scholarly journals A Whole-Grain Diet Improves Whole-Body Protein Turnover Compared to a Macronutrient-Matched Refined-Grain Diet in Adults with Overweight/Obesity

2020 ◽  
Vol 4 (Supplement_2) ◽  
pp. 1661-1661
Author(s):  
Jacob Mey ◽  
John Kirwan
Keyword(s):  
Protein Synthesis ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
Whole Grains ◽  
Whole Body ◽  
Protein Breakdown ◽  
Whole Grain ◽  
Protein Kinetics ◽  
Body Protein ◽  
Fasted State

Abstract Objectives We investigated the effect of consuming a whole-grain diet on whole-body protein metabolism compared to a macronutrient-matched refined-grain diet in adults with overweight/obesity using labelled amino acids (ClinicalTrials.gov Identifier: NCT01411540). Methods We conducted a randomized, controlled crossover trial in 14 adults with overweight/obesity (age: 40 ± 7 yrs, BMI: 33 ± 5 kg/m2) in which isocaloric, macronutrient-matched whole-grain (WG) and refined-grain (RG) diets were fully provided for two 8-week periods (with a 10-week washout period). Diets differed only in the inclusion of whole grains (50 g/1000 kcal). Body composition was measured via DEXA. Whole-body protein kinetics were assessed before and after each diet in the fasted state (13C-Leucine, primed, constant infusion) and over 24 hours (15N-Glycine, bolus). Protein kinetics were normalized to fat-free mass (FFM). Results Both diets resulted in mild weight loss (WG: −2.0 ± 2.5 kg; RG: −2.9 ± 3.3 kg; both P = 0.01 compared to baseline). Fasted-state leucine kinetics revealed greater protein synthesis (WG: 205 ± 61 µmol/kgFFM/hr; RG: 178 ± 36 µmol/kgFFM/hr; P = 0.04) and protein breakdown (WG: 235 ± 68 µmol/kgFFM/hr; RG: 203 ± 40 µmol/kgFFM/hr, P = 0.03) on a WG vs RG diet. This resulted in a more negative fasted-state net balance on a WG diet (WG: −30 ± 8 µmol/kg/hr; RG: −25 ± 6 µmol/kg/hr, P = 0.02). In contrast, 24-hour whole-body protein turnover measured by the end-product method (15N-Glycine), revealed greater protein synthesis (WG: 316 ± 135 mg protein/kgFFM/hr; RG: 250 ± 94 mg protein/kgFFM/hr) with no difference in protein breakdown, yielding a more positive 24-hr net balance on a WG diet (WG: 31 ± 21 mg protein/kgFFM/hr; RG: 10 ± 34 mg protein/kgFFM/hr). Conclusions A whole-grain diet increases whole-body leucine flux and results in a greater 24-hr net protein balance in adults with overweight/obesity compared to a refined-grain diet. This trial suggests whole-grains have an independent effect on protein metabolism and may benefit adults with overweight/obesity. Funding Sources This research was supported by the NIH (UL1 RR024989, T32DK007319 (JPK); T32AT004094 (JTM – trainee)) and an investigator-initiated grant from Nestle (JPK). Nestle Product Technology Center and Cereal Partners Worldwide provided the study meals and foods.

scholarly journals A Whole-Grain Diet Increases Whole-Body Protein Balance Compared to a Macronutrient-Matched Refined-Grain Diet

2021 ◽  
Author(s):  
Jacob T Mey ◽  
Jean-Philippe Godin ◽  
Amanda R Scelsi ◽  
Emily L Kullman ◽  
Steven K Malin ◽  
...  
Keyword(s):  
Older Adults ◽  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Function ◽  
Whole Grains ◽  
Whole Body ◽  
Whole Grain ◽  
Protein Balance ◽  
Body Protein

