The role of insulin, corticosterone and other factors in the acute recovery of muscle protein synthesis on refeeding food-deprived rats

Millward, D. J.; Odedra, B; Bates, P. C.

doi:10.1042/bj2160583

Cited by 79 publications

(46 citation statements)

References 19 publications

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“…It is well known that treatment with glucocorticoids increases vulnerability to infections. The serum glucocorticoid concentration is known to increase in response to various factors, including fasting (Millward et al 1983;Mitev et al 1993) and infections (Zhang et al 1998). In all the fasted groups, the serum corticosterone concentration increased due to the 72 h fasting process (Table 5), and returned to the pre-fasting level within 1 h after initiation of refeeding (results not shown).…”

Section: Effect Of Fasting On Corticosterone and Adrenocorticotrophicmentioning

confidence: 83%

“…Beer et al (1989) have reported that, in human subjects, plasma cortisol, ACTH, b-endorphin and adrenaline concentrations increase, and plasma insulin concentration decreases, within 9 h after initiation of 72 h starvation, returning to or near pre-starvation concentration within 6 h after initiation of refeeding. Millward et al (1983) have shown in rats that change in plasma corticosterone and insulin concentrations due to 4 d food deprivation return to the prefasting level within as little as 40 and 180 min of initiation of refeeding respectively. On the other hand, it has been well documented that various hormones and neuropeptides, as well as cytokines, are able to influence immunological activities and also host resistance (Blalock, 1989).…”

Section: Discussionmentioning

confidence: 99%

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Effect of timing of food deprivation on host resistance to fungal infection in mice

Oarada

Nikawa

N.*³

2002

British Journal of Nutrition

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Mice were deprived of food for a period of 72 h at varying times relative to the time of infection with Paracoccidioides brasiliensis. Host resistance was diminished profoundly when the period of food deprivation was from 48 h before to 24 h after infection (group B). When food deprivation was initiated immediately after infection (group C), host resistance was reduced less profoundly. When food deprivation was initiated at 24 and 48 h post-infection, reductions in host resistance were only moderate or not observed respectively. These results suggest that the earlier in the course of infection starvation occurs, the more profoundly host resistance is impaired. When food deprivation was initiated 72 h before infection, finishing at the time of infection (group A), the reduction in host resistance was considerably less profound compared with group B mice, suggesting that refeeding initiated immediately after infection is responsible for rapid restoration of the antifungal resistance in starved mice. Infection-induced responses of corticosterone and interferon-g were changed according to the timing of food deprivation. Group A mice, similar to non-fasted controls, showed an infection-induced increase in serum corticosterone concentration, while groups B and C did not. Group C mice showed a substantially greater infection-induced increase in serum interferon-g compared with the other fasted and non-fasted control groups.

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Section: Effect Of Fasting On Corticosterone and Adrenocorticotrophicmentioning

confidence: 83%

Section: Discussionmentioning

confidence: 99%

Effect of timing of food deprivation on host resistance to fungal infection in mice

Oarada

Nikawa

N.*³

2002

British Journal of Nutrition

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“…This might be explained by the different response of corticosterone on leptin administration or refeeding. Ahima et al (1996) showed that the fasting-induced increase in serum corticosterone was partly prevented by leptin administration, while it has been shown that refeeding for a period of 60 min resulted in complete recovery of serum corticosterone levels induced by fooddeprivation in rats (Millward et al 1983). Nevertheless, our results are in agreement with a study of Swart et al (2002) reporting that refeeding partly restores fasting-induced alterations in hypothalamic NPY and POMC mRNA expression within 6 h, while leptin administration after food deprivation is not sufficient to affect mRNA levels.…”

Section: Discussionmentioning

confidence: 99%

Differential effects of leptin and refeeding on the fasting-induced decrease of pituitary type 2 deiodinase and thyroid hormone receptor β2 mRNA expression in mice

