Routine Yoga Practice Impacts Whole Body Protein Utilization in Healthy Women

2018 ◽  
Vol 26 (1) ◽  
pp. 68-74 ◽  
Author(s):  
Megan Colletto ◽  
Nancy Rodriguez
Keyword(s):  
Older Women ◽  
Muscle Mass ◽  
Whole Body ◽  
Yoga Practice ◽  
Alternative Mode ◽  
Protein Utilization ◽  
Body Protein ◽  
Functional Measures ◽  
Q Protein

Whole body protein utilization (WBPU), which includes flux (Q), protein synthesis (PS), protein breakdown (PB), and whole body protein balance (WBPB), provides insight regarding muscle mass, a criterion for sarcopenia. To characterize yoga’s impact on WBPU, body composition and functional measures in healthy (50–65 years) women. WBPU and functional measures were compared between women who routinely practiced yoga (YOGA; n = 7) and nonactive counterparts (CON; n = 8). Q (0.61 ± 0.06 vs. 0.78 ± 0.07,p = .04), PS (3.07 ± 0.37 vs. 4.17 ± 0.40,p = .03), PB (2.59 ± 0.48 vs. 3.80 ± 0.48,p = .05) were lower, and lean body mass higher (64 ± 1 vs. 58 ± 2%,p ≤ .01) for YOGA vs. CON, respectively. WBPB and functional measures were similar. Routine yoga practice influenced WBPU in healthy older women. Study findings are novel and provide a basis for future investigations evaluating long-term benefits of yoga as an alternative mode of exercise for maintaining muscle mass in support of active aging.

Whole-body protein utilization in humans

1987 ◽  
Vol 19 (Supplement) ◽  
pp. S166???S171 ◽  
Author(s):  
GAIL E. BUTTERFIELD
Keyword(s):  
Whole Body ◽  
Protein Utilization ◽  
Body Protein

Whole Body Protein Turnover in Chronically Undernourished Individuals

1994 ◽  
Vol 86 (4) ◽  
pp. 441-446 ◽  
Author(s):  
M. J. Soares ◽  
L. S. Piers ◽  
P. S. Shetty ◽  
A. A. Jackson ◽  
J. C. Waterlow
Keyword(s):  
Body Weight ◽  
Protein Synthesis ◽  
Metabolic Rate ◽  
Muscle Mass ◽  
Basal Metabolic Rate ◽  
Normal Weight ◽  
Fat Free Mass ◽  
Whole Body ◽  
Body Protein ◽  
Chronic Undernutrition

1. Two groups of adult men were studied in Bangalore, India, under identical conditions: the ‘normal weight’ subjects (mean body mass index 20.8 kg/m2) were medical students of the institute with access to habitual energy and protein intakes ad libitum. The other group, designated ‘undernourished’, were labourers on daily wages (mean body mass index 16.7 kg/m2). 2. In an earlier study we obtained lower absolute values for both basal metabolic rate and protein synthesis in the undernourished subjects; however, when the data were expressed on a body weight or fat-free mass basis, a trend towards higher rates of protein synthesis, as well as higher basal metabolic rate, was evident. The suggestion was made that such results reflected the relatively higher energy intakes per kg body weight of the undernourished subjects on the day of study. The objective of the present study was therefore to control for the dietary intake during the measurement of whole body protein turnover. 3. In the present study dietary intakes were equated on a body weight basis; however, expressed per kg fat-free mass, the normal weight subjects had received marginally higher intakes of energy and protein. The results, however, were similar to those of the previous study. In absolute terms, basal metabolic rate, protein synthesis and breakdown were lower in the undernourished subjects. When expressed per kg body weight or per kg fat-free mass, the undernourished subjects had higher basal metabolic rates than the well-nourished subjects, whereas no differences were seen in the rate of protein synthesis or breakdown. 4. Estimates of muscle mass, based on creatinine excretion, indicated that the undernourished subjects had a higher proportion of non-muscle to muscle mass. Nitrogen flux (Q) was determined from 15N abundance in two end products, urea (Qu) and ammonia (Qa). The ratio Qu/Qa was increased in the undernourished subjects and was significantly correlated with the ratio of non-muscle to muscle mass (r = 0.81; P < 0.005). These results fit in with our earlier suggestion of a greater proportion of non-muscle (visceral) mass in undernourished subjects. 5. The present data suggest that there are no changes in the rate of protein synthesis or breakdown in chronic undernutrition when results are expressed, conventionally, per kg fat-free mass. It can be theoretically shown, however, that there could be a 15% reduction in the rate of turnover of the visceral tissues in chronic undernutrition. This, together with the reduced urinary nitrogen excretion, would contribute to nitrogen economy in these individuals.

scholarly journals Correction of acidosis in hemodialysis decreases whole-body protein degradation.