Abstract Background There are limited data from randomized control trials to support or refute the contention that whole-grains may enhance protein metabolism in humans. The objectives were threefold: 1) to examine the clinical effects of a whole-grain diet on whole-body protein turnover; 2) the cellular effects of whole-grains on protein synthesis in skeletal muscle cells; and 3) the population effects of whole-grain intake on age-related muscle loss. Methods Adults with overweight/obesity (N = 14, age: 40±7 years, BMI: 33±5 kg/m2) were recruited into a crossover, randomized controlled trial (NCT01411540) in which isocaloric, macronutrient-matched whole-grain and refined-grain diets were fully provisioned for two 8-week periods. Diets differed only in the presence of whole-grains (50 g/1000 kcal). Whole-body protein kinetics were assessed at baseline and after each diet in the fasted-state (13C-Leucine) and integrated over 24-hours (15N-Glycine). In vitro studies utilizing C2C12 cells assessed global protein synthesis by SUnSET and anabolic signaling by Western blot. Complementary epidemiologic assessments using the NHANES database assessed the effect of whole-grain intake on muscle function assessed by gait speed in older adults (N = 2,783). Results Integrated 24-hour net protein balance was 3-fold higher on a whole-grain compared to a refined-grain diet (P = 0.04). A whole-grain wheat extract increased submaximal rates of global protein synthesis (27%, P<0.05) in vitro. In a large sample of older adults, whole-grain intake was associated with greater muscle function in older adults (OR (CI) = 0.92 (0.86, 0.98)). Conclusions Consuming 50 g/1000 kcal of whole-grains per day promotes greater whole-body protein turnover and enhances net protein balance in adults. Whole-grains impact skeletal muscle at the cellular level, and in older adults, associate with greater muscle function. Collectively, these data point to a new mechanism whereby whole-grain consumption favorably enhances protein turnover and improves health outcomes.

Enhancement of tumor proteolysis by TNF-alpha: correlation of in vivo isotope estimates with growth

1991 ◽  
Vol 261 (1) ◽  
pp. R106-R116
Author(s):  
N. W. Istfan ◽  
P. R. Ling ◽  
G. L. Blackburn ◽  
B. R. Bistrian
Keyword(s):  
Protein Synthesis ◽  
Protein Metabolism ◽  
Whole Body ◽  
Independent Effect ◽  
Yoshida Sarcoma ◽  
Protein Breakdown ◽  
Body Protein ◽  
Breakdown Rates ◽  
Made In

To evaluate the accuracy of in vivo estimates of protein synthesis and breakdown, measurements of plasma and tissue leucine kinetics were made in rat tumor tissues at different conditions of growth by use of constant intravenous infusion of [14C]leucine. These measurements were made in Yoshida sarcoma tumors on days 10 and 13 after implantation, with and without tumor necrosis factor (TNF) infusion and on day 10 in Walker-256 carcinosarcoma. Expressed as micromoles of leucine per gram tissue, tumor protein breakdown increased (P less than 0.01) from 0.32 +/- 0.02 to 0.52 +/- 0.09 (SE) mumol/h, with progress of the Yoshida sarcoma tumor between days 10 and 13 after implantation. Similarly, TNF increased tumor proteolysis on day 10 (0.43 +/- 0.03 mumol.h-1.g-1, P less than 0.05 vs. day 10 control) but not on day 13 after implantation of the Yoshida tumor. Estimates of growth derived from the difference between protein synthesis and breakdown rates were not statistically different from those based on actual tumor volume changes in both tumor models. However, estimates of “whole body” protein metabolism (plasma leucine flux) were not affected either by tumor aging or by treatment with TNF. This study shows that in vivo estimates of tissue protein metabolism based on our [14C]leucine constant infusion model closely reflect the growth characteristic of that tissue. A cytotoxic perfusion-independent effect for intravenous TNF on growing tumor tissue is demonstrable as increased protein breakdown. Furthermore, the commonly used concept of whole body protein metabolism, derived solely from tracer dilution in plasma, is an oversimplification.

