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Interactions among the branched-chain amino acids and their effects on methionine utilization in growing pigs: effects on plasma amino– and keto–acid concentrations and branched-chain keto-acid dehydrogenase activity

Published online by Cambridge University Press:  09 March 2007

Stefan Langer ,
Peter W. D. Scislowski ,
David S. Brown ,
Peter Dewey  and
Malcolm F. Fuller
Stefan Langer
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB21 9SB, UK
Peter W. D. Scislowski
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB21 9SB, UK
David S. Brown
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB21 9SB, UK
Peter Dewey
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB21 9SB, UK
Malcolm F. Fuller*
Affiliation:
Rowett Research Institute, Greenburn Road, Bucksburn, Aberdeen AB21 9SB, UK
*
*Corresponding author: Dr Malcolm Fuller, fax +44 (0)1224 716687, email aw@rri.sari.ac.uk
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Abstract

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The present experiment was designed to elucidate the mechanism of the methionine-sparing effect of excess branched-chain amino acids (BCAA) reported in the previous paper (Langer & Fuller, 2000). Twelve growing gilts (30–35 kg) were prepared with arterial catheters. After recovery, they received for 7 d a semipurified diet with a balanced amino acid pattern. On the 7th day blood samples were taken before (16 h postabsorptive) and after the morning meal (4 h postprandial). The animals were then divided into three groups and received for a further 7 d a methionine-limiting diet (80 % of requirement) (1) without any amino acid excess; (2) with excess leucine (50 % over requirement); or (3) with excesses of all three BCAA (leucine, isoleucine, valine, each 50 % over the requirement). On the 7th day blood samples were taken as in the first period, after which the animals were killed and liver and muscle samples taken. Plasma amino acid and branched-chain keto acid (BCKA) concentrations in the blood and branched-chain keto-acid dehydrogenase (BCKDH; EC 1.2.4.4) activity in liver and muscle homogenates were determined. Compared with those on the balanced diet, pigs fed on methionine-limiting diets had significantly lower (P < 0·05) plasma methionine concentrations in the postprandial but not in the postabsorptive state. There was no effect of either leucine or a mixture of all three BCAA fed in excess on plasma methionine concentrations. Excess dietary leucine reduced (P < 0·05) the plasma concentrations of isoleucine and valine in both the postprandial and postabsorptive states. Plasma concentrations of the BCKA reflected the changes in the corresponding amino acids. Basal BCKDH activity in the liver and total BCKDH activity in the biceps femoris muscle were significantly (P < 0·05) increased by excesses of leucine or all BCAA.

Keywords

Branched-chain amino acidsMethionineAmino acid utilization
Type
Research Article
Information
British Journal of Nutrition , Volume 83 , Issue 1 , January 2000 , pp. 49 - 58
Copyright
Copyright © The Nutrition Society 2000

