did not alter the response of protein synthesis to IGF-I in any tissue. The IGF-I-induced increases in tissue protein synthesis decreased with development. IGF-I infusion, with or without insulin replacement, had no effect on protein synthesis in liver, jejunum, pancreas, or kidney. Thus the magnitude, tissue specificity, and developmental change in the response of protein synthesis to acute physiological increases in plasma IGF-I are similar to those previously observed for insulin. This study provides in vivo data indicating that circulating IGF-I and insulin act on the same signaling components to stimulate protein synthesis and that this response is highly sensitive to stimulation in skeletal muscle of the neonate.

Responses of Tissue Protein Synthesis to Nutrient Intake in Rats Exposed to Interleukin-1β Or Turpentine

1993 ◽  
Vol 85 (3) ◽  
pp. 337-342 ◽  
Author(s):  
Peter E. Ballmer ◽  
Margaret A. McNurlan ◽  
Ian Grant ◽  
Peter J. Garlick
Keyword(s):  
Protein Synthesis ◽  
Parenteral Nutrition ◽  
Young Male ◽  
Interleukin 1Β ◽  
Male Rats ◽  
Synthesis Rate ◽  
Phase Reaction ◽  
Inflammatory Conditions ◽  
Tissue Protein Synthesis ◽  
Growing Rat

1. The influence of an acute-phase reaction on the ability of protein synthesis rates in liver and three different muscles (gastrocnemius, soleus and heart) to respond to a short intravenous infusion of nutrients (glucose plus amino acids) was investigated during experimental inflammation induced by injection of human recombinant interleukin-1β or turpentine in young male rats. 2. Interleukin-1β induced a consistent increase of 3°C in body temperature between 3 and 5 h after injection, whereas turpentine induced a delayed fever, peaking by 13 h. 3. Interleukin-1β and turpentine stimulated fractional rates of protein synthesis in liver. The synthesis rate was inhibited by interleukin-1β in gastrocnemius and soleus muscle, but an elevation was seen in heart muscle. In this study there was no significant response of muscle to turpentine injection. 4. Two hours of parenteral nutrition increased fractional synthesis rates in all tissues when compared with Ringer's lactate. Somewhat larger responses to feeding were observed as a result of either interleukin-1β or turpentine injection in all tissues, but these improvements were not significant. 5. We conclude that the response of protein synthesis rates in liver and skeletal muscle to parenteral nutrition is not inhibited, and may be somewhat enhanced, during acute inflammatory conditions in the growing rat.

Skeletal muscle, liver and wool protein synthesis by sheep infected by the nematode Trichostrongylus colubriformis

1975 ◽  
Vol 26 (6) ◽  
pp. 1063
Author(s):  
LEA Symons ◽  
WO Jones
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Liver Protein ◽  
Trichostrongylus Colubriformis ◽  
Intestinal Nematode ◽  
Skeletal Muscle Proteins

Incorporation of radioisotopically labelled L-leucine into skeletal muscle proteins was measured in vivo and in vitro, and into liver proteins in vivo in three groups of sheep: (1) infected by Trichostrongylus colubriformis, (2) uninfected, pair-fed with the infected animals, (3) uninfected, fed ad lib. Incorporation of [14C]L-leucine by an homogenate of wool follicles from infected and uninfected sheep was also measured. Incorporation of leucine by muscle, and hence muscle protein synthesis, was equally depressed in the anorexic infected sheep losing weight, and in pair-fed animals, whether measured in vivo or in vitro, or expressed in terms of either RNA or DNA. Incorporation into protein was elevated equally in vivo in the livers of the infected and pair-fed sheep when expressed in terms of content of tissue nitrogen, but not in terms of cither nucleic acid. Incorporation by the wool follicular homogenate was appreciably depressed by the infection and is consistent with the poor wool growth in nematode infections. These results show that the same depression of skeletal muscle and, possibly, elevation of liver protein synthesis occur in a ruminant as were reported earlier for laboratory monogastric animals with intestinal nematode infections. Pair-feeding uninfected animals in both this and the earlier experiments emphasized the importance of anorexia as a major cause of these effects on protein synthesis. The importance of these effects upon production is discussed briefly.

