Arginine plus proline supplementation elicits metabolic adaptation that favors wound healing in diabetic rats

2012 ◽  
Vol 303 (10) ◽  
pp. R1053-R1061 ◽  
Author(s):  
A. Raynaud-Simon ◽  
L. Belabed ◽  
G. Le Naour ◽  
J. Marc ◽  
F. Capron ◽  
...  
Keyword(s):  
Nitric Oxide ◽  
Wound Healing ◽  
Amino Acid ◽  
Nitrogen Balance ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Diabetic Rats ◽  
Male Rats ◽  
Whole Body ◽  
Metabolic Adaptation

Diabetic patients with wounds are at risk of protein malnutrition, have low arginine plasma levels, and suffer from delayed wound healing. We sought to determine the efficacy of arginine plus proline supplementation on protein and amino acid metabolism and on wound repair in a model of diabetic rats. Eighteen 11-wk-old Zucker diabetic fatty fa/fa male rats underwent a 7-cm abdominal skin incision with implantation of sponges and daily excision of full-thickness round sections of dorsal skin for 5 days. They were randomized to be fed with either a standard formula (S group, Clinutren Iso), a high-protein and arginine (ARG) plus proline (PRO)-enriched formula (ARG+PRO group, Clinutren Repair), or an isonitrogenous isoenergetic control formula (IC group). Nitrogen balance was calculated daily. The rats were euthanized on day 5, and plasma glucose, insulin, amino acids, skin epithelialization, and angiogenesis were measured. In macrophages, we assessed inducible nitric oxide synthase (iNOS) and arginase expression, production of nitric oxide (NO) and amino acid metabolism. Both the ARG+PRO and IC groups showed improved nitrogen balance. ARG plus PRO supplementation increased proline and branched-chain amino acid plasma concentrations and improved angiogenesis. Arginase and iNOS expressions in macrophages were reduced, together with NO and citrulline production. In diabetic rats, ARG plus PRO supplementation improves wound angiogenesis and favors whole body protein metabolism. Low macrophage iNOS expression at day 5 may reflect a low inflammatory state in the wounds, favoring wound closure.

scholarly journals Interactive effects of aging and aerobic capacity on energy metabolism–related metabolites of serum, skeletal muscle, and white adipose tissue

GeroScience ◽  
2021 ◽  
Author(s):  
Haihui Zhuang ◽  
Sira Karvinen ◽  
Timo Törmäkangas ◽  
Xiaobo Zhang ◽  
Xiaowei Ojanen ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Amino Acid ◽  
White Adipose Tissue ◽  
Aerobic Capacity ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Disease Risk ◽  
Whole Body ◽  
Whole Body Metabolism

AbstractAerobic capacity is a strong predictor of longevity. With aging, aerobic capacity decreases concomitantly with changes in whole body metabolism leading to increased disease risk. To address the role of aerobic capacity, aging, and their interaction on metabolism, we utilized rat models selectively bred for low and high intrinsic aerobic capacity (LCRs/HCRs) and compared the metabolomics of serum, muscle, and white adipose tissue (WAT) at two time points: Young rats were sacrificed at 9 months of age, and old rats were sacrificed at 21 months of age. Targeted and semi-quantitative metabolomics analysis was performed on the ultra-pressure liquid chromatography tandem mass spectrometry (UPLC-MS) platform. The effects of aerobic capacity, aging, and their interaction were studied via regression analysis. Our results showed that high aerobic capacity is associated with an accumulation of isovalerylcarnitine in muscle and serum at rest, which is likely due to more efficient leucine catabolism in muscle. With aging, several amino acids were downregulated in muscle, indicating more efficient amino acid metabolism, whereas in WAT less efficient amino acid metabolism and decreased mitochondrial β-oxidation were observed. Our results further revealed that high aerobic capacity and aging interactively affect lipid metabolism in muscle and WAT, possibly combating unfavorable aging-related changes in whole body metabolism. Our results highlight the significant role of WAT metabolism for healthy aging.

