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.

Protein synthesis in skeletal muscle and jejunum is more responsive to feeding in 7-than in 26-day-old pigs

1996 ◽  
Vol 270 (5) ◽  
pp. E802-E809 ◽  
Author(s):  
T. A. Davis ◽  
D. G. Burrin ◽  
M. L. Fiorotto ◽  
H. V. Nguyen
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Plasma Concentrations ◽  
Postnatal Life ◽  
Tissue Protein ◽  
Igf I ◽  
Tissue Protein Synthesis ◽  
Stimulation Of

The study aimed to determine the developmental changes in the response of peripheral and visceral tissue protein synthesis to feeding during early postnatal life and the associated changes in circulating insulin, insulin-like growth factor (IGF-I), and amino acid concentrations. Tissue protein synthesis was measured in vivo with a large dose of L-[4(-3)H]phenylalanine in 7- and 26-day-old pigs that were either fasted for 24 h or refed for 2.75 h after a 24-h fast. Fractional rates of protein synthesis (Ks) in skeletal muscle, heart, and liver were greater in 7-than in 26-day-old pigs. Refeeding stimulated Ks in skeletal muscle, pancreas, jejunum, and liver of both 7-and 26-day-old pigs. The stimulation of skeletal muscle and jejunal Ks by refeeding was greater in 7- than in 26-day-old pigs. Plasma IGF-I concentrations were lower in 7- than in 26-day-old pigs. Plasma concentrations of insulin and amino acids increased with refeeding. The increase in plasma insulin concentrations with refeeding was greater in 7- than in 26-days-old pigs. These results indicate that the stimulation in skeletal muscle and jejunal protein synthesis by feeding is elevated in young compared with older suckling pigs. This enhanced stimulation of protein synthesis by feeding in neonatal pigs is associated with elevated circulating concentrations of insulin but not amino acids or IGF-I.

Modulation of muscle protein synthesis by insulin is maintained during neonatal endotoxemia

2006 ◽  
Vol 291 (1) ◽  
pp. E159-E166 ◽  
Author(s):  
Renan A. Orellana ◽  
Pamela M. J. O'Connor ◽  
Jill A. Bush ◽  
Agus Suryawan ◽  
M. Carole Thivierge ◽  
...  
Keyword(s):  
Insulin Resistance ◽  
Skeletal Muscle ◽  
Amino Acids ◽  
Protein Synthesis ◽  
Gastrocnemius Muscle ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Liver Protein ◽  
Fasting Insulin ◽  
Neonatal Pigs

Sepsis promotes insulin resistance and reduces protein synthesis in skeletal muscle of adults. The effect of sepsis on insulin-stimulated muscle protein synthesis has not been determined in neonates, a highly anabolic population that is uniquely sensitive to insulin. Overnight fasted neonatal pigs were infused for 8 h with endotoxin [lipopolysaccharide (LPS), 0 and 10 μg·kg−1·h−1]. Glucose and amino acids were maintained at fasting levels, insulin was clamped at either fasting or fed (2 or 10 μU/ml) levels, and fractional protein synthesis rates were determined at the end of the infusion. LPS infusion induced a septic-like state, as indicated by a sustained elevation in body temperature, heart rate, and cortisol. At fasting insulin levels, LPS reduced fractional protein synthesis rates in gastrocnemius muscle (−26%) but had no effect on the masseter and heart. By contrast, LPS stimulated liver protein synthesis (+28%). Increasing insulin to fed levels accelerated protein synthesis rates in gastrocnemius (controls by +38%, LPS by +60%), masseter (controls by +50%, LPS by +43%), heart (controls by +34%, LPS by +40%), and diaphragm (controls by +54%, LPS by +29%), and the response to insulin was similar in LPS and controls. Insulin did not alter protein synthesis in liver, kidney, or jejunum in either group. These findings suggest that acute endotoxemia lowers basal fasting muscle protein synthesis in neonates but does not alter the response of protein synthesis to insulin.

