The relationship between nutritional status and insulin-like growth factor binding protein-2 (IGFBP-2) gene expression in chickens was studied. Chickens (6 wk old) were food deprived for 2 d and then refed. IGFBP-2 mRNA in the brain was significantly decreased by food deprivation and levels did not increase when birds were refed for 24 h. Gizzard and hepatic IGFBP-2 mRNA levels were significantly increased by food deprivation and decreased by refeeding. Any nutrients tested decreased hepatic IGFBP-2 gene expression. In kidney, IGFBP-2 mRNA was detected but not influenced by food deprivation and refeeding. In another study, the influence of dietary protein source [isolated soybean protein vs. casein; crude protein (CP) 20%] and the supplementation of essential amino acids on IGFBP-2 gene expression of young chickens (5 wk old) was examined. The influence of feeding a low soybean protein diet (CP 5%) on tissue IGFBP-2 gene expression was also investigated. Hepatic IGFBP-2 mRNA was not detected in any group. Feeding the low protein diet for 7 d decreased brain IGFBP-2 mRNA level and increased gizzard IGFBP-2 level compared with chickens fed 20% protein diets. A significant interaction between protein source and amino acid supplementation was observed in gizzard IGFBP-2 mRNA level. In both casein-fed groups and in chickens fed 20% soybean protein diet without supplemental amino acids, the levels did not differ from one another or from the low protein diet-fed birds. The level was lower in chickens fed the amino acid-supplemented, 20% soybean protein diet. In conclusion, the response of IGFBP-2 gene expression to variations in nutritional status was rapid and different in several tissues of young chickens, which would help modulate the growth-promoting effect of circulating IGF-I by making the IGF-IGFBP complex.

We have examined the influence of nutrition on plasma IGF-I, IGF-II and IGF-binding protein (IGFBP) levels and on hepatic IGF-I gene expression in young meat-type chickens. Plasma IGF concentrations were measured by using RIA with recombinant chicken IGFs as standards. In chickens fed the control diet containing 200 g/kg dietary protein ad libitum for 7 days, plasma IGF-I concentrations increased significantly from those found in the initial control group. Food restriction for either 4 or 7 days decreased plasma IGF-I by 30% from the initial control. When chickens were refed ad libitum for 3 days after 4 days of restricted feeding, plasma IGF-I levels recovered to those of the control birds fed ad libitum. In chickens eating a low protein diet (100 g/kg protein), the plasma IGF-I tended to be lowered but the decrease was not significant. Although the intensity of IGF-I and beta-actin mRNA bands protected in the RNase protection assay was changed by nutrition, no statistical effect of nutrition on the ratio of IGF-I to beta-actin was observed. The nutritional treatments had no effect on plasma IGF-II concentrations. Western ligand blot and chromatographic analyses were used to investigate the influence of nutrition on IGFBP profiles. Both IGF-I and IGF-II ligands in the Western ligand blot revealed the most intense binding at 30 kDa for plasma obtained from chickens with restricted food intake. The 30 kDa band also appeared at a lower intensity in the group fed a low protein diet but not in any other groups. These observations were confirmed by neutral gel chromatography. The chicken IGF-II ligand revealed an intensely labelled band corresponding to 75 kDa and this was not affected by nutrition. IGF-I and IGFBP concentrations in the plasma of young broiler chickens were influenced by nutritional state but IGF-II concentrations were not. The lack of a response in circulating IGF-II levels may have been due to the presence of high concentrations of a 75 kDa specific binding protein which did not respond to nutrition in this experiment.

1. The effect of L-carnitine supplemented into experimental diets with varying dietary protein concentrations (50, 200 and 400 g/kg) on body weight gain and plasma insulin-like growth factor-I (IGF-I) concentration in chicks was examined. 2. Dietary L-carnitine supplementation provided 0, 200, 500 and 1000 mg/kg. Chicks were given the diet ad libitum for 10 d. 3. When L-carnitine was provided as 500 or 1000 mg/kg, body weight gain was significantly improved in birds receiving the 200 and 400 g protein/kg diets. 4. There was an interaction between dietary L-carnitine and protein content on plasma IGF-I concentration. L-carnitine supplementation had little influence on plasma IGF-I concentrations in birds receiving the low protein (50 g/kg) diet. When dietary L-carnitine concentrations were increased from 0 to 1000 mg/kg in the adequate protein (200 g/kg) diet, plasma IGF-I concentrations were also increased. However, when dietary L-carnitine content was more than 500 mg/kg in the 400 g/kg protein group, plasma IGF-I concentration decreased with increasing dietary L-carnitine content. 5. Body weight change correlated significantly with the alteration in plasma IGF-I concentrations in chicks given diets with adequate dietary protein. 6. In conclusion, the improvement in body weight gain caused by dietary L-carnitine supplementation was achieved when chicks were given their dietary protein requirement, which may be partially explained by an increase in plasma IGF-I concentration.