Role of ovarian hormones in the regulation of protein metabolism in women: effects of menopausal status and hormone replacement therapy

2006 ◽  
Vol 291 (3) ◽  
pp. E639-E646 ◽  
Author(s):  
Michael J. Toth ◽  
Cynthia K. Sites ◽  
Dwight E. Matthews
Keyword(s):  
Postmenopausal Women ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
Hormone Replacement ◽  
Menopausal Status ◽  
Ovarian Hormones ◽  
Hormone Deficiency ◽  
Whole Body ◽  
Protein Breakdown ◽  
Body Protein

The age-related decline in fat-free mass is accelerated in women after menopause, implying that ovarian hormone deficiency may have catabolic effects on lean tissue. Because fat-free tissue mass is largely determined by its protein content, alterations in ovarian hormones would likely exert regulatory control through effects on protein balance. To address the hypothesis that ovarian hormones regulate protein metabolism, we examined the effect of menopausal status and hormone replacement therapy (HRT) on protein turnover. Whole body protein breakdown, oxidation, and synthesis were measured under postabsorptive conditions using [13C]leucine in healthy premenopausal ( n = 15, 49 ± 1 yr) and postmenopausal ( n = 18, 53 ± 1 yr) women. In postmenopausal women, whole body protein turnover and plasma albumin synthesis rates (assessed using [13C]leucine and [2H]phenylalanine) were also measured following 2 mo of treatment with oral HRT (0.625 mg conjugated estrogens + 2.5 mg medroxyprogesterone acetate, n = 9) or placebo ( n = 9). No differences in whole body protein breakdown, oxidation, or synthesis were found between premenopausal and postmenopausal women. Protein metabolism remained similar between groups after statistical adjustment for differences in adiposity and when subgroups of women matched for percent body fat were compared. In postmenopausal women, no effect of HRT was found on whole body protein breakdown, synthesis, or oxidation. In contrast, our results support a stimulatory effect of HRT on albumin fractional synthesis rate, although this did not translate into alterations in circulating albumin concentrations. In conclusion, our results suggest no detrimental effect of ovarian hormone deficiency coincident with the postmenopausal state, and no salutary effect of hormone repletion with HRT, on rates of whole body protein turnover, although oral HRT regimens may increase the synthesis rates of albumin.

Aspects of protein metabolism after elective surgery in patients receiving constant nutritional support

1990 ◽  
Vol 78 (6) ◽  
pp. 621-628 ◽  
Author(s):  
F. Carli ◽  
J. Webster ◽  
V. Ramachandra ◽  
M. Pearson ◽  
M. Read ◽  
...  
Keyword(s):  
Amino Acids ◽  
Protein Synthesis ◽  
Metabolic Rate ◽  
Protein Metabolism ◽  
Protein Turnover ◽  
Resting Metabolic Rate ◽  
Plasma Concentrations ◽  
Whole Body ◽  
Body Protein ◽  
Urinary Nitrogen

1. The present study was designed in an attempt to resolve conflicting views currently in the literature relating to the effect of surgery on various aspects of protein metabolism. 2. Sequential post-operative (2, 4 and 6 days) changes in whole-body protein turnover, forearm arteriovenous difference of plasma amino acids, glucose, lactate and free fatty acids, muscle concentration of free amino acids, RNA and protein, urinary nitrogen and 3-methylhistidine, plasma concentrations of insulin, cortisol and growth hormone, and resting metabolic rate, were measured in six patients undergoing uncomplicated elective total abdominal hysterectomy. 3. All patients received a constant daily diet, either orally or intravenously, based on 0.1 g of nitrogen/kg and an energy content of 1.1 times the resting metabolic rate for 7 days before and 6 days after surgery. 4. Whole-body protein turnover, synthesis and breakdown increased significantly 2 days after surgery (P <0.05) and returned towards pre-operative levels thereafter. 5. Forearm release of branched-chain amino acids and alanine, and efflux of glucose and lactate, were enhanced 4 days after surgery (P <0.05). Muscle glutamine and alanine concentrations were decreased on the fourth and sixth days after surgery (P <0.05). The RNA/protein ratio (indicating the capacity for protein synthesis) was unaltered. 6. A significant increase in urinary nitrogen and 3-methylhistidine was observed on days 3 and 4 after surgery (P <0.05). Thereafter, these parameters remained elevated, although failing to reach statistical significance. 7. The resting metabolic rate was significantly increased (P <0.05) 2 days after surgery but the respiratory quotient (0.77) was unchanged. 8. These data support the contention that whole-body protein synthesis and breakdown increase after surgery. Differences observed pre- and post-operatively between leucine kinetic estimates and other methods of quantifying protein metabolism indicate that only like methodologies should be compared.