scholarly journals Impact of habituated dietary protein intake on fasting and postprandial whole-body protein turnover and splanchnic amino acid metabolism in elderly men: a randomized, controlled, crossover trial

2020 ◽  
Vol 112 (6) ◽  
pp. 1468-1484 ◽  
Author(s):  
Grith Højfeldt ◽  
Jacob Bülow ◽  
Jakob Agergaard ◽  
Ali Asmar ◽  
Peter Schjerling ◽  
...  
Keyword(s):  
Amino Acid ◽  
Protein Turnover ◽  
Protein Intake ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
High Protein ◽  
Whole Body ◽  
Body Protein ◽  
Protein Absorption ◽  
Fasted State

ABSTRACT Background Efficacy of protein absorption and subsequent amino acid utilization may be reduced in the elderly. Higher protein intakes have been suggested to counteract this. Objectives We aimed to elucidate how habituated amounts of protein intake affect the fasted state of, and the stimulatory effect of a protein-rich meal on, protein absorption, whole-body protein turnover, and splanchnic amino acid metabolism. Methods Twelve men (65–70 y) were included in a double-blinded crossover intervention study, consisting of a 20-d habituation period to a protein intake at the RDA or a high amount [1.1 g · kg lean body mass (LBM)−1 · d−1 or >2.1 g · kg LBM−1 · d−1, respectively], each followed by an experimental trial with a primed, constant infusion of D8-phenylalanine and D2-tyrosine. Arterial and hepatic venous blood samples were obtained after an overnight fast and repeatedly 4 h after a standardized meal including intrinsically labeled whey protein concentrate and calcium-caseinate proteins. Blood was analyzed for amino acid concentrations and phenylalanine and tyrosine tracer enrichments from which whole-body and splanchnic amino acid and protein kinetics were calculated. Results High (compared with the recommended amount of) protein intake resulted in a higher fasting whole-body protein turnover with a resultant mean ± SEM 0.03 ± 0.01 μmol · kg LBM−1 · min−1 lower net balance (P < 0.05), which was not rescued by the intake of a protein-dense meal. The mean ± SEM plasma protein fractional synthesis rate was 0.13 ± 0.06%/h lower (P < 0.05) after habituation to high protein. Furthermore, higher fasting and postprandial amino acid removal were observed after habituation to high protein, yielding higher urea excretion and increased phenylalanine oxidation rates (P < 0.01). Conclusions Three weeks of habituation to high protein intake (>2.1 g protein · kg LBM−1 · d−1) led to a significantly higher net protein loss in the fasted state. This was not compensated for in the 4-h postprandial period after intake of a meal high in protein. This trial was registered at clinicaltrials.gov as NCT02587156.

Regional muscle and adipose tissue amino acid metabolism in lean and obese women

2002 ◽  
Vol 282 (4) ◽  
pp. E931-E936 ◽  
Author(s):  
Bruce W. Patterson ◽  
Jeffrey F. Horowitz ◽  
Guoyao Wu ◽  
Malcolm Watford ◽  
Simon W. Coppack ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Amino Acid ◽  
Abdominal Obesity ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Fat Free Mass ◽  
Whole Body ◽  
Obese Women ◽  
Body Protein ◽  
Isotope Tracer

