Administration of growth hormone to pigs alters the relative amount of insulin-like growth factor-I mRNA in liver and skeletal muscle

1991 ◽  
Vol 130 (3) ◽  
pp. 331-NP ◽  
Author(s):  
A. L. Grant ◽  
W. G. Helfericht ◽  
S. A. Kramer ◽  
R. A. Merkel ◽  
W. G. Bergen
Keyword(s):  
Skeletal Muscle ◽  
Growth Factor ◽  
High Protein Diet ◽  
High Protein ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Low Protein ◽  
Igf I

ABSTRACT The relative amount of insulin-like growth factor-I (IGF-I) mRNA was determined in the liver and skeletal muscle of market weight crossbred barrows (castrated male pigs) using a solution hybridization–nuclease protection assay. Pigs were given either 50 μg recombinant porcine GH per kg body weight or vehicle daily for 24 days i.m. They were fed corn–soybean meal diets containing either 140 or 200 g crude protein/kg (low or high protein). The percentage of muscle in the carcasses of pigs given GH was greater (P <0·01) than that of controls. Relative to controls, GH increased (P <0·05) the amount of liver IGF-I mRNA by 2·7-fold in pigs fed the low protein diet and 3·0-fold in pigs fed the high protein diet. The amount of IGF-I mRNA in the muscles of GH-treated pigs was 77% and 84% of control pigs in those fed the low and high protein diets respectively (P <0·08). GH increased (P <0·001) the serum concentration of IGF-I 1·6-fold in pigs fed the low protein diet and 2·0-fold in those fed the high protein diet. These results indicate that the administration of GH to pigs influences the relative amount of liver IGF-I mRNA. The increased amount of liver IGF-I mRNA and the increased serum IGF-I concentrations suggest that IGF-I plays an endocrine role in mediating GH-induced muscle hypertrophy in pigs. Journal of Endocrinology (1991) 130, 331–338

scholarly journals Insulin-like growth factor-I, but not growth hormone, is dependent on a high protein intake to increase nitrogen balance in the rat

1999 ◽  
Vol 81 (2) ◽  
pp. 145-152 ◽  
Author(s):  
Myriam Sanchez-Gomez ◽  
Kjell Malmlöf ◽  
Wilson Mejia ◽  
Antonio Bermudez ◽  
Maria Teresa Ochoa ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Growth Factor ◽  
Dietary Protein ◽  
Protein Diet ◽  
N Balance ◽  
Low Protein Diet ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Low Protein ◽  
Igf I

The aim of the present study was to investigate the influence of dietary protein level on the protein anabolic effects of growth hormone (GH) and insulin-like growth factor-I (IGF-I). Female growing rats were fed on either a high- or a low-protein diet with crude protein contents of 222 and 83 g/kg respectively. The diets contained the same amount of metabolizable energy (15·1 MJ/kg) and were given during a 14 d period. During the same time, three groups of rats (n 8) on each diet received subcutaneous infusions of either saline, recombinant human GH (rhGH) or recombinant human IGF-I (rhIGF-I). rhGH and rhIGF-I were given in doses of 360 and 500 μg/d respectively. The low-protein diet alone reduced significantly (P < 0·05) IGF-I concentrations in serum and in tissue taken from the gastrocnemius muscle as well as IGF-I mRNA from the same muscle. The responses to rhGH and rhIGF-I in terms of muscle IGF-I and its mRNA were variable. However, when rhIGF-I was infused into rats on the high-protein diet, significantly elevated levels of IGF-I in muscle tissues could be observed. This was associated with a significantly (P < 0·05) increased N balance, whereas rhGH significantly (P < 0·05) enhanced the N balance in rats on the low-protein diet. Thus, it can be concluded that the level of dietary protein ingested regulates not only the effect of IGF-I on whole-body N economy but also the regulation of IGF-I gene expression in muscles. The exact mechanism by which GH exerts its protein anabolic effect, however, remains to be elucidated.

scholarly journals Physiological concentration of amino acids regulates insulin-like-growth-factor-binding protein 1 expression

1998 ◽  
Vol 334 (1) ◽  
pp. 147-153 ◽  
Author(s):  
Céline JOUSSE ◽  
Alain BRUHAT ◽  
Marc FERRARA ◽  
Pierre FAFOURNOUX
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Growth Factor ◽  
Hepg2 Cells ◽  
Binding Protein ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Insulin Like Growth Factor ◽  
Low Protein ◽  
Igf I

