Modulation of rat skeletal muscle branched-chain alpha-keto acid dehydrogenase in vivo. Effects of dietary protein and meal consumption.

Block, Kevin P.; Aftring, R. Paul; Mehard, William B.; Buse, Maria G.

doi:10.1172/jci112961

Cited by 44 publications

(11 citation statements)

References 51 publications

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“…In contrast, the SC of isoleucine and valine in pigs fed the 120 and 160% Leu:Lys ratios decreased to less than 50% of that in pigs fed the diet with the 88% ratio. These results are also consistent with previous reports (Edmonds and Baker, 1987;Wiltafsky et al, 2010), resulting from increased activity of the enzyme complex that catabolizes all 3 branched chain amino acids in pigs fed diets with excess Leu (Block et al, 1987;Wiltafsky et al, 2010). Furthermore, competitive inhibition for absorption among branched chain amino acids has been documented (Hagihira et al, 1961).…”

Section: Discussionsupporting

confidence: 93%

Gene expression, serum amino acid levels, and growth performance of pigs fed dietary leucine and lysine at different ratios

García¹,

Morales²,

Araiza³

et al. 2015

Genet. Mol. Res.

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ABSTRACT. We examined 96 pigs (28.1 ± 0.83 kg) to analyze the effect of Leu:Lys ratios on expression of the cationic amino acid transporters b 0,+ and CAT-1 in the jejunum and liver as well as myosin expression in 2 muscles to estimate the optimum standardized ileal digestible (SID) Leu:Lys ratio for growth rate and efficiency. A wheatand wheat bran-based diets were formulated to meet the requirements of SID amino acids other than Leu (0.70%) and Lys (0.80%). L-Leu was added to the basal diet in 5 SID Leu:Lys ratios (88, 100, 120, 140, and 160% in diets 1-5). Tissue samples were collected from 8 pigs with ratios of 88, 120, and 160%. Relative expression of b 0,+ , CAT-1, and myosin was analyzed. b 0,+ expression in the jejunum was higher but lower in the liver of pigs with the 120% ratio compared to those with the 88 or 160% ratio; myosin expression in longissimus dorsi was also higher in pigs with the 120% ratio (P < 0.05). CAT-1 was lower in the jejunum and longissimus dorsi of pigs with 120 or 160% ratios than in pigs with 88%. Serum concentration of nearly all amino acids decreased with excess dietary Leu (P < 0.05). The SID Leu:Lys of 104 and 109% 1590 H. García et al. ©FUNPEC-RP www.funpecrp.com.br Genetics and Molecular Research 14 (1): 1589-1601 (2015 optimized average daily gain and feed conversion ratio, respectively. Thus, the dietary Leu:Lys ratio affects the expression of genes coding for amino acid transporters and myosin, the availability of Lys, and the growth rate and efficiency in pigs.

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Section: Discussionsupporting

confidence: 93%

Gene expression, serum amino acid levels, and growth performance of pigs fed dietary leucine and lysine at different ratios

García¹,

Morales²,

Araiza³

et al. 2015

Genet. Mol. Res.

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“…While control rats habitually consumed all their food in less than 23h and may have experienced a food-deprivation period on a daily basis, the rats fed the -Arg/+Ala diet, in contrast, always had food available. The rate-limiting enzyme for BCAA catabolism, branched-chain ketoacid dehydrogenase (BCKADH), has been shown to be more active in meal-fed rats than in rats allowed ad libitum consumption of diet (Block et al, 1987). Therefore, greater activity of BCKADH may have catabolized more BCAA in muscles of rats fed +Arg or -Arg/+Cit diet.…”

Section: Effects' Of Diet On Muscle Free Amino Acid Concentrationsmentioning

confidence: 99%

Feeding and arginine deficient diets differentially alter free amino acid concentrations of hindlimb muscle in young rats

Hartman

Prior

1997

Amino Acids

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Summary. The objective of these experiments was to examine short-and long-term (7 d) effects of arginine-deficient diets on free amino acid concentrations in hindlimb muscle of rats. In rats fed the control diet containing arginine (+Arg), muscle alanine and methionine concentrations were higher 1 and 2h after feeding compared to food-deprived rats, whereas branchedchain amino acids, arginine and asparagine concentrations were lower postprandially. In Experiment 1, rats were fed an arginine-deficient (-Arg) diet with glutamate (+Glu) substituted for arginine; alanine (+Ala), ornithine (+ Orn) or citrulline (+ Cit) were substituted for arginine in Experiment 2. In Experiment 1, arginine concentrations decreased in blood but not in muscle. This contrasts with rats fed -Arg/+ Ala or -Arg/+ Orn diets which had muscle arginine concentrations less than half the concentrations in controls or in rats fed the -Arg/+Cit diet. Muscle essential amino acids in Experiment 2 did not differ by diet, but muscle branched-chain amino acids were elevated relative to controls in the rats fed -Arg/+Ala or -Arg/+Orn diets; however, rats fed the -Arg/+ Cit diet had levels similar to the controls. Also, muscle branched-chain amino acids were correlated with glutamine concentrations in both blood and muscle. The measurements in the post-meal period suggest that muscle amino acid concentrations may more closely reflect dietary amino acid patterns than do blood amino concentrations.

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“…To determine the maximal activity of BCKA dehydrogenase, the enzyme was fully activated by incubating tissue homogenates with 5 mM Mg2e for 15 min at 37°C before measurement of activity. We and others (10,24,25) have previously shown that this method of activating the enzyme is effective.…”

Section: Methodsmentioning

confidence: 87%

“…Abbreviations used in this paper: BCAA, branched chain amino acids; BCKA, branched chain keto acids. protein content has a profound effect on BCAA catabolism (7)(8)(9)(10)(11). In contrast, the effect of dietary carbohydrate and fat on BCAA metabolism has not been adequately investigated.…”

Section: Introductionmentioning

confidence: 99%

Regulation of leucine catabolism by caloric sources. Role of glucose and lipid in nitrogen sparing during nitrogen deprivation.

Vazquez¹,

Paul²,

Adibi³

1988

J. Clin. Invest.

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Previously we showed that hypocaloric amounts of glucose reduce leucine catabolism while an isocaloric amount of fat does not (1985. J. Clin. Invest. 76:737.) Mmol/100 g per h, P < 0.05). However, all these parameters were significantly lower in lipid-infused than starved rats. There was no significant difference between leucine incorporation into liver and muscle proteins of lipid and glucose-infused rats. On the other hand, starved rats showed a lower leucine incorporation into liver proteins. The data show that under conditions of adequate caloric intake lipid has an inhibitory effect on leucine catabolism but not as great as that of glucose. The mechanism of this difference may be related to a lesser inhibition of muscle protein degradation by lipid than glucose, thereby increasing the leucine pool, which in turn stimulates leucine oxidation.

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Modulation of rat skeletal muscle branched-chain alpha-keto acid dehydrogenase in vivo. Effects of dietary protein and meal consumption.

Cited by 44 publications

References 51 publications

Gene expression, serum amino acid levels, and growth performance of pigs fed dietary leucine and lysine at different ratios

Gene expression, serum amino acid levels, and growth performance of pigs fed dietary leucine and lysine at different ratios

Feeding and arginine deficient diets differentially alter free amino acid concentrations of hindlimb muscle in young rats

Regulation of leucine catabolism by caloric sources. Role of glucose and lipid in nitrogen sparing during nitrogen deprivation.

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