The effect of obesity on regional skeletal muscle and adipose tissue amino acid metabolism is not known. We evaluated systemic and regional (forearm and abdominal subcutaneous adipose tissue) amino acid metabolism, by use of a combination of stable isotope tracer and arteriovenous balance methods, in five lean women [body mass index (BMI) <25 kg/m2] and five women with abdominal obesity (BMI 35.0–39.9 kg/m2; waist circumference >100 cm) who were matched on fat-free mass (FFM). All subjects were studied at 22 h of fasting to ensure that the subjects were in net protein breakdown during this early phase of starvation. Leucine rate of appearance in plasma (an index of whole body proteolysis), expressed per unit of FFM, was not significantly different between lean and obese groups (2.05 ± 0.18 and 2.34 ± 0.04 μmol · kg FFM−1 · min−1, respectively). However, the rate of leucine release from forearm and adipose tissues in obese women (24.0 ± 4.8 and 16.6 ± 6.5 nmol · 100 g−1 · min−1, respectively) was lower than in lean women (66.8 ± 10.6 and 38.6 ± 7.0 nmol · 100 g−1 · min−1, respectively; P < 0.05). Approximately 5–10% of total whole body leucine release into plasma was derived from adipose tissue in lean and obese women. The results of this study demonstrate that the rate of release of amino acids per unit of forearm and adipose tissue at 22 h of fasting is lower in women with abdominal obesity than in lean women, which may help obese women decrease body protein losses during fasting. In addition, adipose tissue is a quantitatively important site for proteolysis in both lean and obese subjects.

Exercise-Mediated Peripheral Tissue and Whole-Body Amino Acid Metabolism during Intravenous Feeding in Normal Man

1989 ◽  
Vol 77 (1) ◽  
pp. 113-120 ◽  
Author(s):  
James D. Albert ◽  
Dwight E. Matthews ◽  
Adrian Legaspi ◽  
Kevin J. Tracey ◽  
Malayappa Jeevanandam ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Submaximal Exercise ◽  
Peripheral Tissue ◽  
Whole Body ◽  
Total Amino Acid ◽  
Body Protein ◽  
Daily Exercise ◽  
Amino Acid Flux

1. The effect of a daily submaximal exercise regimen on whole-body and peripheral tissue amino acid metabolism during weight-stable intravenous feeding (IVF) was evaluated in 11 normal volunteers. Five of the subjects performed 1 h of daily bicycle exercise at 75 W during IVF, while the remaining six subjects received IVF without daily exercise. Body nitrogen balance, leg and forearm plasma amino acid flux and whole-body kinetics were measured before and on day 10 of IVF using a [1-13C]leucine and [15N]glycine tracer. 2. At the end of the IVF period, exercised subjects demonstrated leg uptake of total amino acids (237 ± 103 nmol min−1 100 ml−1 of tissue, mean ± sem) which was significantly (P < 0.05) different than in non-exercised subjects (− 1101 ± 253 nmol min−1 100 ml−1 of tissue). 3. In the non-exercised forearm, a significant (P < 0.05) decrease in total amino acid flux was observed in exercised subjects (− 162 ± 88 nmol min−1 100 ml−1 of tissue) compared with non-exercised subjects (−460 ± 105 nmol min−1 100 ml−1 of tissue) on day 10 of IVF. 4. Efflux of 3-methylhistidine significantly (P < 0.05) decreased from the leg in those subjects who performed daily exercise (−0.29 ± 0.12 nmol min−1 100 ml−1 of tissue) compared with those subjects receiving IVF without daily exercise (− 1.46 ± 0.35 nmol min−1 100 ml−1 of tissue). 5. Although IVF increased whole-body leucine turnover in both exercised and non-exercised subjects, only exercised subjects demonstrated a significant (P < 0.05) increase in leucine oxidation which was proportionate to an increased muscle uptake of leucine. Whole-body protein breakdown, as assessed by [15N]glycine, was significantly (P < 0.05) decreased in exercised subjects compared with non-exercised subjects during IVF. 6. These data demonstrate that daily submaximal exercise produced a systemic as well as limb-specific enhancement of amino acid balance in muscle, providing an anti-catabolic response under conditions of partial immobility induced by hospitalization.

scholarly journals Metabolomic Analysis of Biochemical Changes in the Plasma of High-Fat Diet and Streptozotocin-Induced Diabetic Rats after Treatment with Isoflavones Extract of Radix Puerariae

