Branched Chain Amino Acid Uptake and Muscle Free Amino Acid Concentrations Predict Postoperative Muscle Nitrogen Balance

Johnson, Daniel J.; Jiang, Zhu-Ming; Colpoys, Michael F.; Kapadia, Cyrus R.; Smith, Robert J.; Wilmore, Douglas W.

doi:10.1097/00000658-198611000-00002

Cited by 37 publications

(9 citation statements)

References 11 publications

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“…Arginine has immunomodulatory effects, promotes wound healing and protein synthesis, and is a precursor for nitric oxide 12 . BCAA promote protein transcription and translation and inhibit protein degradation 13–15 . Altered circulating or tissue concentrations of these specific amino acids have been found in various disease states 3,14,16,17 .…”

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confidence: 99%

“…BCAA promote protein transcription and translation and inhibit protein degradation 13–15 . Altered circulating or tissue concentrations of these specific amino acids have been found in various disease states 3,14,16,17 . Alterations in BCAA often have been assessed by comparing the ratio of BCAA to aromatic amino acids (AAA) (ie, phenylalanine and tyrosine) or by the Fischer ratio, which is the molar ratio of BCAA : AAA 18,19 …”

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confidence: 99%

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Relationship among Plasma Amino Acids, C‐Reactive Protein, Illness Severity, and Outcome in Critically Ill Dogs

Chan

Rozanski

Freeman

2009

Veterinary Internal Medicne

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Background: Alterations in circulating amino acids have been documented in animal models and in critically ill people but have not been evaluated in dogs with spontaneously occurring disease.Hypothesis/Objectives: To compare amino acid concentrations in critically ill dogs and healthy controls and to investigate potential relationships among amino acids, markers of inflammation, illness severity, and clinical outcome.Animals: Forty-eight critically ill dogs and 24 healthy control dogs. Methods: Plasma was analyzed for amino acids and C-reactive protein (CRP) was measured in serum. The Fischer ratio (the molar ratio of branched chain amino acids [BCAA] to aromatic amino acids [AAA]) and survival prediction index (SPI2) were calculated.Results: Median CRP concentrations were significantly higher in the critically ill dogs compared with controls (P o .001). Critically ill dogs had significantly lower concentrations of alanine (P 5 .001), arginine (P o .001), citrulline (P o .001), glycine (P o .001), methionine (P o .001), proline (P o .001), and serine (P 5 .001) but significantly higher concentrations of lysine (P 5 .02) and phenylalanine (P o .001; Table 1). This pattern resulted in a significantly lower Fischer ratio (P 5 .001) in the critically ill group. Median SPI2 score was significantly higher in dogs that survived (P 5 .03). Concentrations of arginine (P 5 .02), isoleucine (P 5 .01), leucine (P 5 .04), serine (P 5 .04), valine (P 5 .04), total BCAA (P 5 .03), and the Fischer ratio (P 5 .03) were significantly higher in survivors compared with nonsurvivors.Conclusions and Clinical Importance: Critically ill dogs have altered amino acid profiles and additional research to investigate potential benefits of amino acid supplementation is warranted.

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confidence: 99%

Relationship among Plasma Amino Acids, C‐Reactive Protein, Illness Severity, and Outcome in Critically Ill Dogs

Chan

Rozanski

Freeman

2009

Veterinary Internal Medicne

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“…Results from our laboratory (34,35) and from other investigators (23,29) have shown that hemodialysis (HD) induces muscle protein catabolism. BCAA and glutamine have been shown to have a regulatory effect on protein turnover (25,32). Despite their qualitative and quantitative importance, the kinetics of alanine and glutamine in ESRD are largely unknown.…”

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Glutamine kinetics and protein turnover in end-stage renal disease

