scholarly journals Branched-Chain Amino Acid Oxidation Is Elevated in Adults with Morbid Obesity and Decreases Significantly after Sleeve Gastrectomy

2020 ◽  
Vol 150 (12) ◽  
pp. 3180-3189
Author(s):  
Hong Chang Tan ◽  
Jean W Hsu ◽  
Jean-Paul Kovalik ◽  
Alvin Eng ◽  
Weng Hoong Chan ◽  
...  
Keyword(s):  
Morbid Obesity ◽  
Sleeve Gastrectomy ◽  
Plasma Concentrations ◽  
Fat Free Mass ◽  
Acid Oxidation ◽  
Morbidly Obese ◽  
Healthy Weight ◽  
Leucine Oxidation ◽  
Branched Chain Amino Acid ◽  
Branched Chain

ABSTRACT Background Plasma concentrations of branched-chain amino acids (BCAAs) are elevated in obese individuals with insulin resistance (IR) and decrease after bariatric surgery. However, the metabolic mechanisms are unclear. Objectives Our objectives are to compare leucine kinetics between morbidly obese and healthy-weight individuals cross-sectionally, and to prospectively evaluate changes in the morbidly obese after sleeve gastrectomy. We hypothesized that leucine oxidation is slower in obese individuals and increases after surgery. Methods Ten morbidly obese [BMI (in kg/m2) ≥32.5, age 21–50 y] and 10 healthy-weight participants (BMI <25), matched for age (median ∼30 y) but not gender, were infused with [U-13C6] leucine and [2H5] glycerol to quantify leucine and glycerol kinetics. Morbidly obese participants were studied again 6 mo postsurgery. Primary outcomes were kinetic parameters related to BCAA metabolism. Data were analyzed by nonparametric methods and presented as median (IQR). Results Participants with obesity had IR with an HOMA-IR (4.89; 4.36–8.76) greater than that of healthy-weight participants (1.32; 0.99–1.49; P < 0.001) and had significantly faster leucine flux [218; 196–259 compared with 145; 138–149 μmol · kg fat-free mass (FFM)−1 · h−1], oxidation (24.0; 17.9–29.8 compared with 16.1; 14.3–18.5 μmol · kg FFM−1 · h−1), and nonoxidative disposal (204; 190–247 compared with 138; 129–140 μmol · kg FFM−1 · h−1) (P < 0.017 for all). After surgery, the morbidly obese had a marked improvement in IR (3.54; 3.06–6.08; P = 0.008) and significant reductions in BCAA concentrations (113; 95–157 μmol/L) and leucine oxidation (9.37; 6.85–15.2 μmol · kg FFM−1 · h−1) (P = 0.017 for both). Further, leucine flux in this group correlated significantly with IR (r = 0.78, P < 0.001). Conclusions BCAA oxidation is not impaired but elevated in individuals with morbid obesity. Plasma BCAA concentrations are lowered after surgery owing to slower breakdown of body proteins as insulin's ability to suppress proteolysis is restored. These findings suggest that IR is the underlying cause and not the consequence of elevated BCAAs in obesity.

Morbid obesity in the UK: A modelling projection study to 2035

2018 ◽  
Vol 48 (4) ◽  
pp. 422-427 ◽  
Author(s):  
Laura Keaver ◽  
Benshuai Xu ◽  
Abbygail Jaccard ◽  
Laura Webber
Keyword(s):  
Body Mass Index ◽  
Morbid Obesity ◽  
Body Mass ◽  
Communicable Disease ◽  
Age Groups ◽  
Morbidly Obese ◽  
Healthy Weight ◽  
Individual Level ◽  
Annual Distribution ◽  
The Uk