ABSTRACT

1. The change in the rate of protein synthesis of different muscles, concentrations of plasma insulin, plasma insulin-like growth factor-I (IGF-I) and other plasma components were investigated after refeeding in fasted chicks. 5.2 g of the complete diet was refed. This was the maximum that could be force-fed with water. 2. The fractional synthesis rates (FSR) of breast (M. pectoralis major) and leg (M. gastrocnemius) muscles were measured after injection of L-[2, 6-(3)H]phenylalanine. Plasma insulin and IGF-I concentration were determined by radioimmunoassay. 3. In the breast muscle, FSR was significantly reduced by 2-d fasting. The FSR had recovered completely after 1 h of refeeding and was maintained until 6 h. The change in FSR after refeeding was associated with the change in ribosomal efficiency (K(RNA); absolute synthesis rate per unit RNA), while no change in ribosomal capacity (C(S); RNA: protein ratio) was observed. 4. In the leg muscle, FSR was decreased by 2-d fasting and increased gradually toward 6 h after refeeding but did not reach the level of the fed control. In contrast to the breast muscle, no significant changes in Cs and K(RNA) in the leg muscle were observed. 5. Plasma glucose concentration increased significantly at 1 h after refeeding but returned to the fasted level after 24 h. Plasma insulin concentration in chicks refed for 1 h was higher than in the fasted group. There was no significant change in plasma IGF-I concentration. 6. These results suggest that the FSR of breast muscle was more sensitive to refeeding than that of leg muscle which may be explained, in part, by differences in sensitivity to the change in circulating plasma insulin concentration after refeeding.

To determine if a single injection of insulin-like growth factor-I (IGF-I) can affect muscle protein synthesis in chickens, 7-d-old male Single Comb White Leghorn chicks were injected s.c. with physiological saline (control) or 35 microg of recombinant human IGF-I. After 2 h 30 min, or 6, 12, or 24 h the chicks were injected with 3H-phenylalanine and killed, and the fractional synthesis rate (Ks) of breast muscle protein was measured. The Ks of IGF-I-treated birds were lower (P = 0.03) than controls at 2 h 30 min post-injection, higher (P = 0.07) than controls at 6 h post-injection, but not different from controls at later times. A second experiment examined serum changes during the 6 h after chicks were injected with IGF-I or saline as in the first experiment. Serum IGF-I concentration increased relative to almost undetectable levels (1 ng/mL) of controls to 216 +/- 59 ng/mL at 20 min after IGF-I injection (P < 0.001) and decreased to 12 +/- 6 ng/ mL by 6 h. Serum glucose and nonprotein nitrogen concentrations were significantly decreased for all or most of the 3 h after IGF-I injection, respectively, but only glucose concentration was the same as controls by 6 h. Low serum glucose and nonprotein nitrogen during the first few hours after IGF-I injection may contribute to the inhibition of Ks at 2.5 h, but the mechanisms behind the increased Ks at 6 h are not clear. These results support a role for IGF-I in the posthatching muscle development of chicks.

We investigated the influence of refeeding food-deprived chicks with either protein, carbohydrate, fat or combinations thereof on the rates of liver and muscle protein synthesis. After 2 d of food-deprivation, chicks were given individual or mixed protein, carbohydrate and fat. At 30 min after refeeding, the protein fractional synthesis rate (K(s)) was measured by a large dose injection of L-[2,6-(3)H]phenylalanine. When chicks were food-deprived for 2 d, liver K(s) was 67% lower and muscle fractional synthesis rate was half that of well-fed controls. Upon refeeding starved chicks a complete diet, K(s) in the liver and muscle returned to the level of fed controls within 30 min. When food-deprived chicks were refed protein alone or two of the three macronutrients, liver and muscle K(s) were significantly higher than those in the starved group. There was no effect of refeeding with carbohydrate or fat alone. Plasma glucose concentration was significantly greater than in fed or starved groups in chicks refed the complete diet, carbohydrate or carbohydrate mixed with either protein or fat. Refeeding chicks with the various macronutrients did not affect the plasma insulin or insulin-like growth factor-I concentrations. These results suggest that intakes of individual macronutrients additively increase liver and muscle protein synthesis and that the acute increase in muscle protein synthesis after refeeding chicks diets containing the three macronutrients was mainly regulated by the change in ribosomal efficiency.

Glycation starts from nonenzymatic amino-carbonyl reaction that binds carbonyl group of reducing sugars to the amino group of amino acids. Glycation leads to further complex reactions to form advanced glycation end products (AGE). Because AGE are implicated in the gradual development of diabetic complications, tissue accumulation of AGE has been widely examined in various tissues of rats. Avian species are known to have high body temperature and blood glucose concentration compared with mammals. Although these characteristics enabled chickens to be used as experimental models for diabetes mellitus, the information of AGE accumulation in various tissues of chickens has not been limited so far. In the present study, therefore, the radioactive AGE prepared by reacting (14)C-glucose and amino acids were intravenously administrated, and comparison of tissue accumulation of (14)C-labeled AGE was made between chickens and rats. At 30 min after administration, tissues (18-20) were collected, and the radioactivity incorporated into tissues was determined. High levels of radioactivity per gram of tissue in the liver and kidney were observed in both rats and chickens. In chickens but not rats, a large amount of (14)C-labeled AGE incorporated into 1 g of spleen was observed, and the specific accumulation of AGE in the avian spleen might have a particular role in immune response in avian species.