scholarly journals Effect of corticosterone on myofibrillar protein turnover in diabetic rats as assessed by Nτ-methylhistidine excretion

1982 ◽  
Vol 208 (3) ◽  
pp. 593-601 ◽  
Author(s):  
Frank M. Tomas
Keyword(s):  
Plasma Insulin ◽  
Muscle Protein ◽  
Average Rate ◽  
Diabetic Rats ◽  
Myofibrillar Protein ◽  
Protein Breakdown ◽  
Collagen Protein ◽  
Before And After ◽  
Corticosterone Treatment ◽  
Secondary Rise

The effect of corticosterone on myofibrillar protein breakdown in diabetic rats was investigated in order to assess the possible counteracting effects of the secondary rise in plasma insulin concentrations which normally accompanies such treatment. Nτ-Methylhistidine excretion, an index of myofibrillar protein breakdown, was compared before and after corticosterone treatment (4.0 mg/100 g body wt. per day) of normal control, adrenalectomized, 10-day-streptozotocin-diabetic and adrenalectomized diabetic rats. Diabetic rats received 1.5 units of insulin/100 g body wt. per day throughout the experiment and showed marked hyperglycaemia and glucosuria during corticosterone treatment, whereas non-diabetic rats had only mild hyperglycaemia but elevated insulin concentrations. Corticosterone treatment increased the average rate of myofibrillar protein breakdown by 68% and 95% respectively in non-diabetic and diabetic rats. Net loss of muscle non-collagen protein for the same 7-day period was greater in diabetic than in non-diabetic animals (4.15 versus 2.84% per day), and the calculated average synthesis rates were lowest in diabetic rats. Adrenalectomy had little effect except to decrease slightly the rate of muscle protein breakdown. These results show that the rise in plasma insulin concentrations that accompanies exogenous corticosterone administration to non-diabetic rats diminishes the catabolic effect of this glucocorticoid on muscle. Insulin appears to antagonize the effects of the glucocorticoid by attenuating the increased rates of myofibrillar protein breakdown and, to a lesser extent, by limiting the decrease in synthesis rates.

Insulin- and thyroid hormone-independent adaptation of myofibrillar proteolysis to glucocorticoids

1990 ◽  
Vol 259 (5) ◽  
pp. E699-E705 ◽  
Author(s):  
A. G. Kayali ◽  
M. N. Goodman ◽  
J. Lin ◽  
V. R. Young
Keyword(s):  
Skeletal Muscle ◽  
Plasma Insulin ◽  
Diabetic Rats ◽  
Myofibrillar Protein ◽  
Protein Breakdown ◽  
Biphasic Response ◽  
Glucocorticoid Treatment ◽  
Glucocorticoid Administration ◽  
Early Rise ◽  
Later Phase

Myofibrillar protein breakdown in skeletal muscle progresses through two distinct phases in response to chronic glucocorticoid administration in the rat, i.e., an early phase lasting 4–5 days, during which proteolysis increases followed by a later phase during which proteolysis decreases. The possible involvement of insulin and the iodothyronines in this phenomenon has now been examined. Diabetic, thyroidectomized, and normal rats were treated with corticosteroid for 10–11 days, and at timed intervals muscle proteolysis was evaluated by measuring the release of 3-methyl-L-histidine (3-MH) and tyrosine from the perfused hindquarter as well as the excretion of 3-MH in the urine. Corticosterone (CTC) administration to normal rats increased plasma insulin, whereas plasma 3,5,3'-triiodothyronine responded with an early rise followed by a fall after 4–5 days. However, the biphasic response of myofibrillar proteolysis to chronic glucocorticoid treatment was not abolished in CTC-treated diabetic or thyroidectomized rats. CTC treatment increased release of tyrosine by perfused muscle of diabetic rats but, unlike 3-MH release, did not diminish later. Thus the adaptation of myofibrillar proteolysis to chronic glucocorticoid treatment appears to be independent of insulin and thyroid hormones. However, insulin may play a role in curtailing glucocorticoid-induced breakdown of nonmyofibrillar proteins.

scholarly journals Nitrogen balance and myofibrillar protein turnover in double muscled Belgian Blue bulls in relation to compensatory growth after different periods of restricted feeding

1998 ◽  
Vol 78 (4) ◽  
pp. 549-559 ◽  
Author(s):  
C. Van Eenaeme ◽  
M. Evrard ◽  
J. L. Hornick ◽  
P. Baldwin ◽  
M. Diez ◽  
...  
Keyword(s):  
Nitrogen Balance ◽  
Compensatory Growth ◽  
Muscle Protein ◽  
Growth Period ◽  
Myofibrillar Protein ◽  
Control Group ◽  
Protein Breakdown ◽  
Low Protein ◽  
Fattening Period ◽  
Synthesis And Degradation

