• Journal of Nutrition and Health
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• 제29권8호
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• pp.867-873
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• 1996

This study was undertaken to determine whether the anabolic steroid nandrolone phenylpropionate(NPP) can inhibit the muscle atrophy and reduction in muscle protein synthesis caused by glucocorticoids in female rates. Daily injections of 50mg/kg of corticosterone for eight days induced significant reductions in body weight gain and protein without affecting food intake. The mass, protein and RNA content, ratio of RNA to protein, and fractional rate of protein synthesis, measured in vivo, of gastrocnemius muscle were all significantly reduced by corticosterone treatement. Simultaneous administration of NPP at a dose of 10mg/kg with corticosteorne (50mg/kg) fully inhibited the reductions in the mass, protein and RNA content of gastrocnemius muscle, and body weight gain and protein with no alteration in food intake but the reduction in fractional rate of muscle protein syntheis was only partially prevented. The results indicate that the anabolic steroid nandrolone phenylpropionate is capable of preventing muscle atrophy in female rats treated with excess corticosterion.

• Preventive Nutrition and Food Science
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• 제10권1호
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• pp.40-45
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• 2005

Age-related changes in bone metabolism are well established by biochemical markers of bone matrix in serum and urine, but analysis of the residual bone matrix, which is still turning over, has not been investigated. In the present study, we measured in vivo rates of bone protein synthesis using a precursor-product method based on the exchange of ²H from ²H₂O into amino acids. Four percent ²H₂O was administered to mice in drinking water after intraperitonial (i.p) bolus injection of 99.9% ²H₂O. Mice were divided into the two groups: growing young mice were administered 4% ²H₂O for 12 weeks after an i.p bolus injection at 5 week of age, whereas weight stable adult mice started drinking 4% ²H₂O 8 weeks later than the growing group and continued 4% ²H₂O drinking for 8 weeks. Mass isotopomer abundance in alanine from bone protein was analyzed by gas chromatography/mass spectrometry. Body ²H₂O enrichments were in the range of 1.88-2.41% over the labeling period. The fractional synthesis rates (ks) of bone protein were 2.000±0.071%/d for growing mice and 0.243±0.014%/d for adult mice. These results demonstrate that the bone protein synthesis rate decreases with age and present direct evidence of age-related changes in bone protein synthesis.

• Asian-Australasian Journal of Animal Sciences
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• 제18권9호
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• pp.1326-1335
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• 2005

The main purpose of this study is to investigate the effects of dietary lysine deficiency on protein turnover of porcine muscles. There were 18 LYD three-breed-crossing postweanling barrows from six litters cannulated with gastric tubes through the esophagus at approximate 10 kg of body weight and allocated into three treatment groups. When their body weights reached over 12 kg, one group was sacrificed for determining the initial protein masses of m. masseter, m. longissimus dorsi, m. adductor and m. biceps femoris from the right body side. The others received a diet containing 100% or 61.4% (calculated values) of the lysine requirement (NRC, 1998) multiplied by 1.103 for a period of 17 days. Daily feed provision was computed for each pig according to body weight at the same day. All pigs were infused a flooding dose of $^2$H$_5$-phenylalanine to determine the fractional protein synthesis rates (FSR) of the aforementioned muscles in the end. Their four muscles from the right body side were also dissected for measuring the fractional rates of protein accretion (FAR). As for protein degradation, fractional rates (FDR) were calculated by differences between synthesis and accretion. Results showed that the lysine deficiency resulted in, significantly (p<0.05), lighter body weights, smaller muscles and a slower growth rate. The protein mass, accreted by the muscles, of the deficient group was only 54% averaged of the pigs fed adequately (p<0.05). The FAR of these muscles in the deficient group was significantly lower (p<0.05) and only achieved 61.1% averaged of the control; there was no significant difference (p>0.05), nevertheless, in the amino-acid composition of muscles between two groups. The lysine deficiency reduced significantly (p<0.05) the FSR of m. longissimus dorsi but did not influence its FDR. The m. biceps femoris also presented an inhibited FSR while its FDR reduced only exhibited a very high tendency (p = 0.055) compared to the adequately-fed pigs. As for the m. masseter and m. adductor, both of the FSR and FDR were depressed significantly (p<0.05) by the lysine deficiency, and changes in the FSR were severer than those in the FDR, so that their FAR were significantly slower (p<0.05) in comparison with the control group. The lysine deficiency also inhibited the RNA translation activity of the muscles while the effects on RNA capacity were not significant (p>0.05). In conclusion, the FAR of muscle protein was changed by the current lysine deficiency through the alterations in the FSR and/or FDR.

