Hostname: page-component-586b7cd67f-2plfb Total loading time: 0 Render date: 2024-11-23T05:51:23.390Z Has data issue: false hasContentIssue false
  • English
  • Français

Effect of feed intake on ovine hindlimb protein metabolism based on thirteen amino acids and arterio–venous techniques

Published online by Cambridge University Press:  09 March 2007

Simone O. Hoskin ,
Isabelle C. Savary ,
Grietje Zuur  and
Gerald E. Lobley
Simone O. Hoskin*
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB21 9SB, Scotland, UK
Isabelle C. Savary
Affiliation:
INRA-Centre de Clermont-Ferrand/Theix, 63122 Saint Genes-Champanelle, France
Grietje Zuur
Affiliation:
Biomathematics and Statistics Scotland, Rowett Research Institute, Bucksburn, Aberdeen AB21 9SB, Scotland, UK
Gerald E. Lobley
Affiliation:
Rowett Research Institute, Bucksburn, Aberdeen AB21 9SB, Scotland, UK
*
*Corresponding author: Dr Simone O. Hoskin, present address Institute of Food, Nutrition and Human Health, Massey University, Private Bag 11222, Palmerston North, New Zealand, fax +64 6 3505684, email [email protected]
Rights & Permissions [Opens in a new window]

Abstract

Core share and HTML view are not available for this content. However, as you have access to this content, a full PDF is available via the ‘Save PDF’ action button.

It has been suggested that protein synthesis in peripheral tissues: (1) responds in a curvilinear manner to increasing feed intake over a wide range of feeding levels; and (2) has a greater sensitivity to intake than protein breakdown. The aim of the present experiment was to test these hypotheses across the ovine hindlimb. Six growing sheep (6–8 months, 30–35 kg), with catheters in the aorta (two), posterior vena cava and jugular vein, received each of four intakes of dried grass pellets (0·5, 1·0, 1·5 and 2·5×maintenance energy; M) for a minimum of 7 d. A U-13C-labelled algal hydrolysate was infused intravenously for 10 h and from 3–9 h para-aminohippuric acid was infused to measure plasma flow. Arterial and venous plasma were obtained over the last 4 h and the concentrations and enrichments of thirteen 13C-labelled amino acids (AA) were determined by GC–MS. As intake increased, a positive linear response was found for plasma flow, arterial concentrations of the aromatic and branched-chain AA, total flow of all AA into the hindquarters and net mass balance across the hindquarters (except glycine and alanine). Based on two separate statistical analyses, the data for protein synthesis showed a significant linear effect with intake (except for phenylalanine, glycine and alanine). No significant curvilinear effect was found, which tends not to support hypothesis 1. Nonetheless, protein synthesis was not significantly different between 0·5, 1·0 and 1·5×M and thus the 2·5×M intake level was largely responsible for the linear relationship found. There was no significant response in protein breakdown to intake, which supports hypothesis 2.

Keywords

Amino acidsProtein metabolismFeed intakeHindlimbArterio–venousSheep
Type
Research Article
Information
British Journal of Nutrition , Volume 86 , Issue 5 , November 2001 , pp. 577 - 585
Copyright
Copyright © The Nutrition Society 2001