Nitrogen balance and myofibrillar protein breakdown were studied in 16 double-muscled Belgian Blue bulls during a low growth period (0.5 kg d−1) (LGP) of 4 mo (L4), 8 mo (L8), or 14 mo (L14) and the subsequent fattening period (rapid growth period, RGP). The control group (CG) was given a conventional fattening diet; the others received a low-energy, low-protein diet during LGP, and the same diet as the CG during RGP. Measurements were made halfway through the LGP, l mo after the beginning of the fattening period, and 1 mo before slaughter. Nitrogen balance was about half of CG (P < 0.001) during LGP, e.g., 50.8, 21.3, 25.8, and 23.8 g d−1, for CG, L4, L8, and L14, respectively. Between LGP and RGP, N balance increased by about 18 g N d−1 above the control in the compensating groups L4, L8 and L14. This was due to the higher digestibility and the higher metabolizability of the nitrogen in the fattening diet. Lower muscle protein accretion during the LGP resulted from decreased synthesis (P < 0.001) and degradation (P < 0.05) compared with the GC. When changing to RGP different evolution patterns were observed in the three formerly restricted groups, e.g. after a short restriction (L4) both synthesis and degradation rose during the RGP but declined towards the end. After a longer restriction (L8 and L14), synthesis and degradation increased and remained high. The magnitude of these increases was inversely proportional to the length of the restriction period. Key words: Belgian Blue bulls, compensatory growth, nitrogen balance, muscle, muscle protein breakdown

scholarly journals Acute Effect of the Timing of Resistance Exercise and Nutrient Intake on Muscle Protein Breakdown

Nutrients ◽  
2020 ◽  
Vol 12 (4) ◽  
pp. 1177
Author(s):  
Wataru Kume ◽  
Jun Yasuda ◽  
Takeshi Hashimoto
Keyword(s):  
Resistance Exercise ◽  
Nutrient Intake ◽  
Plasma Insulin ◽  
Muscle Protein ◽  
Optimal Timing ◽  
Protein Breakdown ◽  
Mixed Meal ◽  
Muscle Protein Breakdown ◽  
Meal Intake ◽  
Post Condition

Background: Combining resistance exercise (RE) with nutrient intake stimulates muscle protein net balance. However, it is still unclear whether the optimal timing of nutrient intake is before or after RE, especially on muscle protein breakdown (MPB) for an augmented muscle anabolic response. The aim of this study was to investigate the effect of a substantial mixed meal (i.e., nutrient- and protein-dense whole foods) before or after RE, compared with RE without a meal on the acute response of MPB in a crossover-design study. Methods: Eight healthy young men performed three trials: (1) meal intake before RE (Pre), (2) meal intake after RE (Post), and (3) RE without meal intake (No). Plasma insulin and 3-methylhistidine (3-MH), an MPB marker, were measured. Results: Time course change in plasma insulin level after RE was significantly higher in the Post condition than in the Pre and No conditions. The area under the curve of 3-MH concentration was significantly lower in the Post condition than in the Pre and No conditions. Conclusions: These results suggest that a substantial mixed meal immediately after RE may effectively suppress MPB in the morning.

Creatine supplementation has no effect on human muscle protein turnover at rest in the postabsorptive or fed states

2003 ◽  
Vol 284 (4) ◽  
pp. E764-E770 ◽  
Author(s):  
Magali Louis ◽  
Jacques R. Poortmans ◽  
Marc Francaux ◽  
Eric Hultman ◽  
Jacques Berré ◽  
...  
Keyword(s):  
Muscle Mass ◽  
Muscle Protein ◽  
Creatine Supplementation ◽  
Quadriceps Muscle ◽  
Protein Breakdown ◽  
Fed State ◽  
Muscle Protein Breakdown ◽  
Before And After ◽  
Total Creatine ◽  
Myofibrillar Protein Synthesis

Dietary creatine supplementation is associated with increases in muscle mass, but the mechanism is unknown. We tested the hypothesis that creatine supplementation enhanced myofibrillar protein synthesis (MPS) and diminished muscle protein breakdown (MPB) in the fed state. Six healthy men (26 ± 7 yr, body mass index 22 ± 4 kg/m2) were studied twice, 2–4 wk apart, before and after ingestion of creatine (21 g/day, 5 days). We carried out two sets of measurements within 5.5 h of both MPS (by incorporation of [1-13C]leucine in quadriceps muscle) and MPB (as dilution of [1-13C]leucine or [2H5]phenylalanine across the forearm); for the first 3 h, the subjects were postabsorptive but thereafter were fed orally (0.3 g maltodextrin and 0.083 g protein · kg body wt−1 · h−1). Creatine supplementation increased muscle total creatine by ∼30% ( P < 0.01). Feeding had significant effects, doubling MPS ( P < 0.001) and depressing MPB by ∼40% ( P < 0.026), but creatine had no effect on turnover in the postabsorptive or fed states. Thus any increase in muscle mass accompanying creatine supplementation must be associated with increased physical activity.

