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Summary Livestock and laboratory animals show compensatory growth when they are fed ad libitum following a period of restriction feeding. Lysine is a major limiting essential amino acid in the diets both for humans and animals. We hypothesized that changing dietary lysine levels from deficient to sufficient induced compensatory growth in young rats. We elucidated the effect of lysine sufficiency on the dynamics of hormones, relevant to muscle protein synthesis and degradation, insulin-like growth factor-I (IGF-I) and corticosterone, and on the expression of proteolytic-related genes in skeletal muscle during compensatory growth. Lysine sufficiency where the dietary lysine level was increased from 0.46% to 1.30% after 2 wk of subjecting the rats to the lower lysine level induced 80% enhancement of growth rate of rats. During compensatory growth with the lysine sufficiency, fractional muscle protein synthesis rates were higher whereas fractional muscle protein degradation rates were lower than those of the control group ( p Ͻ 0.05). After lysine sufficiency, the expression of atrogin-1/MAFbx mRNA was decreased in gastrocnemius muscle ( p Ͻ 0.05). With the lysine sufficiency, serum IGF-I concentration increased ( p Ͻ 0.05) whereas serum corticosterone decreased ( p Ͻ 0.05). These findings suggest that compensatory growth with lysine sufficiency is due to a change of hormone levels before and after changing diets, resulting in incrementation of protein synthesis and suppression of protein degradation of skeletal muscle. Key Words compensatory growth, lysine, rat, IGF-I, corticosteroneOne of the important subjects in nutritional science is to elucidate how humans and animals respond and adapt to transitions of nutritional status and changes of metabolic reaction that occur during the adaptation.There are numerous reports about adaptation of animals to excess or deficiency of nutrients or energy in diets. Compensatory growth is an example of adaptation to nutritional status. Livestock and laboratory animals show compensatory growth when they are fed ad libitum following a period of restricted feeding or fed adequate energy following a period of energy restriction ( 1-3 ). Previous studies in rats and pigs showed that when animals that had been fed a protein-free or a low protein diet were refed a diet containing a sufficient amount of protein, they developed faster than animals fed a control diet particularly for the first few days after the diet replacement ( 4-6 ). Promoted protein accumulation during compensatory growth is due to a larger difference between the rate of muscle protein synthesis and the rate of muscle protein degradation compared to normal growth. The phenomenon has been considered a transitional state in adapting to the nutritional status. Both anabolic and catabolic hormones may be involved in this response. All of these previous studies indicate that sufficiency of dietary protein and amino acid levels plays a role as a trigger for compensatory growth in animals. However, these studies provide no ...

Nondigestible oligosaccharides are not digested in the small intestine, but are fermented by bacteria colonizing in the large intestine. Physiological effects of non-digestible oligosaccharides have been considered to be conferred by the fermentation of bacteria colonizing in the large intestine. Because cellooligosaccharide is a non-digestible oligosaccharide, various physiological effects are expected. However, physiological functions of cellooligosaccharide are not well understood. This experiment was conducted to clarify the effect of dietary supplementation with cellooligosaccharide on the growth performance in weanling pigs. The result showed that average daily gain was significantly higher ( P < 0.05) in pigs fed a diet supplemented with cellooligosaccharide than in pigs without cellooligosaccharide. There was a tendency to increasing average daily feed intake in pigs with cellooligosaccharide, though the significant difference was not detected ( P = 0.18). Feed efficiency and nutrient digestibility of feces and ileum were not changed by feeding cellooligosaccharide. In addition, blood urea nitrogen was significantly higher ( P < 0.05) in pigs fed the diet supplemented with cellooligosaccharide than in pigs without cellooligosaccharide. The concentrations of acetic and iso-valeric acids in the cecum of pigs fed the diet with cellooligosaccharide tended to be higher ( P < 0.10) than those without cellooligosaccharide. The results obtained in this study demonstrated that dietary supplementation with cellooligosaccharide improves growth performance in weanling pigs.

We previously reported that L-leucine suppresses myofibrillar proteolysis in chick skeletal muscles. In the current study, we compared the effects of L- and D-enantiomers of leucine on myofibrillar proteolysis in skeletal muscle of chicks. We also assessed whether leucine itself or its metabolite, alpha-ketoisocaproate (alpha-KIC), mediates the effects of leucine. Food-deprived (24 h) chicks were orally administered 225 mg/100 g body weight L-leucine, D-leucine or alpha-KIC and were sacrificed after 2 h. L-Leucine administration had an obvious inhibitory effect on myofibrillar proteolysis (plasma N(tau)-methylhistidine concentration) in chicks while D-leucine and alpha-KIC were much more effective. We also examined the expression of the proteolytic-related genes (ubiquitin, proteasome, m-calpain and cathepsin B) by real-time PCR of cDNA in chick skeletal muscles. Ubiquitin mRNA expression was decreased by D-leucine and alpha-KIC but not L-leucine. Proteasome and m-calpain mRNA expressions as well as cathepsin B mRNA expression were likewise decreased by L-leucine, D-leucine and alpha-KIC. These results indicate that D-leucine and alpha-KIC suppress proteolytic-related genes, resulting in an decrease in myofibrillar proteolysis while L-leucine is much less effective in skeletal muscle of chicks, may be explain by conversion of D-leucine to alpha-KIC.