References

Referenses

Airhart, J, Vidrich, A & Khairallah, EA (1974) Compartmentation of free amino acids for protein synthesis in rat liver. Biochemical Journal 140, 539–545.CrossRefGoogle ScholarPubMed
Boisclair, YR, Bauman, DE, Bell, AW, Dunshea, FR & Harkins, M (1994) Nutrient utilisation and protein turnover in the hindlimb of cattle treated with bovine somatotropin. Journal of Nutrition 124, 664–673.CrossRefGoogle ScholarPubMed
Boisclair, YR, Bell, AW, Dunshea, FR, Harkins, M & Bauman, DE (1993) Evaluation of the arteriovenous difference technique to simultaneously estimate protein-synthesis and degradation in the hind-limb of fed and chronically underfed steers. Journal of Nutrition 123, 1076–1088.Google ScholarPubMed
Calder, AG, Garden, KE, Anderson, SE & Lobley, GE (1999) Quantitation of blood and plasma amino acids using isotope dilution mass spectrometry impact gas chromatography/mass spectrometry with U-13C amino acids as internal standards. Rapid Communications in Mass Spectrometry 13, 2080–2083.3.0.CO;2-O>CrossRefGoogle Scholar
Caso, G, Ford, C, Nair, KS, Garlick, PJ & McNurlan, MA (2000) Insulin with euaminoacidemia stimulates muscle protein synthesis in dogs. FASEB Journal 14, A768.Google Scholar
Cetin, I, Fennessey, PV, Sparks, JW, Meschia, G & Battaglia, FC (1992) Fetal serine fluxes across fetal liver, hind-limb, and placenta in late gestation. American Journal of Physiology 263, E786–E793.Google ScholarPubMed
Chang, TW & Goldberg, AL (1978) The origin of alanine produced in skeletal muscle. Journal of Biological Chemistry 253, 3677–3684.CrossRefGoogle ScholarPubMed
Crompton, LA & Lomax, MA (1989) The effect of growth hormone on hind-limb muscle protein metabolism in growing lambs. Proceedings of the Nutrition Society 48, 96A.Google Scholar
Crompton, LA & Lomax, MA (1993) Hind-limb protein-turnover and muscle protein-synthesis in lambs – a comparison of techniques. British Journal of Nutrition 69, 345–358.CrossRefGoogle ScholarPubMed
Davis, TA, Fiorotto, ML, Nguyen, HV & Burrin, DG (1999) Aminoacyl-tRNA and tissue free amino acid pools are equilibrated after a flooding dose of phenylalanine. American Journal of Physiology 277, E103–E109.Google ScholarPubMed
Dawson, JM, Buttery, PJ, Lammiman, MJ, Soar, JB & Essex, CP (1991) Nutritional and endocrinological manipulation of lean deposition in forage-fed steers. British Journal of Nutrition 66, 171–185.CrossRefGoogle ScholarPubMed
Fern, EB & Garlick, PJ (1974) The specific radioactivity of the tissue free amino acid pool as a basis for measuring the rate of protein synthesis in the rat in vivo. Biochemical Journal 142, 413–419.CrossRefGoogle Scholar
Fryburg, DA, Jahn, LA, Hill, SA, Oliveras, DM & Barrett, EJ (1995) Insulin and insulin-like growth factor-1 enhance human skeletal muscle protein anabolism during hyperaminoacidemia by different mechanisms. Journal of Clinical Investigation 96, 1722–1729.CrossRefGoogle ScholarPubMed
Garlick, PJ & Grant, I (1988) Amino acid infusion increases the sensitivity of muscle protein synthesis in vivo to insulin. Effect of branched chain amino acids. Biochemical Journal 254, 579–584.CrossRefGoogle ScholarPubMed
Grizard, J, Dardevet, D, Balage, M, Larbaud, D, Sinaud, S, Savary, I, Grzelkowska, K, Rochon, C, Tauveron, I & Obled, C (1999) Insulin action on skeletal muscle protein metabolism during catabolic states. Reproduction, Nutrition and Development 39, 61–74.CrossRefGoogle ScholarPubMed
Harris, PM, Skene, PA, Buchan, V, Milne, E, Calder, AG, Anderson, SE, Connell, A & Lobley, GE (1992) Effect of food intake on hind-limb and whole-body protein metabolism in young growing sheep: chronic studies based on arterio–venous techniques. British Journal of Nutrition 68, 389–407.CrossRefGoogle ScholarPubMed