1997 ◽  
Vol 8 (4) ◽  
pp. 632-637 ◽  
Author(s):  
K A Graham ◽  
D Reaich ◽  
S M Channon ◽  
S Downie ◽  
T H Goodship
Keyword(s):  
Renal Failure ◽  
Protein Degradation ◽  
Protein Turnover ◽  
Whole Body ◽  
Body Protein ◽  
Chronic Metabolic Acidosis ◽  
Optimal Correction ◽  
Kinetics Of ◽  
Amino Acid Concentrations

Correction of acidosis in hemodialysis (HD) decreases protein degradation. The effect of the correction of chronic metabolic acidosis in chronic renal failure patients treated with HD was determined from the kinetics of infused L-[1-(13)C]leucine. Six HD patients were studied before (acid) and after (bicarbonate) correction of acidosis (pH: acid 7.36 +/- 0.01, bicarbonate 7.40 +/- 0.01, P < 0.005). Leucine appearance from body protein (PD) and leucine disappearance into body protein (PS) decreased significantly with correction of acidosis (PD: acid 180.6 +/- 7.3, bicarbonate 130.9 +/- 7.2 mumol.kg-1.h-1, P < 0.005; PS: acid 172.3 +/- 6.8, bicarbonate 122.0 +/- 6.8 mumol.kg-1.h-1, P < 0.005). There was no significant change in leucine oxidation or plasma amino acid concentrations. These results demonstrate that optimal correction of acidosis in HD is beneficial in terms of protein turnover and may improve long-term nutritional status in HD.

Growth equations for skeletal muscle derived from the cytonuclear ratio and growth constraining supplementary functions

1999 ◽  
Vol 68 (1) ◽  
pp. 129-140 ◽  
Author(s):  
C. Z. Roux
Keyword(s):  
Muscle Mass ◽  
Whole Body ◽  
Muscle Fibres ◽  
Cell Nuclei ◽  
Cross Sectional ◽  
Body Protein ◽  
Mass Growth ◽  
Growth Constraints ◽  
The Difference ◽  
Almost All

AbstractFor purely hypertrophic muscle it is postulated that the growth rate in number of nuclei is proportional to the cytoplasmic mass per nucleus multiplied by a growth constraining supplementary function. Growth constraint depends on the distance from any one of the limit number of nuclei, the limit muscle mass or the limit cytoplasmic mass per nucleus. Furthermore, theory and evidence are presented for a power (allometric) relationship between total number of nuclei (n) and muscle mass (m) given by the equation n = gmh. Evidence points to two clusters of values for h, one in the vicinity of h = 2/3 and the other h = 1/2. Both may depend on a linear relationship between number of nuclei inside muscle fibre and fibre cross-sectional area. The difference between the two situations can be derived from basic assumptions on either local or systemic diffusion mediated control of the number or division of satellite cell nuclei, leading directly to values of h either equal to 2/3 or V2. For likely values of h and suitable choices of growth constraints, almost all well known growth functions in the literature are derived as potentially applicable to total number of nuclei, or muscle mass or their ratio. Muscle mass growth will show a sigmoidal form for h = 1. This explains sigmoidal growth in body mass as it is mostly dominated by muscle mass. A possible linear growth phase before maturity is explicable from the cessation of either length (h = 1) or nuclear (h = 0) growth in muscle fibres, while cytoplasmic growth continues to maturity. Furthermore, two rat examples indicate that whole body protein growth can be described by the equations derived for muscle mass growth.

scholarly journals Impact of Growth Hormone and Dehydroepiandrosterone on Protein Metabolism in Glucocorticoid-Treated Patients

2008 ◽  
Vol 93 (3) ◽  
pp. 688-695 ◽  
Author(s):  
Morton G. Burt ◽  
Gudmundur Johannsson ◽  
A. Margot Umpleby ◽  
Donald J. Chisholm ◽  
Ken K. Y. Ho
Keyword(s):  
Protein Metabolism ◽  
Dose Finding ◽  
Whole Body ◽  
Constant Infusion ◽  
Leucine Incorporation ◽  
Protein Loss ◽  
Body Protein ◽  
Prednisone Dose ◽  
Leucine Oxidation