Dietary protein and lactose increase translation initiation factor activation and tissue protein synthesis in neonatal pigs

2006 ◽  
Vol 290 (2) ◽  
pp. E225-E233 ◽  
Author(s):  
Jason W. Frank ◽  
Jeffery Escobar ◽  
Agus Suryawan ◽  
Hanh V. Nguyen ◽  
Scot R. Kimball ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Translation Initiation ◽  
Dietary Protein ◽  
Protein Intake ◽  
Mrna Translation ◽  
Initiation Factor ◽  
Tissue Protein ◽  
Neonatal Pigs ◽  
Tissue Protein Synthesis

Protein synthesis and eukaryotic initiation factor (eIF) activation are increased in muscle and liver of pigs parenterally infused with amino acids and insulin. To examine the effects of enteral protein and carbohydrate on protein synthesis, pigs ( n = 42, 1.7 kg body wt) were fed isocaloric milk diets containing three levels of protein (5, 15, and 25 g·kg body wt−1·day−1) and two levels of lactose (low = 11 and high = 23 g·kg body wt−1·day−1) from 1 to 6 days of age. On day 7, pigs were gavage fed after 4-h food deprivation, and tissue protein synthesis rates and biomarkers of mRNA translation were assessed. Piglet growth and protein synthesis rates in muscle and liver increased with dietary protein and plateaued at 15 g·kg body wt−1·day−1 ( P < 0.001). Growth tended to be greater in high-lactose-fed pigs ( P = 0.07). Plasma insulin was lowest in pigs fed 5 g·kg body wt−1·day−1 protein ( P < 0.0001). Plasma branched-chain amino acids increased as protein intake increased ( P < 0.0001). Muscle ( P < 0.001) and liver ( P ≤ 0.001) ribosomal protein S6 kinase-1 and eIF4E-binding protein phosphorylation increased with protein intake and plateaued at 15 g·kg body wt−1·day−1. The results indicate that growth and protein synthesis rates in neonatal pigs are influenced by dietary protein and lactose intake and might be mediated by plasma amino acids and insulin levels. However, feeding protein well above the piglet’s requirement does not further stimulate the activation of translation initiation or protein synthesis in skeletal muscle and liver.

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.

Growth hormone acutely stimulates forearm muscle protein synthesis in normal humans

1991 ◽  
Vol 260 (3) ◽  
pp. E499-E504 ◽  
Author(s):  
D. A. Fryburg ◽  
R. A. Gelfand ◽  
E. J. Barrett
Keyword(s):  
Skeletal Muscle ◽  
Amino Acids ◽  
Growth Hormone ◽  
Protein Synthesis ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Skeletal Muscle Protein ◽  
Skeletal Muscle Protein Synthesis ◽  
Igf I ◽  
Normal Humans

The short-term effects of growth hormone (GH) on skeletal muscle protein synthesis and degradation in normal humans are unknown. We studied seven postabsorptive healthy men (age 18-23 yr) who received GH (0.014 micrograms.kg-1.min-1) via intrabrachial artery infusion for 6 h. The effects of GH on forearm amino acid and glucose balances and on forearm amino acid kinetics [( 3H]Phe and [14C]Leu) were determined after 3 and 6 h of the GH infusion. Forearm deep vein GH rose to 35 +/- 6 ng/ml in response to GH, whereas systemic levels of GH, insulin, and insulin-like growth factor I (IGF-I) were unchanged. Forearm glucose uptake did not change during the study. After 6 h, GH suppressed forearm net release (3 vs. 6 h) of Phe (P less than 0.05), Leu (P less than 0.01), total branched-chain amino acids (P less than 0.025), and essential neutral amino acids (0.05 less than P less than 0.1). The effect on the net balance of Phe and Leu was due to an increase in the tissue uptake for Phe (71%, P less than 0.05) and Leu (37%, P less than 0.005) in the absence of any significant change in release of Phe or Leu from tissue. In the absence of any change in systemic GH, IGF-I, or insulin, these findings suggest that locally infused GH stimulates skeletal muscle protein synthesis. These findings have important physiological implications for both the role of daily GH pulses and the mechanisms through which GH can promote protein anabolism.

scholarly journals Differential effects of long-term leucine infusion on tissue protein synthesis in neonatal pigs

Amino Acids ◽  
2010 ◽  
Vol 40 (1) ◽  
pp. 157-165 ◽  
Author(s):  
Fiona A. Wilson ◽  
Agus Suryawan ◽  
Renán A. Orellana ◽  
María C. Gazzaneo ◽  
Hanh V. Nguyen ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Tissue Protein ◽  
Differential Effects ◽  
Neonatal Pigs ◽  
Tissue Protein Synthesis

scholarly journals Prolonged leucine infusion differentially affects tissue protein synthesis in neonatal pigs

2010 ◽  
Vol 24 (S1) ◽  
Author(s):  
Agus Suryawan ◽  
Fiona A. Wilson ◽  
María C. Gazzaneo ◽  
Renán A. Orellana ◽  
Hanh V. Nguyen ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Tissue Protein ◽  
Neonatal Pigs ◽  
Tissue Protein Synthesis

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.

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