• Nutrition Research and Practice
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• 제4권5호
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• pp.375-382
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• 2010

The precise effects of protein intake on fractional synthesis rate (FSR) of muscle protein are still under debate. The sample size of these studies was small and the conclusions in young and elderly subjects were inconsistent. To assess the effect of dietary protein intake on the FSR level, we conducted a meta-analysis of controlled protein intake trials. Random-effects models were used to calculate the weighted mean differences (WMDs). Ten studies were included and effects of short-term protein intake were evaluated. In an overall pooled estimate, protein intake significantly increased the FSR (20 trials, 368 participants; WMD: 0.025%/h; 95%CI: 0.019-0.031; P < 0.0001). Meta-regression analysis suggested that the protein dose was positively related to the effect size (regression coefficient = 0.108%/h; 95%CI: 0.035, 0.182; P = 0.009). A subgroup analysis indicated that protein intake significantly increased FSR when the protein dose was ${\leq}$ 0.80 g/kg BW (16 trials, 308 participants; WMD: 0.027%/h; 95%CI: 0.019-0.031; P < 0.0001), but did not affect FSR when the protein dose was > 0.80 g/kg BW (4 trials, 60 participants; WMD: 0.016%/h; 95%CI: 0.004-0.029; P = 0.98). In conclusion, this study is the first integrated results showing that a short-term protein intake is effective at improving the FSR of muscle protein in the healthy elderly as well as young subjects. This beneficial effect seems to be dose-dependent when the dose levels of protein range from 0.08 to 0.80 g/kg BW.

• Asian-Australasian Journal of Animal Sciences
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• 제9권2호
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• pp.171-174
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• 1996

Muscle protein synthesis in vitro was measured in chicks fed low-protein(10% CP) and control(20% CP) diets. Right leg muscles (M. gastrocnemius) were mounted on a support made of stainless steel to stretch in constant tension, whereas left leg muscles were unmounted. Both leg muscles were incubated in Dulbecco's modified Eagle's medium including L-[$4-^3H$] phenylalanine for 60 min to measure in vitro protein synthesis. There was no significant difference in fractional synthesis rate(FSR) of muscle protein between both dietary protein levels, whereas FSR with stretch in constant tension was significantly higher than that without constant tension due to an increase in the absolute synthesis rate(ASR) per unit RNA(the efficiency of RNA to synthesize protein). The ASR of muscle protein in chicks fed the control diet was significantly higher than that in the low-protein diet group.

• Journal of Nutrition and Health
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• 제29권8호
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• pp.874-880
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• 1996

The effects of an anabolic steroid, nandrolone phenylpropionate(NPP), on body weight gain and body protein, and muscle protein metabolism were inestigated in adrenocorticotrophic hormone(ACTH)-treated male and female rats. Daily injections of 100ug/day of ACTH for 7-8 days caused a cessation of growth in females and a net loss of body weight in males which were associated with significant reductions in body protein content. However, food intake was not affected by ACTH in either sex. The weight, protein content and fractional rate of protein synthesis, measured in vivo, of gastrocnemius muscle were all significantly reduced in both sexes. NPP at a dose of 4mg/kg body weight prevented the reduction in body weight gain in ACTH-treate females but not in males. However, boy protein content was increased by NPP in both sexes which was associated with increases in the weight, protein content and fractional rate of protein synthesis of gastrocnemius muscle. ACTH treatment caused a marked increase in plasma concentrations of corticosterone in both sexes. NPP suppressed much of the increases in corticosterone concentrations in both sexes. The results of the present study suggest that NPP exerts at least part of its anabolic effect by reducing plasma concentrations of catabolic glucocorticoid hormones, through suppressing the response of the adrenals to ACTH.

• Asian-Australasian Journal of Animal Sciences
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• 제15권12호
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• pp.1760-1764
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• 2002

In order to elucidate the physiological function of circulating IGF-I on muscle protein synthesis in the chicken under malnutritional conditions, we administrated recombinant chicken IGF-I using a osmotic mini pump to fasted young chickens and measured the rate of muscle protein synthesis and plasma metabolite. The pumps delivered IGF-I at the rate of $22{\mu}g/d\{300{\mu}g{\cdot}(kg\;body\;weight{\cdot}d)^{-1}\}$. Fractional rate of protein synthesis in the muscle was measured using a large dose injection of L-[$2,6-^3H$]phenylalanine. Constant infusion of chicken IGF-I did not affect plasma glucose level. Significant interaction between dietary treatment and IGF-I infusion was observed in plasma NEFA and total cholesterol concentrations. When chicks were fasted, IGF-I infusion decreased plasma NEFA and total cholesterol concentrations. On the other hand, IGF-I administration did not affect plasma levels of both metabolites. Fasting reduced plasma triglyceride concentration significantly. IGF-I infusion also decreased the level of plasma triglyceride. Plasma IGF-I concentration of young chickens was halved by fasting for 1 d. IGF-I infusion using an osmotic minipump for 1 d increased plasma IGF-I concentration in fasted chicks to the level of fed chicks. Fasting decreased body weight and the loss of body weight was significantly ameliorated by IGF-I infusion. There was a significant interaction between dietary treatment and IGF-I infusion in the fractional rate of breast muscle protein synthesis. There was no effect of IGF-I infusion on muscle protein synthesis in fed chicks. Muscle protein synthesis reduced by fasting was ameliorated by IGF-I infusion, but did not reach to the level of fed control. Muscle weight of fasted chicks infused with IGF-I was similar to fasted birds without IGF-I infusion, which suggests that muscle protein degradation would be increased by IGF-I infusion as well as protein synthesis in fasted chicks.