Ghrelin inhibits skeletal muscle protein breakdown in rats with thermal injury through normalizing elevated expression of E3 ubiquitin ligases MuRF1 and MAFbx

2009 ◽  
Vol 296 (4) ◽  
pp. R893-R901 ◽  
Author(s):  
Ambikaipakan Balasubramaniam ◽  
Rashika Joshi ◽  
Chunhua Su ◽  
Lou Ann Friend ◽  
Sulaiman Sheriff ◽  
...  
Keyword(s):  
Skeletal Muscle ◽  
Mrna Expression ◽  
Burn Injury ◽  
Muscle Protein ◽  
Ubiquitin Ligases ◽  
Myofibrillar Protein ◽  
E3 Ubiquitin Ligases ◽  
Protein Breakdown ◽  
Skeletal Muscle Protein ◽  
Muscle Protein Breakdown

We previously determined that ghrelin synthesis was downregulated after burn injury and that exogenous ghrelin retained its ability both to stimulate food intake and to restore plasma growth hormone levels in burned rats. These observations and the finding that anabolic hormones can attenuate skeletal muscle catabolism led us to investigate whether ghrelin could attenuate burn-induced skeletal muscle protein breakdown in rats. These studies were performed in young rats (50–60 g) 24 h after ∼30% total body surface area burn injury. Burn injury increased total and myofibrillar protein breakdown in extensor digitorum longus (EDL) muscles assessed by in vitro tyrosine and 3-methyl-histidine release, respectively. Continuous 24-h administration of ghrelin (0.2 mg·kg−1·h−1) significantly inhibited both total and myofibrillar protein breakdown in burned rats. Ghrelin significantly attenuated burn-induced changes in mRNA expression of IGFBP-1 and IGFBP-3 in liver. In EDL, ghrelin attenuated the increases in mRNA expression of the binding proteins, but had no significant effect on reduced expression of IGF-I. Ghrelin markedly reduced the elevated mRNA expression of TNF-α and IL-6 in EDL muscle that occurred after burn. Moreover, ghrelin normalized plasma glucocorticoid levels, which were elevated after burn. Expression of the muscle-specific ubiquitin-ligating enzyme (E3) ubiquitin ligases MuRF1 and MAFbx were markedly elevated in both EDL and gastrocnemius and were normalized by ghrelin. These results suggest that ghrelin is a powerful anticatabolic compound that reduces skeletal muscle protein breakdown through attenuating multiple burn-induced abnormalities.

N τ-Methylhistidine Excretion and Myofibrillar Protein Breakdown in Patients Receiving Intravenous or Enteral Nutrition

1980 ◽  
Vol 59 (3) ◽  
pp. 211-214 ◽  
Author(s):  
I. B. Holbrook ◽  
E. Gross ◽  
P. J. Milewski ◽  
K. Shipley ◽  
M. H. Irving
Keyword(s):  
Enteral Nutrition ◽  
Muscle Protein ◽  
Myofibrillar Protein ◽  
Protein Breakdown ◽  
Breakdown Rate ◽  
Creatinine Excretion ◽  
Non Invasive ◽  
Breakdown Rates ◽  
Invasive Measurement

1. Nτ-Methylhistidine, nitrogen and creatinine were measured in the urine of 10 volunteers on normal and meat-free diets and in 10 vegetarians, and compared with the results from the urine of eight patients with intestinal fistulae on intravenous or enteral nutrition containing no meat. The values obtained were used to calculate fractional breakdown rate of myofibrillar protein. 2. There was a significant fall in the excretion of Nτ-methylhistidine and creatinine and in apparent fractional breakdown rates after 2 days on a meat-free diet. 3. One of the patients had lower, and two of the patients had higher, fractional breakdown rates compared with the vegetarians. 4. Nτ-Methylhistidine and creatinine excretion-5-be a useful and non-invasive measurement of myofibrillar protein degradation in patients on meat-free diets. Firm conclusions cannot, however, be drawn without confirmatory, direct measurement of the breakdown rates of muscle protein in vivo.