Two experiments were conducted to elucidate the nitrogen (N) balance of pigs exhibiting compensatory growth when changing the dietary lysine levels from deficiency to sufficiency. Experiment 1 elucidated whether pigs exhibited compensatory growth with dietary lysine sufficiency. Twenty 6-week-old males were assigned to one of two treatments: control and LC (lysine and control). Control pigs were fed a control diet throughout the 24-day experimental period, whereas LC pigs were fed a low lysine diet until day 21 of the experiment, followed by the control diet until the end of experiment. The dietary lysine sufficiency treatment induced an 80% increase in the growth rate of LC pigs (P < 0.05). Experiment 2 focused on the N balance of pigs that exhibited compensatory growth with dietary lysine sufficiency. Eighteen 6-week-old males were assigned to one of three treatments: control, LC, and LL (low lysine). LL pigs were fed a low lysine diet throughout the 24-day experimental period. Pigs that exhibited compensatory growth with dietary lysine sufficiency tended to retain a higher amount of N than control pigs (P = 0.10). These finding suggest that the compensatory growth induced in pigs by dietary lysine sufficiency was partly attributable to a higher level of N retention.

Previous studies have shown that the muscle protein degradation rates of broiler are lower than those of layer chickens. In this study, we assessed proteolytic-related gene expression in the pectoralis muscle of layer and broiler chickens. The mRNA levels of atrogin-1/MAFbx and proteasome C2 subunit, but not those of ubiquitin, m-calpain large subunit, cathepsin B, or caspase-3, were lower in the skeletal muscle of the broilers than in the layers at 7 and 14 d of age. We infer that the lower muscle protein degradation of broilers than of layers at least partly relates to lower mRNA expression of atrogin-1/MAFbx and proteasome C2 subunit in the skeletal muscle of broilers.

We examined the effects of orally administered glycine on myofibrillar proteolysis in food-deprived chicks. Food-deprived (24 h) chicks were orally administered 57, 113, and 225 mg glycine/100 g body weight and killed after 2 h. The plasma N(tau)-methylhistidine concentration, used as myofibrillar proteolysis, was decreased by glycine. We also examined the expression of proteolytic-related genes by real-time PCR of cDNA from chick skeletal muscles. The mRNA expression of atrogin-1/MAFbx, proteasome C2 subunit, m-calpain large subunit, and cathepsin B was decreased by glycine in a dose-dependent manner. The plasma corticosterone concentration was also decreased by glycine, but the plasma insulin concentration was unaffected. These results indicate that orally administered glycine suppresses myofibrillar proteolysis and expression of proteolytic-related genes of skeletal muscle by decreasing the plasma corticosterone concentration in chicks.

The cationic amino acid transporter (CAT) protein family transports lysine and arginine in cellular amino acid pools. We hypothesized that CAT expression changes in pig skeletal muscles during rapid pig postnatal development. We aimed to investigate the tissue distribution and changes in the ontogenic expression of CATs in pig skeletal muscles during postnatal development. Six piglets at 1, 12, 26, 45, and 75 days old were selected from six litters, and their longissimus dorsi (LD), biceps femoris (BF), and rhomboideus (RH) muscles, and their stomach, duodenum, jejunum, ileum, colon, liver, kidney, heart, and cerebrum were collected. CAT-1 was expressed in all the 12 tissues investigated. CAT-2 (CAT-2A isoform) expression was highest in the skeletal muscle and liver and lowest in the jejunum, ileum, kidney, and heart. CAT-3 was expressed mainly in the colon and detected in the jejunum, ileum, and cerebrum. The CAT-1 expression was higher in the skeletal muscle of day 1 pigs than in that of older pigs (P < 0.05). The CAT-2 mRNA level was lowest at day 1, but increased with postnatal development (P < 0.05). There was no significant change in CAT-1 expression among the LD, BF, and RH during postnatal development (P > 0.05); however, there was a change in CAT-2 expression. The CAT-2 expression was highest in the LD of 12-, 26-, 45-, and 75-day-old pigs, followed by the BF and RH (P < 0.05). These results suggest that CAT-1 and CAT-2 play different roles in pig skeletal muscles during postnatal development.