2016 ◽  
Vol 2016 ◽  
pp. 1-12 ◽  
Author(s):  
Yan Zhang ◽  
Ping Wang ◽  
Youdong Xu ◽  
Xianli Meng ◽  
Yi Zhang
Keyword(s):  
Liquid Chromatography ◽  
Amino Acid ◽  
Discriminant Analysis ◽  
Least Squares ◽  
High Fat Diet ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Diabetic Rats ◽  
High Fat ◽  
Radix Puerariae

The main purpose of this study was to investigate the protective effects of total isoflavones from Radix Puerariae (PTIF) in diabetic rats. Diabetes was induced by a high-fat diet and intraperitoneal injection of low-dose streptozotocin (STZ; 40 mg/kg). At 26 weeks onwards, PTIF 421 mg/kg was administrated to the rats once daily consecutively for 10 weeks. Metabolic profiling changes were analyzed by Ultraperformance Liquid Chromatography-Quadrupole-Exactive Orbitrap-Mass Spectrometry (UPLC-Q-Exactive Orbitrap-MS). The principal component discriminant analysis (PCA-DA), partial least-squares discriminant analysis (PLS-DA), and orthogonal partial least-squares discriminant analysis (OPLS-DA) were used for multivariate analysis. Moreover, free amino acids in serum were determined by high-performance liquid chromatography with fluorescence detector (HPLC-FLD). Additionally, oxidative stress and inflammatory cytokines were evaluated. Eleven potential metabolite biomarkers, which are mainly related to the coagulation, lipid metabolism, and amino acid metabolism, have been identified. PCA-DA scores plots indicated that biochemical changes in diabetic rats were gradually restored to normal after administration of PTIF. Furthermore, the levels of BCAAs, glutamate, arginine, and tyrosine were significantly increased in diabetic rats. Treatment with PTIF could regulate the disturbed amino acid metabolism. Consequently, PTIF has great therapeutic potential in the treatment of DM by improving metabolism disorders and inhibiting oxidative damage.

Amino acid metabolism after intense exercise

1990 ◽  
Vol 258 (2) ◽  
pp. E249-E255 ◽  
Author(s):  
J. T. Devlin ◽  
I. Brodsky ◽  
A. Scrimgeour ◽  
S. Fuller ◽  
D. M. Bier
Keyword(s):  
Protein Synthesis ◽  
Amino Acid ◽  
Protein Degradation ◽  
Amino Acid Metabolism ◽  
Acid Metabolism ◽  
Recovery Period ◽  
Whole Body ◽  
Protein Breakdown ◽  
Body Protein ◽  
Leucine Oxidation

We studied postexercise amino acid metabolism, in the whole body and across the forearm. Seven volunteers were infused with L-[alpha-15N]lysine and L-[1-13C]-leucine twice [one time during 3 h after cycle exercise (75% VO2max), and one time in the resting state]. Whole body protein breakdown was estimated from dilution of L-[alpha-15N]lysine and L-[1-13C]ketoisocaproic acid (KIC) enrichments in plasma. Leucine oxidation was calculated from 13CO2 enrichments in expired air. Whole body protein breakdown was not increased above resting levels during the recovery period. Leucine oxidation was decreased after exercise (postexercise 13 +/- 2.3 vs. resting 19 +/- 3.2 mumol.kg-1.h-1; P less than 0.02), while nonoxidative leucine disposal was increased (115 +/- 6.1 vs. 103 +/- 5.6 micrograms.kg-1.min-1; P less than 0.02). After exercise, forearm net lysine balance was unchanged (87 +/- 25 vs. 93 +/- 28 nmol.100 ml-1.min-1), but there were decreases in forearm muscle protein degradation (219 +/- 51 vs. 356 +/- 85 nmol.100 ml-1.min-1; P less than 0.05) and synthesis (132 +/- 41 vs. 255 +/- 69 nmol.100 ml-1.min-1; P less than 0.01). In conclusion, after exercise 1) whole body protein degradation is not increased, 2) leucine disposal is directed away from oxidative and toward nonoxidative pathways, 3) forearm protein synthesis is decreased. Postexercise increases in whole body protein synthesis occur in tissues other than nonexercised muscle.

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