scholarly journals Some Biochemical and Histological Effects of 2-Chloroethanol in Rats

1992 ◽  
Vol 1 (3) ◽  
pp. 37-56 ◽  
Author(s):  
Leonard Friedman ◽  
John Scalera ◽  
James E. Keys ◽  
Edmund L. Peters ◽  
Dennis W. Gaines ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Rna Synthesis ◽  
Liver Lipid ◽  
Intraperitoneal Administration ◽  
Female Rats ◽  
Male Rats ◽  
Liver Protein ◽  
Adult Rats

The effects of 2-chioroethanol (2-CE) on rat tissue following in vitro and in vivo exposure were studied. At concentrations as low as 2.5 mg/ml, protein synthesis in liver slices was inhibited; at concentrations of 25 mg/ml and above, RNA synthesis and respiration were also impaired. Single oral doses of 2-CE to young adult rats at levels of 15-40 mg/kg body weight depressed liver nonprotein sulfhydryl (GSH) concentration and liver protein but not RNA synthesis. Liver lipid was increased by 7 hr after a single oral dose of 30 mg/kg. The time courses and dose-response relationship for GSH depletion and restoration and for protein synthesis inhibition and recovery were similar. The livers of female rats were more sensitive than the livers of male rats to the effects of 2-CE. Protein synthesis was also depressed in kidneys of 2-CE-treated male rats but at higher doses than those needed for this effect to occur in livers of the same animals. Liver polysome disaggregation also occurred after oral 2-CE doses of 20 mg/kg and greater. The effects of 2-CE on ribosome profiles and protein synthesis were at least partially reversed by concurrent intraperitoneal administration of cysteine. The possible relationship of these findings to a role of GSH in protein synthesis is discussed.

scholarly journals Short-term effects of corticosterone treatment on muscle protein synthesis in relation to the response to feeding

1987 ◽  
Vol 248 (2) ◽  
pp. 439-442 ◽  
Author(s):  
P J Garlick ◽  
I Grant ◽  
R T Glennie
Keyword(s):  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Plasma Corticosterone ◽  
Male Rats ◽  
Liver Protein ◽  
Carrier Medium ◽  
Corticosterone Treatment ◽  
Small Inhibition

1. Rates of protein synthesis in liver and muscle of 100 g male rats were measured in vivo at 1 h or 4 h after injection of 2.5 mg of corticosterone and compared with those from animals given carrier medium alone. 2. In post-absorptive rats, corticosterone for 1 h had no effect on either muscle or liver protein synthesis. After 4 h there was a decrease in both tissues, but this was only statistically significant in muscle. 3. In fed rats, rates of protein synthesis were higher than those in post-absorptive animals, but the effects of corticosterone injection were similar. 4. Re-feeding of post-absorptive rats led to an increase in muscle protein synthesis after 1 h and 4 h. At 1 h this increase was not inhibited when plasma corticosterone concentrations were maintained high by injection of the hormone immediately before feeding commenced, but at 4 h there was a small inhibition. 5. It is concluded that the action of corticosterone in depressing muscle protein synthesis is time-dependent and requires longer than 1 h to develop. The failure of the hormone to alter the response to re-feeding for 1 h in post-absorptive rats suggest that corticosteroids are not important mediators of the acute stimulation of muscle protein synthesis by food intake.

scholarly journals Measurement of the protein-synthetic activity in vivo of various tissues in rats by using [3H]Puromycin

1979 ◽  
Vol 184 (3) ◽  
pp. 663-668 ◽  
Author(s):  
K Nakano ◽  
H Hara
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Relative Rate ◽  
Chain Elongation ◽  
Synthetic Activity ◽  
Tissue Protein Synthesis ◽  
A New Technique ◽  
Protein Free Diet