Raj¹,

Welbourne²,

Dominic³

et al. 2005

American Journal of Physiology-Endocrinology and Metabolism

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-Alanine and glutamine constitute the two most important nitrogen carriers released from the muscle. We studied the intracellular amino acid transport kinetics and protein turnover in nine end-stage renal disease (ESRD) patients and eight controls by use of stable isotopes of phenylalanine, alanine, and glutamine. The amino acid transport kinetics and protein turnover were calculated with a three-pool model from the amino acid concentrations and enrichment in the artery, vein, and muscle compartments. Muscle protein breakdown was more than synthesis (nmol⅐min Ϫ1 ⅐100 ml leg Ϫ1 ) during hemodialysis (HD) (169.8 Ϯ 20.0 vs. 125.9 Ϯ 21.8, P Ͻ 0.05) and in controls (126.9 Ϯ 6.9 vs. 98.4 Ϯ 7.5, P Ͻ 0.05), but synthesis and catabolism were comparable pre-HD (100.7 Ϯ 15.7 vs. 103.4 Ϯ 14.8). Whole body protein catabolism decreased by 15% during HD. The intracellular appearance of alanine (399.0 Ϯ 47.1 vs. 243.0 Ϯ 34.689) and glutamine (369.7 Ϯ 40.6 vs. 235.6 Ϯ 27.5) from muscle protein breakdown increased during dialysis (nmol ⅐ min Ϫ1 ⅐ 100 ml leg Ϫ1 , P Ͻ 0.01). However, the de novo synthesis of alanine (3,468.9 Ϯ 572.2 vs. 3,140.5 Ϯ 467.7) and glutamine (1,751.4 Ϯ 82.6 vs. 1,782.2 Ϯ 86.4) did not change significantly intradialysis (nmol ⅐ min Ϫ1 ⅐ 100 ml leg Ϫ1 ). Branched-chain amino acid catabolism (191.8 Ϯ 63.4 vs. Ϫ59.1 Ϯ 42.9) and nonprotein glutamate disposal (347.0 Ϯ 46.3 vs. 222.3 Ϯ 43.6) increased intradialysis compared with pre-HD (nmol ⅐ min Ϫ1 ⅐ 100 ml leg Ϫ1 , P Ͻ 0.01). The mRNA levels of glutamine synthase (1.45 Ϯ 0.14 vs. 0.33 Ϯ 0.08, P Ͻ 0.001) and branched-chain keto acid dehydrogenase-E2 (3.86 Ϯ 0.48 vs. 2.14 Ϯ 0.27, P Ͻ 0.05) in the muscle increased during HD. Thus intracellular concentrations of alanine and glutamine are maintained during HD by augmented release of the amino acids from muscle protein catabolism. Although muscle protein breakdown increased intradialysis, the whole body protein catabolism decreased, suggesting central utilization of amino acids released from skeletal muscle. amino acids; protein catabolism; nitrogen carriers; hemodialysis ALANINE AND GLUTAMINE play a central role in substrate recycling and interorgan nitrogen metabolism. Together, they comprise Ͻ15% of amino acid content of protein, yet they account for ϳ60% of the amino nitrogen leaving the muscle (10). In disease states, glutamine consumption exceeds the release from the muscle (19). Branched-chain amino acids (BCAA) include valine, leucine, and isoleucine. Metabolism of BCAA, alanine, glutamine, and glutamate are interrelated (Fig. 1). Ferrando et al. (16) demonstrated an inverse relationship between alanine and glutamine production in the muscle in patients with burn. The precursors for glutamine synthesis include glutamate, ␣-ketoglutarate, free ammonia, and amino nitrogen derived from catabolism of BCAA. On the other hand, pyruvate is transaminated with glutamate to generate alanine and ␣-ketoglutarate. In catabolic states, net synthesis of glutamine is decreased, but de novo alanine synthesis is increased....

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“…In both stressed and normal animal and human models, the infusion of BCAA has been found to increase the release of glutamine from skeletal muscle and to elevate the plasma glutamine concentration. 5,7,25–27 Johnson et al 28 studied the effect of infusing BCAA‐enriched parenteral nutrition (i.e. 45% of amino acids compared with the 6–18% found in conventional parenteral nutrition) on protein and glutamine kinetics in dogs after laparotomy.…”

Section: Metabolismmentioning

confidence: 99%

Branched‐chain amino acids

Platell

Kong

Mccauley³

et al. 2000

J of Gastro and Hepatol

123

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The branched‐chain amino acids (BCAA), isoleucine, leucine and valine, are unique in that they are principally metabolized extrahepatically in the skeletal muscle. This observation led to the investigation of these nutrients in a number of clinical scenarios. By far the most intensively studied applications for BCAA have been in patients with liver failure and/or patients in catabolic disease states. However, the resulting studies have not demonstrated a clear clinical benefit for BCAA nutritional supplements. In patients with liver failure, the BCAA did improve nitrogen retention and protein synthesis, but their effect on patient outcome was less clear. Similarly, in critically ill septic patients, BCAA did not improve either survival or morbidity. The BCAA are important nutrients, and it seems that any specific benefits associated with their use will be based upon a greater understanding of the underlying cellular biology. Potential areas of further research may include the combination of BCAA supplements with other anabolic factors (e.g. growth hormone) in managing patients with catabolic disease states.

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Branched Chain Amino Acid Uptake and Muscle Free Amino Acid Concentrations Predict Postoperative Muscle Nitrogen Balance

Cited by 37 publications

References 11 publications

Relationship among Plasma Amino Acids, C‐Reactive Protein, Illness Severity, and Outcome in Critically Ill Dogs

Relationship among Plasma Amino Acids, C‐Reactive Protein, Illness Severity, and Outcome in Critically Ill Dogs

Glutamine kinetics and protein turnover in end-stage renal disease

Branched‐chain amino acids

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