scholarly journals Low Serum Branched-chain Amino Acid and Insulin-Like Growth Factor-1 Levels Are Associated with Sarcopenia and Slow Gait Speed in Patients with Liver Cirrhosis

2020 ◽  
Vol 9 (10) ◽  
pp. 3239
Author(s):  
Chisato Saeki ◽  
Tomoya Kanai ◽  
Masanori Nakano ◽  
Tsunekazu Oikawa ◽  
Yuichi Torisu ◽  
...  
Keyword(s):  
Liver Cirrhosis ◽  
Amino Acid ◽  
Growth Factor ◽  
Gait Speed ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Insulin Like Growth Factor ◽  
Branched Chain Amino Acid ◽  
Branched Chain ◽  
Low Serum

Branched-chain amino acid (BCAA) and insulin-like growth factor 1 (IGF-1) are essential for muscle protein synthesis. We investigated the association of serum BCAA and IGF-1 levels with sarcopenia and gait speed in 192 patients with liver cirrhosis (LC). Sarcopenia was diagnosed according to the Japan Society of Hepatology criteria. Slow gait speed was defined as <1.0 m/s. Subjects were divided into three groups based on baseline BCAA or IGF-1 levels: low (L), intermediate (I), and high (H) groups. The L-BCAA group had the highest prevalence of sarcopenia (60.4%, p < 0.001) and slow gait speed (56.3%, p = 0.008), whereas the H-BCAA group had the lowest prevalence of sarcopenia (8.5%, p < 0.001). The L-IGF-1 group showed the highest prevalence of sarcopenia (46.9%, p < 0.001), whereas the H-IGF-1 group had the lowest prevalence of sarcopenia (10.0%, p < 0.001) and slow gait speed (18.0%, p = 0.003). Using the optimal BCAA and IGF-1 cutoff values for predicting sarcopenia (372 μmol/L and 48.5 ng/mL, respectively), the sensitivity and specificity were 0.709 and 0.759 for BCAA and 0.636 and 0.715 for IGF-1, respectively. Low serum BCAA and IGF-1 levels were associated with sarcopenia and slow gait speed in patients with LC.

Effect of Infused Branched-Chain Amino Acids on Muscle and Whole-Body Amino Acid Metabolism in Man

1990 ◽  
Vol 79 (5) ◽  
pp. 457-466 ◽  
Author(s):  
Rita J. Louard ◽  
Eugene J. Barrett ◽  
Robert A. Gelfand
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Branched Chain Amino Acids ◽  
Whole Body ◽  
Acid Infusion ◽  
Amino Acid Infusion ◽  
Branched Chain Amino Acid ◽  
Branched Chain

1. Using the forearm balance method, together with systemic infusions of l-[ring-2,6-3H]phenylalanine and l-[1-14C]leucine, we examined the effects of infused branched-chain amino acids on whole-body and skeletal muscle amino acid kinetics in 10 postabsorptive normal subjects; 10 control subjects received only saline. 2. Infusion of branched-chain amino acids caused a four-fold rise in arterial branched-chain amino acid levels and a two-fold rise in branched-chain keto acids; significant declines were observed in circulating levels of most other amino acids, including phenylalanine, which fell by 34%. Plasma insulin levels were unchanged from basal levels (8 ± 1 μ-units/ml). 3. Whole-body phenylalanine flux, an index of proteolysis, was significantly suppressed by branched-chain amino acid infusion (P < 0.002), and forearm phenylalanine production was also inhibited (P < 0.03). With branched-chain amino acid infusion total leucine flux rose, with marked increments in both oxidative and non-oxidative leucine disposal (P < 0.001). Proteolysis, as measured by endogenous leucine production, showed a modest 12% decrease, although this was not significant when compared with saline controls. The net forearm balance of leucine and other branched-chain amino acids changed from a basal net output to a marked net uptake (P < 0.001) during branched-chain amino acid infusion, with significant stimulation of local leucine disposal. Despite the rise in whole-body non-oxidative leucine disposal, and in forearm leucine uptake and disposal, forearm phenylalanine disposal, an index of muscle protein synthesis, was not stimulated by infusion of branched-chain amino acids. 4. The results suggest that in normal man branched-chain amino acid infusion suppresses skeletal muscle proteolysis independently of any rise of plasma insulin. Muscle branched-chain amino acid uptake rose dramatically in the absence of any apparent increase in muscle protein synthesis, as measured by phenylalanine disposal, or in branched-chain keto acid release. Thus, an increase in muscle branched-chain amino acid concentrations and/ or local branched-chain amino acid oxidation must account for the increased disposal of branched-chain amino acids.

Isoleucine increases muscle mass through promoting myogenesis and intramyocellular fat deposition

2021 ◽  
Author(s):  
Shuge Liu ◽  
Yunmei Sun ◽  
Rui Zhao ◽  
Yingqian Wang ◽  
Wanrong Zhang ◽  
...  
Keyword(s):  
Body Weight ◽  
Protein Synthesis ◽  
Amino Acid ◽  
Muscle Mass ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Vital Role ◽  
Fat Deposition ◽  
Branched Chain Amino Acid ◽  
Branched Chain

Isoleucine (Ile), as a branched-chain amino acid (BCAA), has a vital role in regulating body weight and muscle protein synthesis.

scholarly journals The effects of branched-chain amino acid interactions on growth performance, blood metabolites, enzyme kinetics and transcriptomics in weaned pigs

2010 ◽  
Vol 103 (7) ◽  
pp. 964-976 ◽  
Author(s):  
Markus Karl Wiltafsky ◽  
Michael Walter Pfaffl ◽  
Franz Xaver Roth
Keyword(s):  
Growth Hormone ◽  
Amino Acid ◽  
Growth Factor ◽  
Growth Performance ◽  
Mrna Levels ◽  
Dependent Manner ◽  
Insulin Like Growth Factor ◽  
Branched Chain Amino Acid ◽  
Branched Chain ◽  
The Impact