• Korean Chemical Engineering Research
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• 제54권3호
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• pp.404-409
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• 2016

비등온의 열중량분석기(TGA)에 의해 nitrate-citrate 혼합물의 전구체로부터 $LaMnO_3$ 합성반응의 열적특성과 반응특성을 고찰하였다. TGA의 승온속도는 5.0, 10.0, 15.0, 20.0 K/min으로 조정하였다. $LaMnO_3$ 합성반응은 승온속도의 변화에 따라 450~600 K (X=0.4~0.7)에서 빠르게 진행되었다. $LaMnO_3$ 합성반응의 활성화에너지는 Friedman, Ozawa-Flynn-Wall 그리고 Vyazovkin의 방법으로 해석하였는데, 반응전환율의 변화에 따라 23~243 kJ/g-mol 범위 값을 나타내었다. 반응차수는 승온속도와 반응전환율이 증가함에 따라 감소하였다. 반응차수의 평균값은 반응전환율이 0.1~0.3의 범위인 반응초기에는 4.5이었으며, 반응전환율이 0.7~0.9 범위인 반응의 종결 부분에서는 1.87이었다. 반응속도의 빈도인자는 승온속도와 반응전환율의 증가에 따라 점차 증가하였다. 반응속도의 빈도인자(frequency factor)는 반응전환율이 0.1~0.3인 경우에는 205.6 ($min^{-1}$)이었으며 반응전환율이 0.7~0.9인 경우에는 475.2 ($min^{-1}$)이었다.

• Asian-Australasian Journal of Animal Sciences
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• 제11권5호
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• pp.545-549
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• 1998

The influence of refeeding with either vitamin, mineral, fibre of water on protein synthesis and mRNA content in the liver and breast muscle of fasted chicks was investigated. At 15 d of age, chicks were fasted for 2 d and then refed either vitamin, mineral, fibre or water. The fractional synthesis rate (FSR) of protein was measured after 30 min of refeeding by using a large dose injection of L - 2, $6[^3H]$ phenylalanine. In the liver, FSR was reduced by fasting and tended to increase but not significantly by refeeding with vitamin or mineral. FSR was not affected by refeeding with fibre or water. There was no influence of fasting and refeeding on ribosomal capacity (the RNA : protein ratio) and ribosomal efficiency (total protein synthesised per total RNA). The absolute synthesis rate (ASR) of liver protein and hepatic mRNA content were reduced by fasting and unchanged by refeeding. In the muscle, FSR, ASR and mRNA content were significantly decreased by fasting and not recovered by refeeding with either vitamin, mineral, fibre or water. It concluded that vitamin, mineral, fibre and water have little capacity to stimulate liver and muscle protein synthesis reduced by fasting.

• Asian-Australasian Journal of Animal Sciences
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• 제3권4호
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• pp.313-318
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• 1990

Forty-two outbred female Sprague-Dawley rats weighing 145 g were used to study the effects of a beta-agonist, cimaterol, on growth, body composition and urinary excretion of 3-methylhistidine (MH) at 3, 6 and 18 d. Cimaterol (CIM) was administered in the feed at 10 mg/kg. The growth promoting effect of CIM was most evident during the initial part of the feeding period, followed by a gradual decrease in the magnitude of the response with no significant effect at 18 d. The action of CIM was confined to skeletal and cardiac muscles with no stimulating effect on other organs. The amount of urine excretion and urinary MH excretion was reduced (p<.01) at 3 d in the CIM group. No difference was found at 6 d, followed by an increased urine excretion (p<.05) and MH excretion (p<.01) at 18 d. An inverse relationship between growth rate and urinary MH excretion suggested that the increased growth rate of CIM-fed rats during the initial part of the feeding period is primarily attributed to the decreased protein degradation rate. It was further suggested that both fractional synthesis rate and fractional degradation rate increased during the later part of the feeding period.