The validity of a new technique was examined for estimating the protein-synthetic activity of various tissues in vivo. The basic assumption underlying the method is that the number of peptide chains growing on each active ribosome would increase as the protein-synthetic activity of each tissue increases. The principle of the procedure, which was devised originally by Wool & Kurihara [(1967) Proc. Natl. Acad. Sci. U.S.A. 58, 2401-2407] to determine in vitro the number of functional ribosomes in skeletal muscle, is as follows. Puromycin is known to bind easily to the C-terminal end of the growing peptide on ribosomes and thus stop further chain elongation. Hence, if the number of puromycin molecules attached to the nascent peptide is determined by using radioactive puromycin as a tracer, one can estimate the number of growing peptides, i.e. the activity of tissue protein synthesis. By using this technique, it is shown that both starvation and the feeding of a protein-free diet caused marked decreases in the relative rate of formation of peptidyl-puromycin, i.e. activity of protein synthesis in liver, skeletal muscle, heart, spleen, testis, lung, kidney and intestine.

Corrigendum - Skeletal muscle, liver and wool protein synthesis by sheep infected by the nematode Trichostrongylus colubriformis

1975 ◽  
Vol 26 (6) ◽  
pp. 1063
Author(s):  
LEA Symons ◽  
WO Jones
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Liver Protein ◽  
Trichostrongylus Colubriformis ◽  
Intestinal Nematode ◽  
Skeletal Muscle Proteins

Incorporation of radioisotopically labelled L-leucine into skeletal muscle proteins was measured in vivo and in vitro, and into liver proteins in vivo in three groups of sheep: (1) infected by Trichostrongylus colubriformis, (2) uninfected, pair-fed with the infected animals, (3) uninfected, fed ad lib. Incorporation of [14C]L-leucine by an homogenate of wool follicles from infected and uninfected sheep was also measured. Incorporation of leucine by muscle, and hence muscle protein synthesis, was equally depressed in the anorexic infected sheep losing weight, and in pair-fed animals, whether measured in vivo or in vitro, or expressed in terms of either RNA or DNA. Incorporation into protein was elevated equally in vivo in the livers of the infected and pair-fed sheep when expressed in terms of content of tissue nitrogen, but not in terms of cither nucleic acid. Incorporation by the wool follicular homogenate was appreciably depressed by the infection and is consistent with the poor wool growth in nematode infections. These results show that the same depression of skeletal muscle and, possibly, elevation of liver protein synthesis occur in a ruminant as were reported earlier for laboratory monogastric animals with intestinal nematode infections. Pair-feeding uninfected animals in both this and the earlier experiments emphasized the importance of anorexia as a major cause of these effects on protein synthesis. The importance of these effects upon production is discussed briefly.

Protein synthesis in liver, skeletal muscle, and brown adipose tissue of rats fed a protein-deficient diet

1983 ◽  
Vol 3 (6) ◽  
pp. 569-575 ◽  
Author(s):  
P. W. Emery ◽  
N. J. Rothwell ◽  
M. J. Stock
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Adipose Tissue ◽  
Brown Adipose Tissue ◽  
Protein Content ◽  
Deficient Diet ◽  
Rna Content ◽  
Brown Adipose ◽  
Tissue Protein Synthesis

Feeding protein-deficient diets to rats is known to stimulate diet-induced thermogenesis and activate brown adipose tissue (BAT). The fact that BAT protein content, unlike that of other tissues, is unnaffected by protein deficiency prompted us to measure tissue protein synthesis in vivo in animals maintained on normal- (18.8%) and low- (7.6%) protein (LP) diets. Protein synthesis was depressed in the liver of the LP rats due to a fall in RNA activity, with no change in RNA content, and synthesis was also reduced in skeletal muscle from the LP group, but this was due to decreased RNA content with no change in RNA activity. Conversely, protein synthesis, RNA, DNA, and protein content of interscapular BAT were all unaltered in protein-restricted animals. These data indicate that, unlike liver, skeletal muscle, and whole carcass, BAT protein synthesis is not reduced in protein-restricted rats, and this may be related to activation of thermo-genesis in the tissue.