The impact of excess dietary leucine (Leu) was studied in two growth assays with pigs (8–25 kg). In each trial, forty-eight pigs were allotted to one of six dietary groups. The dietary Leu supply increased from treatment L100 to L200 (three increments). To guarantee that interactions between the branched-chain amino acids (BCAA) were not cushioned either surpluses of isoleucine (Ile, expt 1) or valine (Val; expt 2) were avoided. In the fifth treatment, the effects of a simultaneous excess of Leu and Val (expt 1), or of Leu and Ile (expt 2) were investigated. The sixth treatment was a positive control. An increase in dietary Leu decreased growth performance, and increased plasma Leu and serum α-keto-isocaproate levels in a linear, dose-dependent manner. Levels of plasma Ile and Val, and of serum α-keto-β-methylvalerate and α-keto-isovalerate, indicated increased catabolism. Linear increases in the activity of basal branched-chain α-keto acid dehydrogenase in the liver confirmed these findings. No major alterations occurred in the mRNA of branched-chain amino acid catabolism genes. In liver tissue from expt 2, however, the mRNA levels of growth hormone receptor, insulin-like growth factor acid labile subunit and insulin-like growth factor 1 decreased significantly with increasing dietary Leu. In conclusion, excess dietary Leu increased the catabolism of BCAA mainly through posttranscriptional mechanisms. The impact of excess Leu on the growth hormone–insulin-like growth factor-1 axis requires further investigation.

Oral Branched-Chain Amino Acid Granules Reduce the Incidence of Hepatocellular Carcinoma and Improve Event-Free Survival in Patients with Liver Cirrhosis

2011 ◽  
Vol 29 (3) ◽  
pp. 326-332 ◽  
Author(s):  
Sosuke Hayaishi ◽  
Hobyung Chung ◽  
Masatoshi Kudo ◽  
Emi Ishikawa ◽  
Masahiro Takita ◽  
...  
Keyword(s):  
Hepatocellular Carcinoma ◽  
Liver Cirrhosis ◽  
Amino Acid ◽  
Event Free Survival ◽  
Free Survival ◽  
Branched Chain Amino Acid ◽  
Branched Chain

Anti-hypoalbuminemic effect of branched-chain amino acid granules in patients with liver cirrhosis is independent of dietary energy and protein intake

2011 ◽  
Vol 41 (11) ◽  
pp. 1027-1035 ◽  
Author(s):  
Hiroshi Yatsuhashi ◽  
Yoshifumi Ohnishi ◽  
Seiichi Nakayama ◽  
Hiroaki Iwase ◽  
Teiji Nakamura ◽  
...  
Keyword(s):  
Liver Cirrhosis ◽  
Amino Acid ◽  
Protein Intake ◽  
Dietary Energy ◽  
Branched Chain Amino Acid ◽  
Branched Chain

Treatment of liver cirrhosis with branched chain amino acid-supplemented diet

1981 ◽  
Vol 16 (4) ◽  
pp. 389-392 ◽  
Author(s):  
Misako Okita ◽  
Akiharu Watanabe ◽  
Hideo Nagashima
Keyword(s):  
Liver Cirrhosis ◽  
Amino Acid ◽  
Branched Chain Amino Acid ◽  
Branched Chain

scholarly journals Severe diabetes prohibits elevations in muscle protein synthesis after acute resistance exercise in rats

2000 ◽  
Vol 88 (1) ◽  
pp. 102-108 ◽  
Author(s):  
Mark J. Fedele ◽  
Jazmir M. Hernandez ◽  
Charles H. Lang ◽  
Thomas C. Vary ◽  
Scot R. Kimball ◽  
...  
Keyword(s):  
Protein Synthesis ◽  
Growth Factor ◽  
Resistance Exercise ◽  
Muscle Protein ◽  
Muscle Protein Synthesis ◽  
Critical Concentration ◽  
Diabetic Rats ◽  
Insulin Like Growth Factor ◽  
Factor I ◽  
Growth Factor I

This study determined whether rates of protein synthesis increase after acute resistance exercise in skeletal muscle from severely diabetic rats. Previous studies consistently show that postexercise rates of protein synthesis are elevated in nondiabetic and moderately diabetic rats. Severely diabetic rats performed acute resistance exercise ( n= 8) or remained sedentary ( n = 8). A group of nondiabetic age-matched rats served as controls ( n = 9). Rates of protein synthesis were measured 16 h after exercise. Plasma glucose concentrations were >500 mg/dl in the diabetic rats. Rates of protein synthesis (nmol phenylalanine incorporated ⋅ g muscle−1 ⋅ h−1, means ± SE) were not different between exercised (117 ± 7) and sedentary (106 ± 9) diabetic rats but were significantly ( P < 0.05) lower than in sedentary nondiabetic rats (162 ± 9) and in exercised nondiabetic rats (197 ± 7). Circulating insulin concentrations were 442 ± 65 pM in nondiabetic rats and 53 ± 11 and 72 ± 19 pM in sedentary and exercised diabetic rats, respectively. Plasma insulin-like growth factor I concentrations were reduced by 33% in diabetic rats compared with nondiabetic rats, and there was no difference between exercised and sedentary diabetic rats. Muscle insulin-like growth factor I was not affected by resistance exercise in diabetic rats. The results show that there is a critical concentration of insulin below which rates of protein synthesis begin to decline in vivo. In contrast to previous studies using less diabetic rats, severely diabetic rats cannot increase rates of protein synthesis after acute resistance exercise.

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