Boelen

Kwakkel

Vos

et al. 2006

Journal of Endocrinology

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Profound changes in thyroid hormone metabolism occur in the central part of the hypothalamus-pituitary-thyroid (HPT) axis during fasting. Hypothalamic changes are partly reversed by leptin administration, which decreases during fasting. It is unknown to what extent leptin affects the HPT axis at the level of the pituitary. We, therefore, studied fasting-induced alterations in pituitary thyroid hormone metabolism, as well as effects of leptin administration on these changes. Because refeeding rapidly increased serum leptin, the same parameters were studied after fasting followed by refeeding. Fasting for 24 h decreased serum T 3 and T 4 and pituitary TSHb, type 2 deiodinase (D2), and thyroid hormone receptor b2 (TRb2) mRNA expression. The decrease in D2 and TRb2 mRNA expression was prevented when 20 mg leptin was administered twice during fasting. By contrast, the decrease in TSHb mRNA expression was unaffected. A single dose of leptin given after 24 h fasting did not affect decreased TSHb, D2, and TRb2 mRNA expression, while 4 h refeeding resulted in pituitary D2 and TRb2 mRNA expression as observed in control mice. Serum leptin, T 3 , and T 4 after refeeding were similar compared with leptin administration. We conclude that fasting decreases pituitary TSHb, D2, and TRb2 mRNA expression, which (with the exception of TSHb) can be prevented by leptin administration during fasting. Following 24 h fasting, 4 h refeeding completely restores pituitary D2 and TRb2 mRNA expression, while a single leptin dose is ineffective. This indicates that other postingestion signals may be necessary to modulate rapidly the fasting-induced decrease in pituitary D2 and TRb2 mRNA expression.

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“…However, it is important to emphasise that the presence of insulin seems nevertheless indispensable in the postprandial stimulation of muscle protein synthesis by amino acids. Indeed, the acute decrease of postprandial insulinaemia to post-absorptive levels due to either anti-insulin serum (Millward et al 1983) or diazoxide treatment (Sinaud et al 1999;Balage et al 2001) greatly impaired muscle protein synthesis.…”

Section: Stimulation Of Muscle Protein Metabolism By Leucine and Ageingmentioning

confidence: 99%

“…The stimulation of skeletal muscle protein synthesis caused by feeding a complete diet has been shown to be mediated by an increase in the initiation of mRNA translation (Millward et al 1983;Kelly & Jefferson, 1985;Preedy & Garlick, 1986;Yoshizawa et al 1995). One of the most tightly regulated steps in translation initiation is the binding of mRNA to the 40S subunit (Pain, 1996;Rhoads, 1999;Shah et al 2000).…”

Section: Leucine: An Active Bio-substratementioning

confidence: 99%

Leucine: a key amino acid in ageing-associated sarcopenia?

Dardevet

Rieu

Fafournoux

et al. 2003

NRR

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During ageing, a progressive loss of muscle mass has been well described in both man and rodents. This loss of proteins results from an imbalance between protein synthesis and degradation rates. Although some authors have shown a decrease of myofibrillar protein synthesis rates in human volunteers, this imbalance is not clearly apparent when basal rates of protein turnover are measured. A decrease in muscle protein synthesis stimulation was detected nevertheless in ageing rats during the postprandial period, suggesting that the 'meal signal' was altered during ageing. Many results now suggest that aged muscle is less sensitive to the stimulatory effect of amino acids at physiological concentrations but is still able to respond if the increase in aminoacidaemia is sufficiently large. Indeed amino acids play an important role in regulating muscle protein turnover both in vitro and in vivo. At the molecular level, amino acids modulate gene expression. Amino acid response elements have been characterised in the promoter of transcriptional factor CCAAT-enhancer binding protein homologous protein and asparagine synthetase genes. Among amino acids, leucine seems to play the major role in regulating the metabolic function. It inhibits proteolysis and stimulates muscle protein synthesis independently of insulin. Leucine has been shown to act as a real mediator by modulating specifically the activities of intracellular kinases linked to the translation of proteins such as phosphatidylinosinol 3Ј kinase and mammalian target of rapamycin-70 kDa ribosomal protein S6 (p70 S6K ) kinases. We recently demonstrated in vitro that protein synthesis of ageing rat muscles becomes resistant to the stimulatory effect of leucine in its physiological concentration range. However, when leucine concentration was increased greatly above its postprandial level, protein synthesis was stimulated normally. Moreover, we studied the effect of meal leucine supplementation on in vivo protein synthesis in adult and ageing rats. Leucine supplementation had no additional effect on muscle protein synthesis in adults but totally restored its stimulation in ageing rats. Whether chronic oral leucine supplementation would be beneficial for maintaining muscle protein mass in elderly men and women remains to be studied.

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The role of insulin, corticosterone and other factors in the acute recovery of muscle protein synthesis on refeeding food-deprived rats

Cited by 79 publications

References 19 publications

Effect of timing of food deprivation on host resistance to fungal infection in mice

Effect of timing of food deprivation on host resistance to fungal infection in mice

Differential effects of leptin and refeeding on the fasting-induced decrease of pituitary type 2 deiodinase and thyroid hormone receptor β2 mRNA expression in mice

Leucine: a key amino acid in ageing-associated sarcopenia?

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