References

Abumrad, NN, Abumrad, NA, Sandler, MP & Lacy, WW (1984) The metabolic effects and fate of branched-chain amino and keto acids across human skeletal muscle. In Advances in Hepatic Encephalopathy and Urea Cycle Diseases, pp. 505–518 [Kleinberger,, G, Ferenci, P, Riederer, P and Thaler, H, editors]. Basel: Karger.Google Scholar
Baumrucker, CR (1985) Amino acid transport systems in bovine mammary tissue. Journal of Dairy Science 68, 2436–2451.CrossRefGoogle ScholarPubMed
Bech-Andersen, S, Mason, VC & Dhanoa, MS (1990) Hydrolysate preparation for amino acid determinations in feed constituents. 9. Modifications to oxidation and hydrolysis conditions for streamlined procedures. Journal of Animal Physiology and Animal Nutrition 63, 188–197.CrossRefGoogle Scholar
Benevenga, NJ (1984) Evidence for alternative pathways of methionine catabolism. In Advances in Nutritional Research, vol. 6, pp. 1–18 [Draper, HH, editor]. New York, NY: Plenum Press.Google Scholar
Block, KP (1989) Interactions among leucine, isoleucine, and valine with special to the branched-chain amino acid antagonism. In Absorption and Utilization of Amino Acids, vol. 1, pp. 229–244 [Friedman, M, editor]. Boca Raton, FL: CRC Press.Google Scholar
Block, KP & Harper, AE (1984) Valine metabolism in vitro: effects of high dietary levels of leucine and isoleucine. Metabolism 33, 559–566.CrossRefGoogle Scholar
Block, KP & Harper, AE (1991) High levels of dietary amino and branched-chain α-keto acids alter plasma and brain amino acid concentrations in rats. Journal of Nutrition 121, 663–671.CrossRefGoogle ScholarPubMed
Buse, MG & Reid, SS (1975) Leucine. A possible regulator of protein turnover in muscle Journal of Clinical Investigation 56, 1250–1261.CrossRefGoogle ScholarPubMed
Calvert, CC, Klasing, KC & Austic, RE (1982) Involvement of food intake and amino acid catabolism in the branched-chain amino acids antagonism in chicks Journal of Nutrition 112, 627–635.CrossRefGoogle ScholarPubMed
Case, GL & Benevenga, NJ (1976) Evidence for S-adenosylmethionine independent catabolism of methionine in the rat. Journal of Nutrition 106, 1721–1736.CrossRefGoogle ScholarPubMed
Crowell, PL, Block, KP, Repa, JJ, Torres, N, Nawabi, MD, Buse, MG & Harper, AE (1990) High branched-chain α-keto acid intake, branched-chain α-keto acid dehydrogenase activity, and plasma and brain amino acid and plasma keto acid concentrations in rats. American Journal of Clinical Nutrition 52, 313–319.CrossRefGoogle ScholarPubMed
D'Mello, JPF & Lewis, D (1970) Amino acid interactions in chick nutrition. 2. Interrelationships between leucine, isoleucine and valine. British Poultry Science 11, 313–323.CrossRefGoogle ScholarPubMed
Davidson, J, Mathieson, J & Boyne, AW (1970) The use of automation in determining nitrogen by the Kjeldahl method, with final calculation by computer. Analyst 95, 181–193.CrossRefGoogle Scholar
Dixon, JL & Benevenga, NJ (1980) The decarboxylation of α-keto-gamma-methiolbutyrate in rat liver mitochondria. Biochemical and Biophysical Research Communications 97, 939–946.CrossRefGoogle ScholarPubMed
Eriksson, S, Hagenfeldt, L & Wahren, J (1981) A comparison of the effects of intravenous infusion of individual branched-chain amino acids on blood amino acid levels in man. Clinical Science 60, 95–100.CrossRefGoogle ScholarPubMed
Fuller, MF, Weekes, TEC, Cadenhead, A & Bruce, JB (1977) The protein-sparing effect of carbohydrate. 2. The role of insulin. British Journal of Nutrition 38, 489–496.CrossRefGoogle ScholarPubMed
Goldberg, AL & Tischler, ME (1981) Regulatory effects of leucine on carbohydrate and protein metabolism. In Metabolism and Clinical Implications of Branched Chain Amino and Ketoacids, pp. 205–216 [Walser, M, and Williamson, JR, editors]. New York, NY: Elsevier/North-Holland.Google Scholar