Abstract Context: Chronic pharmacological glucocorticoid (GC) use causes substantial morbidity from protein wasting. GH and androgens are anabolic agents that may potentially reverse GC-induced protein loss. Objective: Our objective was to assess the effect of GH and dehydroepiandrosterone (DHEA) on protein metabolism in subjects on long-term GC therapy. Design: This was an open, stepwise GH dose-finding study (study 1), followed by a randomized cross-over intervention study (study 2). Setting: The studies were performed at a clinical research facility. Patients and Intervention: In study 1, six subjects (age 69 ± 4 yr) treated with long-term (&gt;6 months) GCs (prednisone dose 8.3 ± 0.8 mg/d) were studied before and after two sequential GH doses (0.8 and 1.6 mg/d) for 2 wk each. In study 2, 10 women (age 71 ± 3 yr) treated with long-term GCs (prednisone dose 5.4 ± 0.5 mg/d) were studied at baseline and after 2-wk treatment with GH 0.8 mg/d, DHEA 50 mg/d, or GH and DHEA (combination treatment). Main Outcome Measure: Changes in whole body protein metabolism were assessed using a 3-h primed constant infusion of 1-[13C]leucine, from which rates of leucine appearance, leucine oxidation, and leucine incorporation into protein were estimated. Results: In study 1, GH 0.8 and 1.6 mg/d significantly reduced leucine oxidation by 19% (P = 0.03) and 31% (P = 0.02), and increased leucine incorporation into protein by 10% (P = 0.13) and 19% (P = 0.04), respectively. The lower GH dose did not cause hyperglycemia, whereas GH 1.6 mg/d resulted in fasting hyperglycemia in two of six subjects. In study 2, DHEA did not significantly change leucine metabolism alone or when combined with GH. Blood glucose was not affected by DHEA. Conclusion: GH, at a modest supraphysiological dose of 0.8 mg/d, induces protein anabolism in chronic GC users without causing diabetes. DHEA 50 mg/d does not enhance the effect of GH. GH may safely prevent or reverse protein loss induced by chronic GC therapy.

scholarly journals Effects of long-term protein excess or deficiency on whole-body protein turnover in sheep nourished by intragastric infusion of nutrients

1995 ◽  
Vol 73 (6) ◽  
pp. 829-839 ◽  
Author(s):  
S. M. Liu ◽  
G. E. Lobley ◽  
N. A. Macleod ◽  
D. J. Kyle ◽  
X.B. Chen ◽  
...  
Keyword(s):  
Dietary Protein ◽  
Protein Turnover ◽  
Protein Intake ◽  
Volatile Fatty Acids ◽  
Whole Body ◽  
N Losses ◽  
Body Protein ◽  
Fractional Rate ◽  
The Difference

The effect of long-term dietary protein excess and deficit on whole-body protein-N turnover (WBPNT) was examined in lambs nourished by intragastric infusions of nutrients. Ten sheep were given 500 mg N/kg metabolic weight (W0.75) per d from casein for 2 weeks and then either 50 (L), 500 (M) or 1500 (H) mg N/kgW0.75per d for 6 weeks. Volatile fatty acids were infused at 500 kJ/kgW0.75per d. Daily WBPNT was measured by continuous intravenous infusion of [l-13C]leucine 3 d before, and on days 2, 21 and 42 after the alteration in protein intake. Whole-body protein-N synthesis (WBPNS) was calculated as the difference between WBPNT and the protein-N losses as urinary NH3and urea. Whole-body protein-N degradation (WBPNS) was then estimated from WBPNS minus protein gain determined from N balance. Fractional rates of WBPNS and WBPND were calculated against fleece-free body N content. WBPNS rates at the L, M and H intakes were respectively 35·1, 41·5 amd 6·37 g/d (P< 0.001) on average over the 6 weeks and WBPND rates were 39·5, 41·1 and 56·8 g/d (P< 0.001). The fractional rates of WBPNS were 5·01, 6·37 and 7·73% per d (P< 0.001) while those of WBPND were 5·64, 6·29 and 6·81% per d (P< 0.005) respectively. On days 2, 21 and 42, WBPNS rates at intake H were 54·0, 61·8 and 75·4 g/d (P= 0·03) respectively, and WBPND rates were 43·2, 56·4 and 70·9 g/d (P= 0.03); at intake L the amounts were 38·2, 34·2 and 32·8 g/d for WBPNS (P= 0.003) and for WBPND were 43·4, 38·0 and 36·9 g/d (P= 0·016) respectively. There were no significant (P> 0·05) differences in fractional rates of WBPNS and WBPND with time at either the L or H intake. We concluded that absolute protein turnover was affected both by dietary protein intake and by body condition while the fractional rate of turnover was predominantly influenced by intake.