Background: Morbid obesity (body mass index ⩾40 kg/m2) carries a higher risk of non-communicable disease and is associated with more complex health issues and challenges than obesity body mass index ≥30kg/m2 and <40kg/m2, resulting in much higher financial implications for health systems. Although obesity trends have previously been projected to 2035, these projections do not separate morbid obesity from obesity. This study therefore complements these projections and looks at the prevalence and development of morbid obesity in the UK. Methods: Individual level body mass index data for people aged >15 years in England, Wales (2004–2014) and Scotland (2008–2014) were collated from national surveys and stratified by sex and five-year age groups (e.g. 15–19 years), then aggregated to calculate the annual distribution of healthy weight, overweight, obesity and morbid obesity for each age and sex group. A categorical multi-variate non-linear regression model was fitted to these distributions to project trends to 2035. Results: The prevalence of morbid obesity was predicted to increase to 5, 8 and 11% in Scotland, England and Wales, respectively, by 2035. Welsh women aged 55–64 years had the highest projected prevalence of 20%. In total, almost five million people are forecast to be classified as morbidly obese across the three countries in 2035. Conclusions: The prevalence of morbid obesity is predicted to increase by 2035 across the three UK countries, with Wales projected to have the highest rates. This is likely to have serious health and financial implications for society and the UK health system.

Effect of carnitine on branched-chain amino acid oxidation by liver and skeletal muscle.

1978 ◽  
Vol 234 (5) ◽  
pp. E494 ◽  
Author(s):  
H S Paul ◽  
S A Adibi
Keyword(s):  
Amino Acids ◽  
Liver Mitochondria ◽  
Branched Chain Amino Acids ◽  
Diabetic Rats ◽  
Acid Oxidation ◽  
Acyltransferase Activity ◽  
Remarkable Effect ◽  
Carnitine Acyltransferase ◽  
Branched Chain Amino Acid ◽  
Branched Chain

The effect of L-carnitine (0.5-2.0 mM) on the rates of alpha-decarboxylation of 1-14C-labeled branched-chain amino acids by gastrocnemius muscle and liver homogenates of fed rats was investigated. Carnitine increased the rate of alpha-decarboxylation of leucine (125%) and valine (28%) by muscle, but it was without effect on the oxidation of these amino acids by liver. Carnitine increased the rate of alpha-decarboxylation of alpha-ketoisocaproate by both tissues. This effect was more pronounced in muscle (130% increase) than in liver (41% increase). The activity of carnitine acyltransferase, with isovaleryl-CoA as a substrate, was 18 times higher in muscle mitochondria than in liver mitochondria. Both starvation and diabetes increased the rate of alpha-decarboxylation of leucine by muscle without having a remarkable effect on the concentration of carnitine or the activity of carnitine acyltransferase. We conclude that: a) carnitine stimulates decarboxylation of branched-chain amino acids by increasing the conversion of their ketoanalogues into carnitine esters, b) a greater carnitine acyltransferase activity in muscle than in liver may be responsible for the greater carnitine effect in muscle, c) carnitine does not appear responsible for the enhancement of leucine oxidation by muscle of starved and diabetic rats.

scholarly journals Two mechanisms produce tissue-specific inhibition of fatty acid oxidation by oxfenicine

1985 ◽  
Vol 227 (2) ◽  
pp. 651-660 ◽  
Author(s):  
T W Stephens ◽  
A J Higgins ◽  
G A Cook ◽  
R A Harris
Keyword(s):  
Fatty Acid ◽  
Amino Acid ◽  
Fatty Acid Oxidation ◽  
Carnitine Palmitoyltransferase ◽  
Partial Purification ◽  
Acid Oxidation ◽  
Branched Chain Amino Acid ◽  
Malonyl Coa ◽  
Carnitine Palmitoyltransferase I ◽  
Branched Chain

Oxfenicine [S-2-(4-hydroxyphenyl)glycine] is transaminated in heart and liver to 4-hydroxyphenylglyoxylate, an inhibitor of fatty acid oxidation shown in this study to act at the level of carnitine palmitoyltransferase I (EC 2.3.1.21). Oxfenicine was an effective inhibitor of fatty acid oxidation in heart, but not in liver. Tissue specificity of oxfenicine inhibition of fatty acid oxidation was due to greater oxfenicine transaminase activity in heart and to greater sensitivity of heart carnitine palmitoyltransferase I to inhibition by 4-hydroxyphenylglyoxylate [I50 (concentration giving 50% inhibition) of 11 and 510 microM for the enzymes of heart and liver mitochondria, respectively]. Branched-chain-amino-acid aminotransferase (isoenzyme I, EC 2.6.1.42) was responsible for the transamination of oxfenicine in heart. A positive correlation was found between the capacity of various tissues to transaminate oxfenicine and the known content of branched-chain-amino-acid aminotransferase in these tissues. Out of three observed liver oxfenicine aminotransferase activities, one may correspond to asparagine aminotransferase, but the major activity could not be identified by partial purification and characterization. As reported previously for malonyl-CoA inhibition of carnitine palmitoyltransferase I, 4-hydroxyphenylglyoxylate inhibition of this enzyme was found to be very pH-dependent. In striking contrast with the kinetics of malonyl-CoA inhibition, 4-hydroxyphenylglyoxylate inhibition was not affected by oleoyl-CoA concentration, but was partially reversed by increasing carnitine concentrations.