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.

Muscle protein metabolism in female swimmers after a combination of resistance and endurance exercise

1996 ◽  
Vol 81 (5) ◽  
pp. 2034-2038 ◽  
Author(s):  
Kevin D. Tipton ◽  
Arny A. Ferrando ◽  
Bradley D. Williams ◽  
Robert R. Wolfe
Keyword(s):  
Protein Synthesis ◽  
Resistance Training ◽  
Endurance Exercise ◽  
Protein Metabolism ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Whole Body ◽  
Protein Breakdown ◽  
Body Protein ◽  
Muscle Protein Metabolism

Tipton, Kevin D., Arny A. Ferrando, Bradley D. Williams, and Robert R. Wolfe. Muscle protein metabolism in female swimmers after a combination of resistance and endurance exercise. J. Appl. Physiol. 81(5): 2034–2038, 1996.—There is little known about the responses of muscle protein metabolism in women to exercise. Furthermore, the effect of adding resistance training to an endurance training regimen on net protein anabolism has not been established in either men or women. The purpose of this study was to quantify the acute effects of combined swimming and resistance training on protein metabolism in female swimmers by the direct measurement of muscle protein synthesis and whole body protein degradation. Seven collegiate female swimmers were each studied on four separate occasions with a primed constant infusion of ring-[13C6]phenylalanine (Phe) to measure the fractional synthetic rate (FSR) of the posterior deltoid and whole body protein breakdown. Measurements were made over a 5-h period at rest and after each of three randomly ordered workouts: 1) 4,600 m of intense interval swimming (SW); 2) a whole body resistance-training workout with no swimming on that day (RW); and 3) swimming and resistance training combined (SR). Whole body protein breakdown was similar for all treatments (0.75 ± 0.04, 0.69 ± 0.03, 0.69 ± 0.02, and 0.71 ± 0.04 μmol ⋅ min−1 ⋅ kg−1for rest, RW, SW, and SR, respectively). The FSR of the posterior deltoid was significantly greater ( P< 0.05) after SR (0.082 ± 0.015%/h) than at rest (0.045 ± 0.006%/h). There was no significant difference in the FSR after RW (0.048 ± 0.004%/h) or SW (0.064 ± 0.008%/h) from rest or from SR. These data indicate that the combination of swimming and resistance exercise stimulates net muscle protein synthesis above resting levels in female swimmers.

Whole body protein kinetics in women: effect of pregnancy and IDDM during anabolic stimulation

2000 ◽  
Vol 279 (5) ◽  
pp. E978-E988 ◽  
Author(s):  
Paul G. Whittaker ◽  
Choy H. Lee ◽  
Roy Taylor
Keyword(s):  
Amino Acids ◽  
Type 1 Diabetes ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Metabolism ◽  
Whole Body ◽  
Protein Breakdown ◽  
Body Protein ◽  
In Pregnancy