Effect of testosterone on muscle mass and muscle protein synthesis

1989 ◽  
Vol 66 (1) ◽  
pp. 498-503 ◽  
Author(s):  
R. C. Griggs ◽  
W. Kingston ◽  
R. F. Jozefowicz ◽  
B. E. Herr ◽  
G. Forbes ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Muscle Mass ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Whole Body ◽  
Synthesis Rate ◽  
Protein Synthesis Rate ◽  
Total Body Potassium ◽  
Body Protein ◽  
Total Body

We have studied the effect of a pharmacological dose of testosterone enanthate (3 mg.kg-1.wk-1 for 12 wk) on muscle mass and total-body potassium and on whole-body and muscle protein synthesis in normal male subjects. Muscle mass estimated by creatinine excretion increased in all nine subjects (20% mean increase, P less than 0.02); total body potassium mass estimated by 40K counting increased in all subjects (12% mean increase, P less than 0.0001). In four subjects, a primed continuous infusion protocol with L-[1–13C]leucine was used to determine whole-body leucine flux and oxidation. Whole-body protein synthesis was estimated from nonoxidative flux. Muscle protein synthesis rate was determined by measuring [13C]leucine incorporation into muscle samples obtained by needle biopsy. Testosterone increased muscle protein synthesis in all subjects (27% mean increase, P less than 0.05). Leucine oxidation decreased slightly (17% mean decrease, P less than 0.01), but whole-body protein synthesis did not change significantly. Muscle morphometry showed no significant increase in muscle fiber diameter. These studies suggest that testosterone increases muscle mass by increasing muscle protein synthesis.

scholarly journals Long-Term Effects of Histidine Depletion on Whole-Body Protein Metabolism in Healthy Adults

2002 ◽  
Vol 132 (11) ◽  
pp. 3340-3348 ◽  
Author(s):  
Wantanee Kriengsinyos ◽  
Mahroukh Rafii ◽  
Linda J. Wykes ◽  
Ronald O. Ball ◽  
Paul B. Pencharz
Keyword(s):  
Protein Metabolism ◽  
Healthy Adults ◽  
Whole Body ◽  
Long Term Effects ◽  
Body Protein

Effect of Exercise on Protein Turnover in Man

1981 ◽  
Vol 61 (5) ◽  
pp. 627-639 ◽  
Author(s):  
M. J. Rennie ◽  
R. H. T. Edwards ◽  
S. Krywawych ◽  
C. T. M. Davies ◽  
D. Halliday ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Turnover ◽  
Whole Body ◽  
Protein Breakdown ◽  
Body Protein ◽  
Fractional Rate ◽  
Plasma And Urine Samples ◽  
Amino Acid Concentrations ◽  
Substantial Rise

1. We have investigated the effects of moderate long-term exercise on protein turnover in fed man by measuring the extent of whole-body nitrogen production, the labelling of urinary ammonia from ingested [15N]glycine and plasma, muscle and urine free amino acid concentrations. 2. Judged both from nitrogen production, and from the extent of 13CO2 production from ingested l-[l-13C]leucine, exercise causes a substantial rise in amino acid catabolism. 3. Amino acids catabolized during exercise appear to become available through a fall in whole-body protein synthesis and a rise in whole-body protein breakdown. After exercise, protein balance becomes positive through a rise in the rate of whole-body synthesis in excess of breakdown. 4. Studies of free 3-methylhistidine in muscle, plasma and urine samples suggest that exercise decreases the fractional rate of myofibrillar protein breakdown, in contrast with the apparent rise in whole-body breakdown.

mTORC1 and the regulation of skeletal muscle anabolism and mass

2012 ◽  
Vol 37 (3) ◽  
pp. 395-406 ◽  
Author(s):  
Olasunkanmi A.J. Adegoke ◽  
Abdikarim Abdullahi ◽  
Pegah Tavajohi-Fini
Keyword(s):  
Skeletal Muscle ◽  
Resistance Exercise ◽  
Muscle Mass ◽  
Muscle Wasting ◽  
Mammalian Target Of Rapamycin ◽  
Muscle Metabolism ◽  
Whole Body ◽  
Muscle Health ◽  
Increased Activity

The mass and integrity of skeletal muscle is vital to whole-body substrate metabolism and health. Indeed, defects in muscle metabolism and functions underlie or exacerbate diseases like diabetes, rheumatoid arthritis, and cancer. Physical activity and nutrition are the 2 most important environmental factors that can affect muscle health. At the molecular level, the mammalian target of rapamycin complex 1 (mTORC1) is a critical signalling complex that regulates muscle mass. In response to nutrition and resistance exercise, increased muscle mass and activation of mTORC1 occur in parallel. In this review, we summarize recent findings on mTORC1 and its regulation in skeletal muscle in response to resistance exercise, alone or in combination with intake of protein or amino acids. Because increased activity of the complex is implicated in the development of muscle insulin resistance, obesity, and some cancers (e.g., ovarian, breast), drugs that target mTORC1 are being developed or are in clinical trials. However, various cancers are associated with extensive muscle wasting, due in part to tumour burden and malnutrition. This muscle wasting may also be a side effect of anticancer drugs. Because loss of muscle mass is associated not only with metabolic abnormalities but also dose limiting toxicity, we review the possible implications for skeletal muscle of long-term inhibition of mTORC1, especially in muscle wasting conditions.

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