Guidotti, GG & Gazzola, GC (1992) Amino acid transporters: systematic approach and principles of control. In Mammalian Amino Acid Transport, pp. 3–29 [Kilberg, MS and Häusinger, D, editors]. New York, NY: Plenum Press.CrossRefGoogle Scholar
Hargrove, DM, Rogers, QR, Calvert, CC & Morris, JG (1988) Effects of dietary excesses of branched-chain amino acids on growth, food intake and plasma amino acid concentrations of kittens. Journal of Nutrition 118, 311–320.CrossRefGoogle ScholarPubMed
Harper, AE (1983) Some recent developments in the study of amino acid metabolism. Proceedings of the Nutrition Society 42, 437–449.Google Scholar
Harper, AE, Miller, RH & Block, KP (1984) Branched-chain amino acid metabolism. Annual Review of Nutrition 4, 409–454.CrossRefGoogle ScholarPubMed
Harper, AE & Peters, JC (1983) Amino acid signals and food intake and p: relation to body protein metabolism. In Nutritional Adequacy, Nutrient Availability and Needs, Nestlé Nutrition Research Symposium/Experientia Supplementum, vol. 44, pp. 107–134 [Mauron, J, editor]. Basel: Birkhäuser Verlag.CrossRefGoogle Scholar
Harper, AE & Zapalowski, C (1981) Metabolism of branched chain amino acids. In Nitrogen Metabolism in Man, pp. 97–115 [Waterlow, JC, and Stephen, JML, editors]. London and New Jersey: Applied Science Publishers.Google Scholar
Henry, Y, Duée, PH & Rérat, A (1976) Isoleucine requirement of the growing pig and leucine–isoleucine interrelationship. Journal of Animal Science 42, 357–364.CrossRefGoogle ScholarPubMed
Jones, SMA & Yeaman, SJ (1986) Oxidative decarboxylation of 4-methylthio-2-oxobutyrate by branched-chain 2-oxo acid dehydrogenase complex. Biochemical Journal 237, 621–623.CrossRefGoogle ScholarPubMed
Krebs, H & Lund, P (1977) Aspects of the regulation of the metabolism of branched-chain amino acids. Advances in Enzyme Regulation 15, 375–394.CrossRefGoogle Scholar
Kyriazakis, I & Emmans, GC (1993) Whole body amino acid composition of the growing pig. Journal of the Science of Food and Agriculture 62, 29–33.CrossRefGoogle Scholar
Langer, S & Fuller, MF (2000) Interactions among the branched-chain amino acids and their effects on methionine utilization in growing pigs: effects on nitrogen retention and amino acid utilization. British Journal of Nutrition 83, 43–48.CrossRefGoogle ScholarPubMed
Li, JB & Jefferson, LS (1978) Influence of amino acid availability on protein turnover in perfused skeletal muscle. Biochimica et Biophysica Acta 544, 351–359.CrossRefGoogle ScholarPubMed
Livesey, G (1981) Metabolism of 'essential' 2-oxo acids by liver and a role for branched-chain oxo acid dehydrogenase in the catabolism of methionine. In Metabolism and Clinical Implications of Branched Chain Amino and Ketoacids, pp. 143–148 [Walser, M, and Williamson, JR, editors]. New York, NY: Elsevier/North-Holland.Google Scholar
Livesey, G (1984) Methionine degradation: 'anabolic and catabolic'. Trends in Biochemical Science 5, 27–29.CrossRefGoogle Scholar
Livesey, G & Lund, P (1980) Methionine metabolism via the transamination pathway in rat liver. Biochemical Society Transactions 8, 540–541.CrossRefGoogle ScholarPubMed
Matthews, DE, Schwarz, HP, Yang, RD, Motil, KJ, Young, VR & Bier, DM (1982) Relationship of plasma leucine and α-ketoisocaproate during a L-[1-13C]leucine infusion in man: a method for measuring human intracellular leucine tracer enrichment. Metabolism 31, 1105–1112.CrossRefGoogle Scholar
Mitch, WE & Clark, AS (1984) Specificity of effects of leucine and its metabolites on protein degradation in skeletal muscle. Biochemical Journal 222, 579–586.CrossRefGoogle ScholarPubMed