Ilan, J & Singer, M (1975) Sampling of the leucine pool from the growing peptide chain: difference in leucine specific activity of peptidyl-transfer RNA from free and membrane-bound polysomes. Journal of Molecular Biology 91, 39–51.CrossRefGoogle ScholarPubMed
Khairallah, EA & Mortimore, GE (1976) Assessment of protein turnover in perfused rat liver. Evidence for amino acid compartmentation from differential labeling of free and tRNA-bound valine. Journal of Biological Chemistry 251, 1375–1384.CrossRefGoogle Scholar
Lee, J, Harris, PM, Sinclair, BR & Treloar, BP (1993) Whole body metabolism of cysteine and glutathione and their utilization in the skin of Romney sheep: consequences for wool growth. Journal of Agricultural Science, Cambridge 121, 111–124.CrossRefGoogle Scholar
Liu, SM, Mata, G, Figliomeni, S, Powell, BC, Nesci, A & Masters, DG (2000) Transsulfuration, protein synthesis rate and follicle mRNA in the skin of young Merino lambs in response to infusions of methionine and serine. British Journal of Nutrition 83, 401–409.Google ScholarPubMed
Liu, SM, Mata, G, Odonoghue, H & Masters, DG (1998) The influence of live weight, live-weight change and diet on protein synthesis in the skin and skeletal muscle in young Merino sheep. British Journal of Nutrition 79, 267–274.CrossRefGoogle ScholarPubMed
Ljungqvist, OH, Persson, M, Ford, GC & Nair, KS (1997) Functional heterogeneity of leucine pools in human skeletal muscle. American Journal of Physiology 36, E564–E570.Google Scholar
Lobley, GE, (1993) Protein metabolism and turnover. In Quantitative Aspects of Ruminant Digestion and Metabolism, 313–339.[Forbes, JM and France, JM, editors] Oxon, UK: CAB International.Google Scholar
Lobley, GE (1993 a) Species comparisons of tissue protein metabolism: effects of age and hormonal action. Journal of Nutrition 123, 337–343.CrossRefGoogle ScholarPubMed
Lobley, GE (1998) Nutritional and hormonal control of muscle and peripheral tissue metabolism in farm species. Livestock Production Science 56, 91–114.CrossRefGoogle Scholar
Lobley, GE, Connell, A & Buchan, V (1987) Effect of food intake on protein and energy metabolism in finishing beef steers. British Journal of Nutrition 57, 457–465.CrossRefGoogle ScholarPubMed
Lobley, GE, Connell, A, Lomax, MA, Brown, DS, Milne, E, Calder, AG & Farningham, DAH (1995) Hepatic detoxification of ammonia in the ovine liver- possible consequences for amino-acid catabolism. British Journal of Nutrition 73, 667–685.CrossRefGoogle ScholarPubMed
Lobley, GE, Connell, A, Revell, DK, Bequette, BJ, Brown, DS & Calder, AG (1996) Splanchnic-bed transfers of amino acids in sheep blood and plasma, as monitored through use of a multiple U-13C-labelled amino acid mixture. British Journal of Nutrition 75, 217–235.CrossRefGoogle ScholarPubMed
Lobley, GE, Harris, PM, Skene, PA, Brown, D, Milne, E, Calder, AG, Anderson, SE, Garlick, PJ, Nevison, I & Connell, A (1992) Responses in tissue protein synthesis to sub- and supra-maintenance intake in growing young sheep: comparison of large-dose and continuous-infusion techniques. British Journal of Nutrition 68, 373–388.CrossRefGoogle ScholarPubMed
Lobley, GE, Sinclair, KD, Grant, CM, Miller, L, Mantle, D, Calder, AG, Warkup, CC & Maltin, CA (2000) The effects of breed and level of nutrition on whole-body and muscle protein metabolism in pure-bred Aberdeen Angus and Charolais beef steers. British Journal of Nutrition 84, 275–284.CrossRefGoogle ScholarPubMed
MacRae, JC, Walker, A, Brown, D & Lobley, GE (1993) Accretion of total protein and individual amino-acids by organs and tissues of growing lambs and the ability of nitrogen-balance techniques to quantitate protein retention. Animal Production 57, 237–245.Google Scholar
