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Growth and muscle protein turnover in the chick.

ABSTRACT: The growth rates of young chicks were varied from 0 to 10% per day by manipulation of the adequacy of the amino acid and energy supply. The rates of protein synthesis in the white breast (pectoralis thoracica) muscle and the dark leg (gastrocnemius and peronaeus longus) muscles were estimated by feeding l-[U-(14)C]tyrosine in amino acid/agar-gel diets (;dietary infusion'). This treatment rapidly and consistently produced an isotopic equilibrium in the expired CO(2) and in the free tyrosine of plasma and the muscles. Wholebody protein synthesis in 2-week-old chicks was estimated from the tyrosine flux and was 6.4g/day per 100g body wt. In 1-week-old chicks the rate of protein synthesis was more rapid in the breast muscles than in the leg muscles, but decreased until the rates were similar in 2-week-old birds. Synthesis was also more rapid in fast-growing Rock Cornish broilers than in medium-slow-growing New HampshirexSingle Comb White Leghorn chicks. No or barely significant decrease in the high rates of protein synthesis, in the protein/RNA ratio and in the activity of RNA for protein synthesis occurred in non- or slow-growing chicks fed on diets deficient in lysine, total nitrogen or energy. Thus the machinery of protein synthesis in the young chick seems to be relatively insensitive to dietary manipulation. In the leg muscles, there was a small but significant correlation between the fractional rate of growth and protein synthesis. A decrease in the fractional rate of degradation, however, appeared to account for much of the accumulation of muscle protein in rapidly growing birds. In addition, the rapid accumulation of breast-muscle protein in rapidly growing chicks appeared to be achieved almost entirely by a marked decrease in the fractional rate of degradation.

SUBMITTER: Maruyama K

PROVIDER: S-EPMC1186267 | biostudies-other | 1978 Nov

REPOSITORIES: biostudies-other

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Project description:BackgroundHypoxemia in humans may occur during high altitude mountaineering and in patients suffering from ventilatory insufficiencies such as cardiovascular- or respiratory disease including Chronic Obstructive Pulmonary Disease (COPD). In these conditions, hypoxemia has been correlated to reduced appetite and decreased food intake. Since hypoxemia and reduced food intake intersect in various physiological and pathological conditions and both induce loss of muscle mass, we investigated whether hypoxia aggravates fasting-induced skeletal muscle atrophy and evaluated underlying protein turnover signaling.MethodsMice were kept under hypoxic (8% oxygen) or normoxic conditions (21% oxygen), or were pair-fed to the hypoxia group for 12 days. Following an additional 24 hours of fasting, muscle weight and protein turnover signaling were assessed in the gastrocnemius muscle by RT-qPCR and Western blotting.ResultsLoss of gastrocnemius muscle mass in response to fasting in the hypoxic group was increased compared to the normoxic group, but not to the pair-fed normoxic control group. Conversely, the fasting-induced increase in poly-ubiquitin conjugation, and expression of the ubiquitin 26S-proteasome E3 ligases, autophagy-lysosomal degradation-related mRNA transcripts and proteins, and markers of the integrated stress response (ISR), were attenuated in the hypoxia group compared to the pair-fed group. Mammalian target of rapamycin complex 1 (mTORC1) downstream signaling was reduced by fasting under normoxic conditions, but sustained under hypoxic conditions. Activation of AMP-activated protein kinase (AMPK) / tuberous sclerosis complex 2 (TSC2) signaling by fasting was absent, in line with retained mTORC1 activity under hypoxic conditions. Similarly, hypoxia suppressed AMPK-mediated glucocorticoid receptor (GR) signaling following fasting, which corresponded with blunted proteolytic signaling responses.ConclusionsHypoxia aggravates fasting-induced muscle wasting, and suppresses AMPK and ISR activation. Altered AMPK-mediated regulation of mTORC1 and GR may underlie aberrant protein turnover signaling and affect muscle atrophy responses in hypoxic skeletal muscle.

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Growth and muscle protein turnover in the chick.

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