Muscle wasting in emphysema

1988 ◽  
Vol 75 (4) ◽  
pp. 415-420 ◽  
Author(s):  
W. L. Morrison ◽  
J. N. A. Gibson ◽  
C. Scrimgeour ◽  
M. J. Rennie
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Wasting ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Myofibrillar Protein ◽  
Whole Body ◽  
Protein Breakdown ◽  
Body Protein ◽  
Net Protein

1. We have investigated arteriovenous exchanges of tyrosine and 3-methylhistidine across leg tissue in the postabsorptive state as specific indicators of net protein balance and myofibrillar protein breakdown, respectively, in eight patients with emphysema and in 11 healthy controls. Whole-body protein turnover was measured using l-[1-13C]leucine. 2. Leg efflux of tyrosine was increased by 47% in emphysematous patients compared with normal control subjects, but 3-methylhistidine efflux was not significantly altered. 3. In emphysema, whole-body leucine flux was normal, whole-body leucine oxidation was increased, and whole-body protein synthesis was depressed. 4. These results indicate that the predominant mechanism of muscle wasting in emphysema is a fall in muscle protein synthesis, which is accompanied by an overall fall in whole-body protein turnover.

scholarly journals Prostaglandin E2 does not regulate total or myofibrillar protein breakdown in incubated skeletal muscle from normal or septic rats

1990 ◽  
Vol 270 (1) ◽  
pp. 45-50 ◽  
Author(s):  
P O Hasselgren ◽  
O Zamir ◽  
J H James ◽  
J E Fischer
Keyword(s):  
Skeletal Muscle ◽  
Arachidonic Acid ◽  
Prostaglandin E2 ◽  
Plasma Levels ◽  
Muscle Protein ◽  
Myofibrillar Protein ◽  
Protein Breakdown ◽  
Muscle Protein Breakdown

The role of prostaglandins in the regulation of muscle protein breakdown is controversial. We examined the influence of arachidonic acid (5 microM), prostaglandin E2 (PGE2) (2.8 microM) and the prostaglandin-synthesis inhibitor indomethacin (3 microM) on total and myofibrillar protein breakdown in rat extensor digitorum longus and soleus muscles incubated under different conditions in vitro. In other experiments, the effects of indomethacin, administered in vivo to septic rats (3 mg/kg, injected subcutaneously twice after induction of sepsis by caecal ligation and puncture) on plasma levels and muscle release of PGE2 and on total and myofibrillar protein breakdown rates were determined. Total and myofibrillar proteolysis was assessed by measuring production by incubated muscles of tyrosine and 3-methylhistidine respectively. Arachidonic acid or PGE2 added during incubation of muscles from normal rats did not affect total or myofibrillar protein degradation under a variety of different conditions in vitro. Indomethacin inhibited muscle PGE2 production by incubated muscles from septic rats, but did not lower proteolytic rates. Administration in vivo of indomethacin did not affect total or myofibrillar muscle protein breakdown, despite effective plasma levels of indomethacin with decreased plasma PGE2 levels and inhibition of muscle PGE2 release. The present results suggest that protein breakdown in skeletal muscle of normal or septic rats is not regulated by PGE2 or other prostaglandins.

Muscle Protein Degradation in Premature Human Infants

1979 ◽  
Vol 57 (6) ◽  
pp. 535-544 ◽  
Author(s):  
F. J. Ballard ◽  
F. M. Tomas ◽  
L. M. Pope ◽  
P. G. Hendry ◽  
B. E. James ◽  
...  
Keyword(s):  
Protein Degradation ◽  
Premature Infants ◽  
Muscle Protein ◽  
Myofibrillar Protein ◽  
Human Beings ◽  
Protein Breakdown ◽  
Human Infants ◽  
Balance Study ◽  
Muscle Protein Degradation ◽  
Total Muscle

1. Myofibrillar protein degradation has been measured by the rate of 3-methylhistidine excretion in premature infants weighing between 635 g and 1295 g. Analyses were made in conjunction with 1–3 day nitrogen balance studies. 2. In 56 balance studies in 36 infants, total muscle protein breakdown varied between 0·70 and 2·58 (mean 1·05) g day−1 kg−1 body weight while the percentage of total muscle protein degraded each day was between 3·3 and 8·3 (mean 4·8). 3. Both total and fractional rates of protein breakdown showed highly significant negative correlations with nitrogen retention but no relationship to total energy input. 4. Protein degradation was higher than average in infants who were losing weight at the time of the balance study, lower in infants who were gaining weight and higher in those who died within 2 weeks of the analysis. 5. Myofibrillar protein breakdown was not different between infants fed orally and those receiving total parenteral nutrition. 6. Generally the effects of nitrogen and energy status on muscle protein degradation in the premature infants are different from changes reported in adult human beings or adult rats. We suggest that this difference may be a consequence of the very limited energy reserves of the premature infant.

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