Protein undernutrition is characterized by growth failure in young growing animals. Current evidence suggests that biosynthesis of insulin-like growth factor (IGF)-I and IGF-binding protein 1 (IGFBP-1) are key control points for nutritional regulation of growth. Here we examined the role of amino acid limitation in regulating the IGFBP-1 expression in the hepatic cell line. Our data show that leucine limitation strongly induces IGFBP-1 without affecting IGF-I and IGF-II expression in human HepG2 cells and in isolated rat hepatocytes. Depletion of arginine, cystine and all essential amino acids leads to induction of IGFBP-1 mRNA and protein expression in a dose-dependent manner. IGFBP-1 expression is significantly induced by leucine concentration in the range of that observed in the blood of rats fed a low-protein diet or in humans affected by kwashiorkor. Moreover, treatment of HepG2 cells with amino acids at a concentration reproducing the amino acid concentration found in portal blood of rats fed a low-protein diet leads to a significantly higher expression of IGFBP-1. These data represent the first demonstration that an amino acid limitation, as occurs during dietary protein deficiency, induces IGFBP-1 expression in hepatic cells. Therefore, amino acids by themselves can play, in concert with hormones, an important role in the control of gene expression.

scholarly journals High‐protein diet more effectively reduces hepatic fat than low‐protein diet despite lower autophagy and FGF21 levels

2020 ◽  
Vol 40 (12) ◽  
pp. 2982-2997 ◽  
Author(s):  
Chenchen Xu ◽  
Mariya Markova ◽  
Nicole Seebeck ◽  
Anne Loft ◽  
Silke Hornemann ◽  
...  
Keyword(s):  
High Protein Diet ◽  
High Protein ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Low Protein ◽  
Hepatic Fat

scholarly journals Insulin-like growth factor I stimulates degradation of an mRNA transcript encoding the 14 kDa ubiquitin-conjugating enzyme

1996 ◽  
Vol 319 (2) ◽  
pp. 455-461 ◽  
Author(s):  
Simon S WING ◽  
Nathalie BEDARD
Keyword(s):  
Skeletal Muscle ◽  
Growth Factor ◽  
Binding Proteins ◽  
Mrna Levels ◽  
Insulin Like Growth Factor ◽  
Mrna Transcript ◽  
Factor I ◽  
Igf I ◽  
Ubiquitin Conjugating Enzyme ◽  
Growth Factor I

Upon fasting, the ubiquitin-dependent proteolytic system is activated in skeletal muscle in parallel with the increases in rates of proteolysis. Levels of mRNA encoding the 14 kDa ubiquitin-conjugating enzyme (E214k), which can catalyse the first irreversible reaction in this pathway, rise and fall in parallel with the rates of proteolysis [Wing and Banville (1994) Am. J. Physiol. 267, E39-E48], indicating that the conjugation of ubiquitin to proteins is a regulated step. To characterize the mechanisms of this regulation, we have examined the effects of insulin, insulin-like growth factor I (IGF-I) and des(1–3) insulin-like growth factor I (DES-IGF-I), which does not bind IGF-binding proteins, on E214k mRNA levels in L6 myotubes. Insulin suppressed levels of E214k mRNA with an IC50 of 4×10-9 M, but had no effects on mRNAs encoding polyubiquitin and proteasome subunits C2 and C8, which, like E214k, also increase in skeletal muscle upon fasting. Reduction of E214k mRNA levels was more sensitive to IGF-I with an IC50 of approx. 5×10-10 M. During the incubation of these cells for 12 h there was significant secretion of IGF-I-binding proteins into the medium. DES-IGF-I, which has markedly reduced affinity for these binding proteins, was found to potently reduce E214k mRNA levels with an IC50 of 3×10-11 M. DES-IGF-I did not alter rates of transcription of the E214k gene, but enhanced the rate of degradation of the 1.2 kb mRNA transcript. The half-life of the 1.2 kb transcript was approximately one-third that of the 1.8 kb transcript and can explain the more marked regulation of this transcript observed previously. This indicates that the additional 3´ non-coding sequence in the 1.8 kb transcript confers stability. These observations suggest that IGF-I is an important regulator of E214k expression and demonstrate, for the first time, stimulation of degradation of a specific mRNA transcript by this hormone, while overall RNA accumulates.

Low-Protein Diet Regulates a Proximal Nephron Insulin-like Growth Factor Binding Protein

1994 ◽  
Vol 23 (6) ◽  
pp. 849-855 ◽  
Author(s):  
Michael K. Hise ◽  
Nicki M. Mantzouris ◽  
Joel S. Lahn ◽  
M. Saeed Sheikh ◽  
Zhi-Ming Shao ◽  
...  
Keyword(s):  
Growth Factor ◽  
Binding Protein ◽  
Protein Diet ◽  
Low Protein Diet ◽  
Insulin Like Growth Factor ◽  
Factor Binding ◽  
Low Protein
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