The effects of pregnancy and type 1 diabetes [insulin-dependent diabetes mellitus (IDDM)] on protein metabolism are still uncertain. Therefore, six normal and five IDDM women were studied during and after pregnancy, using [13C]leucine and [2H5]phenylalanine with a hyperinsulinemic-euglycemic clamp and amino acid infusion. Fasting total plasma amino acids were lower in pregnancy in normal but not IDDM women (2,631 ± 427 vs. 2,057 ± 471 and 2,523 ± 430 vs. 2,500 ± 440 μmol/l, respectively). Whole body protein breakdown (leucine) increased in pregnancy [change in normal (ΔN) and IDDM women (ΔD) 0.59 ± 0.40 and 0.48 ± 0.26 g · kg−1 · day−1, both P < 0.001], whereas reductions in protein breakdown due to insulin/amino acids (ΔN −0.57 ± 0.19, ΔD −0.58 ± 0.20 g · kg−1 · day−1, both P < 0.001) were unaffected by pregnancy. Protein breakdown in IDDM women was not higher than normal, and neither pregnancy nor type 1 diabetes altered the insulin sensitivity of amino acid turnover. Nonoxidized leucine disposal (protein synthesis) increased in pregnancy (ΔN 0.67 ± 0.45, ΔD 0.64 ± 0.34 g · kg−1 · day−1, both P < 0.001). Pregnancy reduced the response of phenylalanine hydroxylation to insulin/amino acids in both groups (ΔN −1.14 ± 0.74, ΔD −1.12 ± 0.77 g · kg−1 · day−1, both P < 0.05). These alterations may enable amino acid conservation for protein synthesis and accretion in late pregnancy. Well-controlled type 1 diabetes caused no abnormalities in the regulation of basal or stimulated protein metabolism.

Effects in vivo of decreased plasma and intracellular muscle glutamine concentration on whole-body and hindquarter protein kinetics in rats

1999 ◽  
Vol 96 (6) ◽  
pp. 639-646 ◽  
Author(s):  
Steven W. M. OLDE DAMINK ◽  
Ivo DE BLAAUW ◽  
Nicolaas E. P. DEUTZ ◽  
Peter B. SOETERS
Keyword(s):  
Protein Synthesis ◽  
Protein Turnover ◽  
Muscle Protein ◽  
Whole Body ◽  
Glutamine Supplementation ◽  
Constant Infusion ◽  
Glutamine Concentration ◽  
Protein Kinetics ◽  
Body Protein

Glutamine is considered to be a ‘conditionally’ essential amino acid. During situations of severe stress like sepsis or after trauma there is a fall in plasma glutamine levels, enhanced glutamine turnover and intracellular muscle glutamine depletion. Under these conditions, decreased intramuscular glutamine concentration correlates with reduced rates of protein synthesis. It has therefore been hypothesized that intracellular muscle glutamine levels have a regulatory role in muscle protein turnover rates. Administration of the glutamine synthetase inhibitor methionine sulphoximine (MSO) was used to decrease glutamine levels in male Wistar rats. Immediately after the MSO treatment (t = 0 h), and at t = 6 h and t = 12 h, rats received intraperitoneal injections (10 ml/100 g body weight) with glutamine (200 mM) to test whether this attenuated the fall in plasma and intracellular muscle glutamine. Control animals received alanine and saline after MSO treatment, while saline was also given to a group of normal rats. At t = 18 h rats received a primed constant infusion of l-[2,6-3H]phenylalanine. A three-pool compartment tracer model was used to measure whole-body protein turnover and muscle protein kinetics. Administration of MSO resulted in a 40% decrease in plasma glutamine and a 60% decrease in intracellular muscle glutamine, both of which were successfully attenuated by glutamine infusions. The decreased intracellular muscle glutamine levels had no effect on whole-body protein turnover or muscle protein kinetics. Also, glutamine supplementation did not alter these parameters. Alanine supplementation increased both hindquarter protein synthesis and breakdown but the net balance of phenylalanine remained unchanged. In conclusion, our results show that decreased plasma and muscle glutamine levels have no effect on whole-body protein turnover or muscle protein kinetics. Therefore, it is unlikely that, in vivo, the intracellular muscle concentration of glutamine is a major regulating factor in muscle protein kinetics.