GH and IGF-I differentially increase protein synthesis in skeletal muscle and jejunum of parenterally fed rats

1996 ◽  
Vol 271 (5) ◽  
pp. E872-E878 ◽  
Author(s):  
H. C. Lo ◽  
D. M. Ney
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Body Weight Gain ◽  
Serum Insulin ◽  
Jejunal Mucosa ◽  
Tissue Mass ◽  
Tissue Protein ◽  
Igf I ◽  
Tissue Protein Synthesis

Growth hormone (GH) and insulin-like growth factor I (IGF-I) selectively increase tissue mass. We compared the fractional rate of protein synthesis (Ks in skeletal muscle, jejunal mucosa and muscularis, and liver to investigate the differential effects of GH and IGF-I on tissue protein synthesis. Surgically stressed rats were maintained with hypocaloric total parenteral nutrition (TPN) and given recombinant human (rh) GH (rhGH), rhIGF-I, rhGH + rhIGF-I (800 or 800 + 800 micrograms/day, respectively), or TPN alone. After 3 days, a flooding dose of valine (800 mumol with 5.56 MBq L-[3,4-3H]valine) was administered, and rats were killed 20 min later. Body weight gain, nitrogen retention, and serum IGF-I concentrations confirmed that GH plus IGF-I additively increased anabolism. Serum insulin concentrations were significantly increased by GH and decreased by IGF-I. GH significantly increased Ks in skeletal muscle and jejunal muscularis, IGF-I significantly increased Ks in jejunal mucosa and muscularis, and neither GH nor IGF-I altered Ks in liver. GH and IGF-I differentially increase tissue protein synthesis in vivo.

scholarly journals The effect of insulin infusion and food intake on muscle protein synthesis in postabsorptive rats

1983 ◽  
Vol 210 (3) ◽  
pp. 669-676 ◽  
Author(s):  
P J Garlick ◽  
M Fern ◽  
V R Preedy
Keyword(s):  
Skeletal Muscle ◽  
Protein Synthesis ◽  
Food Intake ◽  
Plasma Insulin ◽  
Insulin Infusion ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Young Male ◽  
Male Rats ◽  
Significant Stimulation

1. Insulin was infused into young male rats in the postabsorptive state. Rates of protein synthesis in skeletal muscle were determined during the final 10 min of infusion from the incorporation of label into protein after intravenous injection of a massive dose of [3H]phenylalanine. Rates of synthesis were not altered during the first 10 min of insulin infusion, but were increased significantly between 10 and 60 min. 2. Rats were infused with different amounts of insulin for 30 min. When concentrations were increased from 10 to 40 microunits/ml of plasma there was no change in muscle protein synthesis, but concentrations higher than 70 microunits/ml caused a significant stimulation. Concentrations below 10 microunits/ml, obtained by infusion of anti-insulin serum, did not depress synthesis below that found in the postabsorptive rat. 3. Infusion of glucose for 30 or 60 min led to an increase in plasma insulin to 40 microunits/ml, but this also failed to stimulate muscle protein synthesis. 4. Rates of synthesis in postabsorptive rats, even when stimulated maximally by insulin, were not so high as those in fed rats or in postabsorptive rats refed for 60 min. However, in fed and refed rats insulin concentrations were below that required to stimulate synthesis in postabsorptive animals. Despite this, infusion of large amounts of insulin into fed rats did not increase synthesis further. 5. The sensitivity of plasma glucose to insulin infusion was different from that of protein synthesis. A decrease in glucose concentration preceded the increase in synthesis and occurred at lower insulin concentrations. 6. It is concluded that changes in circulating insulin may have been partly responsible for the increase in muscle protein synthesis brought about by feeding, but that other factors must also play a part.

Sign in / Sign up

Export Citation Format

Share Document