Prolonged submaximal eccentric exercise is associated with increased levels of plasma IL-6

1997 ◽  
Vol 273 (1) ◽  
pp. E85-E91 ◽  
Author(s):  
T. Rohde ◽  
D. A. MacLean ◽  
E. A. Richter ◽  
B. Kiens ◽  
B. K. Pedersen
Keyword(s):  
Eccentric Exercise ◽  
Proliferative Response ◽  
Muscle Protein ◽  
Plasma Concentrations ◽  
Cytokine Response ◽  
Cytotoxic Activities ◽  
Branched Chain Amino Acid ◽  
Muscle Protein Degradation ◽  
Branched Chain ◽  
The Relationship

To study the relationship between exercise-related muscle proteolysis and the cytokine response, a prolonged eccentric exercise model of one leg was used. Subjects performed two trials [a branched-chain amino acid (BCAA) supplementation and a control trial]. The release of amino acids from muscle during and after the eccentric exercise was decreased in the BCAA trial, suggesting a suppression of net muscle protein degradation. The plasma concentrations of interleukin (IL)-6 increased from 0.75 +/- 0.19 (preexercise) to 5.02 +/- 0.96 pg/ml (2 h postexercise) in the control trial and in the BCAA supplementation trial from 1.07 +/- 0.41 to 4.15 +/- 1.21 pg/ml. Eccentric exercise had no effect on the concentrations of neutrophils, lymphocytes, CD16+/CD56+, CD4+, CD8+, CD14+/CD38+, lymphocyte proliferative response, or cytotoxic activities. BCAA supplementation reduced the concentration of CD14+/CD38+ cells. This study shows that the concentration of IL-6 in plasma is increased after prolonged eccentric exercise and suggests that the cytokine response is independent of the muscle proteolysis that occur during exercise.

scholarly journals Carbohydrate, Protein, and Fat Metabolism during Exercise after Oral Carnitine Supplementation in Humans

2008 ◽  
Vol 18 (6) ◽  
pp. 567-584 ◽  
Author(s):  
Elizabeth M. Broad ◽  
Ronald J. Maughan ◽  
Stuart D.R Galloway
Keyword(s):  
Metabolic Stress ◽  
Nitrogen Excretion ◽  
Moderate Intensity ◽  
Acid Oxidation ◽  
Plasma Urea ◽  
Branched Chain Amino Acid ◽  
Before And After ◽  
Branched Chain ◽  
Response To Exercise ◽  
To Receive

Twenty nonvegetarian active males were pair-matched and randomly assigned to receive 2 g of L-carnitine L-tartrate (LC) or placebo per day for 2 wk. Participants exercised for 90 min at 70% VO2max after 2 days of a prescribed diet (M ±SD: 13.6 ± 1.6 MJ, 57% carbohydrate, 15% protein, 26% fat, 2% alcohol) before and after supplementation. Results indicated no change in carbohydrate oxidation, nitrogen excretion, branched-chain amino acid oxidation, or plasma urea during exercise between the beginning and end of supplementation in either group. After 2 wk of LC supplementation the plasma ammonia response to exercise tended to be suppressed (0 vs. 2 wk at 60 min exercise, 97 ± 26 vs. 80 ± 9, and 90 min exercise, 116 ± 47 vs. 87 ± 25 μmol/L), with no change in the placebo group. The data indicate that 2 wk of LC supplementation does not affect fat, carbohydrate, and protein contribution to metabolism during prolonged moderate-intensity cycling exercise. The tendency toward suppressed ammonia accumulation, however, indicates that oral LC supplementation might have the potential to reduce the metabolic stress of exercise or alter ammonia production or removal, which warrants further investigation.

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