Resting metabolic rate and protein turnover in apparently healthy elderly Gambian men

1995 ◽  
Vol 268 (6) ◽  
pp. E1083-E1088 ◽  
Author(s):  
C. Benedek ◽  
P. Y. Berclaz ◽  
E. Jequier ◽  
Y. Schutz
Keyword(s):  
Body Composition ◽  
Body Weight ◽  
Protein Synthesis ◽  
G Protein ◽  
Protein Turnover ◽  
The Elderly ◽  
Young Group ◽  
Whole Body ◽  
Protein Breakdown ◽  
Body Protein

Body composition, resting energy expenditure (REE), and whole body protein metabolism were studied in 26 young and 28 elderly Gambian men matched for body mass index during the dry season in a rural village in The Gambia. REE was measured by indirect calorimetry (hood system) in the fasting state and after five successive meals. Rates of whole body nitrogen flux, protein synthesis, and protein breakdown were determined in the fed state from the level of isotopic enrichment of urinary ammonia over a period of 12 h after a single oral dose of [15N]glycine. Expressed in absolute value, REE was significantly lower in the elderly compared with the young group (3.21 +/- 0.07 vs. 4.04 +/- 0.07 kJ/min, P < 0.001) and when adjusted to body weight (3.29 +/- 0.05 vs. 3.96 +/- 0.05 kJ/min, P < 0.0001) and fat-free mass (FFM; 3.38 +/- 0.01 vs. 3.87 +/- 0.01 kJ/min, P < 0.0001). The rate of protein synthesis averaged 207 +/- 13 g protein/day in the elderly and 230 +/- 13 g protein/day in the young group, whereas protein breakdown averaged 184 +/- 13 g protein/day in the elderly and 203 +/- 13 g protein/day in the young group (nonsignificant). When values were adjusted for body weight or FFM, they did not reveal any difference between the two groups. It is concluded that the reduced REE adjusted for body composition observed in elderly Gambian men is not explained by a decrease in protein turnover.

Increased Whole Body Protein Breakdown Predominates over Increased Whole Body Protein Synthesis in Multiple Organ Failure

1993 ◽  
Vol 84 (6) ◽  
pp. 655-661 ◽  
Author(s):  
J. Arnold ◽  
I. T. Campbell ◽  
Therese A. Samuels ◽  
J. C. Devlin ◽  
Ceri J. Green ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Multiple Organ Failure ◽  
Organ Failure ◽  
Protein Turnover ◽  
Multiple Organ ◽  
Whole Body ◽  
Protein Breakdown ◽  
Body Protein ◽  
Control Subjects ◽  
Healthy Control

1. Whole body protein turnover was measured using a primed-constant infusion of L-[1−13C]leucine with measurement of breath 13CO2 production and plasma 13C α-ketoisocaproate enrichment. Ten fasting patients, requiring mechanical ventilation and suffering from multiple organ failure, and six healthy control subjects were studied. 2. Protein breakdown and leucine removal from the plasma for protein synthesis were significantly higher in the patients than in the control subjects (P <0.01). In addition, leucine oxidation was almost 75% higher in the patients than in the healthy control subjects (P <0.05). 3. Plasma concentrations of glucose, insulin and growth hormone were not different between the two groups, but those of glucagon (not significant), noradrenaline (P <0.05) and cortisol (P <0.01) were almost two- and three-fold higher in the patients than in the control subjects. 4. Mean energy expenditure, measured by indirect calorimetry, was 30% higher in the patients than in the healthy control subjects (P <0.01). 5. Combining the data from both groups of subjects and using multiple regression analysis, cortisol was found to be the most significant predictor of (i) protein breakdown (48% of variance explained), (ii) leucine oxidation (69%) and (iii) hourly energy expenditure (54%). 6. The present investigation using [13C]leucine tracer methods demonstrated, in patients with multiple organ failure, that whole body protein breakdown and synthesis increased concomitantly and were twice as high as rates measured in healthy control subjects. Of the hormones measured in the present study, Cortisol appears to have the most significant effect on whole body protein turnover.

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