Oddy, VH, Lindsay, DB, Barker, PJ & Northrop, AJ (1987) Effect of insulin on hind-limb and whole-body leucine and protein metabolism in fed and fasted lambs. British Journal of Nutrition 58, 437–452.CrossRefGoogle ScholarPubMed
Pell, JM & Bates, PC (1987) Collagen and non-collagen protein turnover in skeletal muscle of growth hormone-treated lambs. Journal of Endocrinology 115, R1–R4.CrossRefGoogle ScholarPubMed
Pell, JM, Caldarone, EM & Bergman, EN (1986) Leucine and α-ketoisocaproate metabolism and interconversions in fed and fasted sheep. Metabolism 35, 1005–1016.CrossRefGoogle ScholarPubMed
Ponter, AA, Cortamira, NO, Seve, B, Salter, DN & Morgan, LM (1994) The effects of energy source and tryptophan on the rate of protein synthesis and on hormones of the entero–insular axis in the piglet. British Journal of Nutrition 71, 661–674.CrossRefGoogle ScholarPubMed
Reeds, PJ, Cadenhead, A, Fuller, MF, Lobley, GE & McDonald, JD (1980) Protein turnover in growing pigs. Effects of age and food intake. British Journal of Nutrition 43, 3–455.CrossRefGoogle ScholarPubMed
Rocha, HJG, Nash, JE, Connell, A & Lobley, GE (1993) Protein-synthesis in ovine muscle and skin – sequential measurements with 3 different amino-acids based on the large-dose procedure. Comparative Biochemistry and PhysiologyB – Biochemistry & Molecular Biology 105, 301–307.CrossRefGoogle ScholarPubMed
Savary, IC, Hoskin, SO, Dennison, N & Lobley, GE (2001) Lysine metabolism across the hindquarters of sheep; effect of intake on transfers from plasma and the red blood cells. British Journal of Nutrition 85, 565–573.CrossRefGoogle ScholarPubMed
Schneible, PA & Young, RB (1984) Leucine pools in normal and dystrophic chicken skeletal muscle cells in culture. Journal of Biological Chemistry 259, 1436–1440.CrossRefGoogle ScholarPubMed
Seve, B, Reeds, PJ, Fuller, MF, Cadenhead, A & Hay, SM (1986) Protein synthesis and retention in some tissues of the young pig as influenced by dietary protein intake after early weaning. Possible connection to the energy metabolism. Reproduction, Nutrition and Development 26, 849–961.CrossRefGoogle Scholar
Teleni, E, Annison, EF & Lindsay, DB (1986) Metabolism of valine and the exchange of amino-acids across the hind-limb muscles of fed and starved sheep. Australian Journal of Biological Sciences 39, 379–393.CrossRefGoogle ScholarPubMed
Tesseraud, S, Grizard, J, Debras, E, Papet, I, Bonnet, Y, Bayle, G & Champredon, C (1993) Leucine metabolism in lactating and dry goats: effect of insulin and substrate availability. American Journal of Physiology 265, E402–E413.Google ScholarPubMed
Thomson, BC, Hosking, BJ, Sainz, RD & Oddy, VH (1997) The effect of nutritional status on protein degradation and components of the calpain system in skeletal muscle of weaned wether lambs. Journal of Agricultural Science, Cambridge 129, 471–477.CrossRefGoogle Scholar
Watt, PW, Corbett, ME & Rennie, MJ (1992) Stimulation of protein synthesis in pig skeletal muscle by infusion of amino acids during constant insulin availability. American Journal of Physiology 263, E453–E460.Google ScholarPubMed
Wester, TJ, Lobley, GE, Birnie, LM & Lomax, MA (2000) Insulin stimulates phenylalanine uptake across the hind-limb in fed lambs. Journal of Nutrition 130, 608–611.CrossRefGoogle ScholarPubMed
Wolff, JE & Bergman, EN (1972) Gluconeogenesis from plasma amino acids in the fed sheep. American Journal of Physiology 223, 455–460.CrossRefGoogle ScholarPubMed
Zhang, X, Chinkes, DL, Doyle, D & Wolfe, RR (1998) Metabolism of skin and muscle protein metabolism is regulated differently in response to nutrition. American Journal of Physiology 274, E484–E492.Google ScholarPubMed