Mitchell, AD & Benevenga, NJ (1978) The role of transamination in methionine oxidation in the rat. Journal of Nutrition 108, 67–78.CrossRefGoogle ScholarPubMed
Nair, KS, Schwartz, RG & Welle, S (1992) Leucine as a regulator of whole body and skeletal muscle protein metabolism in humans. American Journal of Physiology 263, E928–E934.Google ScholarPubMed
Naumann, C & Bassler, R (1993) Methodenbuch (Band III) Die chemische Untersuchung von Futtermitteln. Darmstadt: VDLUFA-Verlag.Google Scholar
Oestemer, GA, Hanson, LE & Meade, RJ (1973) Leucine–isoleucine interrelationship in the young pig Journal of Animal Science 36, 674–678.CrossRefGoogle ScholarPubMed
Oxender, DL & Christensen, HN (1963) Distinct mediating systems for the transport of neutral amino acids by the Ehrlich cell Journal of Biological Chemistry 238, 3686–3699.CrossRefGoogle ScholarPubMed
Papet, D, Breuille, F, Glomot, F & Arnal, M (1988) Nutritional and metabolic effects of dietary leucine excess in preruminant. lambs Journal of Nutrition 118, 450–455.CrossRefGoogle ScholarPubMed
Paxton, R & Harris, RA (1984) Regulation of branched-chain α-ketoacid dehydrogenase kinase. Archives of Biochemistry and Biophysics 231, 48–57.CrossRefGoogle ScholarPubMed
Peng, Y, Gubin, J, Harper, AE, Vavich, MG & Kemmerer, AR (1973) Food intake regulation: amino acid toxicity and changes in rat brain and plasma amino acids. Journal of Nutrition 103, 608–617.CrossRefGoogle ScholarPubMed
Rogers, QR, Spolter, PD & Harper, AE (1962) Effect of leucine–isoleucine antagonism on plasma amino acid pattern of rats. Archives of Biochemistry and Biophysics 97, 497–504.CrossRefGoogle Scholar
Rüdiger, HW, Langenbeck, U & Goedde, HW (1972) A simplified method for the preparation of 14C-labelled branched-chain α-oxo acids. Biochemical Journal 126, 445–446.CrossRefGoogle Scholar
Shinnick, FL & Harper, AE (1977) Effects of branched-chain amino acid antagonism in the rat on tissue amino acid and keto acid concentrations. Journal of Nutrition 107, 887–895.CrossRefGoogle ScholarPubMed
Smith, TK & Austic, RE (1978) The branched-chain amino acid antagonism in chicks. Journal of Nutrition 108, 1180–1191.CrossRefGoogle ScholarPubMed
Synderman, SE, Cusworth, DC, Roitman, E & Holt, LE (1959) Amino acid interrelationship: the effect of variations in leucine intake. Proceedings of the Society for Experimental Biology and Medicine 18, 546 Abstr.Google Scholar
Tackman, JM, Tews, JK & Harper, AE (1990) Dietary disproportions of amino acids in the rat: effect on food intake, plasma and brain amino acids and brain serotonin. Journal of Nutrition 120, 521–533.CrossRefGoogle ScholarPubMed
Tannous, RI, Rogers, QR & Harper, AE (1966) Effect of leucine–isoleucine antagonism on the amino acid pattern of plasma and tissues of the rat. Archives of Biochemistry and Biophysics 113, 356–361.CrossRefGoogle ScholarPubMed
Taylor, AJ, Cole, DJA & Lewis, D (1984) Amino acid requirements of growing pigs. 5. The interactions between isoleucine and leucine. Animal Production 38, 257–261.Google Scholar
Wahren, J, Eriksson, S & Hagenfeldt, L (1981) Influence of branched-chain amino acids and ketoacids on arterial concentrations and brain exchange of amino acids in man. In Metabolism and Clinical Implications of Branched Chain Amino and Ketoacids, pp. 471–480 [Walser, M, and Williamson, JR, editors]. New York, NY: Elsevier/North-Holland.Google Scholar
Wang, TC & Fuller, MF (1989) The optimum dietary amino acid pattern for growing pigs. 1. Experiments by amino acid deletion. British Journal of Nutrition 62, 77–89.CrossRefGoogle ScholarPubMed
Wu, G & Thompson, JR (1989) Is methionine transaminated in skeletal muscle?. Biochemical Journal 257, 281–284.CrossRefGoogle ScholarPubMed