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Transsulfuration, protein synthesis rate and follicle mRNA in the skin of young Merino lambs in response to infusions of methionine and serine

Published online by Cambridge University Press:  09 March 2007

S. M. Liu ,
G. Mata ,
S. Figliomeni ,
B. C. Powell ,
A. Nesci  and
D. G. Masters
S. M. Liu*
Affiliation:
CSIRO Animal Production and CRC for Premium Quality Wool, Private Bag PO, Wembley WA 6014, Australia
G. Mata
Affiliation:
CSIRO Animal Production and CRC for Premium Quality Wool, Private Bag PO, Wembley WA 6014, Australia
S. Figliomeni
Affiliation:
CSIRO Animal Production and CRC for Premium Quality Wool, Private Bag PO, Wembley WA 6014, Australia
B. C. Powell
Affiliation:
Department of Animal Science, University of Adelaide, Waite Campus, Glen Osmond, SA 5006, Australia
A. Nesci
Affiliation:
Department of Animal Science, University of Adelaide, Waite Campus, Glen Osmond, SA 5006, Australia
D. G. Masters
Affiliation:
CSIRO Animal Production and CRC for Premium Quality Wool, Private Bag PO, Wembley WA 6014, Australia
*
*Corresponding author: Dr S. M. Liu, fax +618 9387 8991, email [email protected]
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Abstract

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Methionine (Met) is usually the first limiting amino acid for sheep and supplements of Met may increase production of wool and meat. The wool response may be due to an increased supply of cysteine (Cys) from transsulfuration (TS) of Met. Met is catabolized through homocysteine to form Cys when the S from Met is transferred to serine (Ser). We hypothesized that providing additional Met would create a deficiency of Ser and that by simultaneously providing Met and Ser, TS and wool growth could be increased more than by providing Met alone. The effects of i.v. infusions of Met and Ser to young Merino lambs on TS, fractional synthesis rate (FSR) of protein in skin, follicle mRNA and wool growth were examined. Following 4 d of constant i.v. infusion of 3 g Met/d, or 10 g Ser/d or both, the isotope tracers: L-[3-13C]CYS, l-[ring-d5]phenylalanine (Phe) and l-[2,3,3-d3]Ser were infused over 8 h to allow for measurements of irreversible loss rate (ILR), and TS in whole body and skin. Skin biopsies were taken for measurement of FSR. Wool growth rate was measured using autoradiography. An infusion of Met significantly (P < 0·05) improved wool growth rate and increased skin FSR, Cys supply from TS and enhanced levels of follicle mRNA (from the K2.10 intermediate filament gene and three gene families encoding keratin associated proteins KAP1, KAP4 and KAP12). The extra Met lowered Ser ILR. The infusion of Ser doubled Ser ILR in the body and increased skin FSR calculated using the Cys tracer in plasma (P < 0·05). However, there were no significant (P > 0·05) changes in TS, skin FSR calculated using the Phe and Ser tracers, follicle mRNA or wool growth rate as a result of Ser infusion. While there were trends towards increased TS and FSR with Ser infusion, the overall lack of significant changes indicates a high capacity for the de novo synthesis of Ser.

Keywords

Stable isotopesAmino acidsCysteineGlycineWoolSheep
Type
Research Article
Information
British Journal of Nutrition , Volume 83 , Issue 4 , April 2000 , pp. 401 - 409
Copyright
Copyright © The Nutrition Society 2000

References

Agricultural Research Council (1984) The Nutrient Requirements of Ruminant Livestock. Slough: Commonwealth Agricultural Bureaux.Google Scholar
Arends, J, Schafer, G, Schauder, P, Bircher, J and Bier, DM (1995) Comparison of serine and hippurate as precursor equivalents during infusion of [15N]glycine for measurement of fractional synthesis rates of apolipoprotein B of very-low-density lipoprotein. Metabolism 44, 1253–1258.CrossRefGoogle ScholarPubMed
Benevenga, NJ & Egan, AR (1983) Quantitative aspects of methionine metabolism. In Sulfur Amino Acids — Biochemical and Clinical Aspects, pp. 327–341. New York, NY: Alan R. Liss, Inc.Google Scholar
Calder, AG and Smith, A (1988) Stable isotope ratio analysis of leucine and ketoisocaproic acid in blood plasma by gas chromatography/mass spectrometry. Use of tertiary butyldimethylsilyl derivatives. Rapid Communications in Mass Spectrometry 2, 14–16.CrossRefGoogle ScholarPubMed
Calder, AG, Anderson, SE, Grant, IMcNurlan, MA and Garlick, PJ (1992) The determination of low d5-phenylalanine enrichment (0.002–0.09 atom percent excess), after conversion to phenylethylamine, in relation to protein turnover studies by gas chromatography/electron ionization mass spectrometry. Rapid Communications in Mass Spectrometry 6, 421–424.CrossRefGoogle ScholarPubMed
Campbell, CG, Titgemeyer, EC and St-Jean, G (1997) Sulphur amino acid utilization by growing steers. Journal of Animal Science 75, 230–238.CrossRefGoogle ScholarPubMed
Cetin, I, Fennessey, PV, Quick, JAN, Marconi, AM, Meschia, G, Battaglia, FC and Sparks, JW (1991) Glycine turnover and oxidation and hepatic serine synthesis from glycine in foetal lambs. American Journal of Physiology 260, E371–E378.Google Scholar
Chomczynski, P and Sacchi, N (1987) Single-step of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Analytical Biochemistry 162, 156–159.CrossRefGoogle ScholarPubMed
Cooper, AJL (1983) Biochemistry of sulphur-containing amino acids. Annual Review of Biochemistry 52, 187–222.CrossRefGoogle Scholar
Downes, AM, Clarke, WH and Dagg, TC (1967) The use of radioisotopes in the measurement of wool growth. Atomic Energy in Australia 10, 2–7.Google Scholar
Fratini, A, Powell, BC, Hynd, PI, Keough, RA and Rogers, GE (1994) Dietary cysteine regulates the levels of mRNAs encoding a family of cysteine-rich proteins of wool. Journal of Investigative Dermatology 102, 178–185.CrossRefGoogle ScholarPubMed
Frontiera, MS, Stabler, SP, Kolhouse, JF and Allen, RH (1994) Regulation of methionine metabolism: effects of nitrous oxide and excess dietary methionine. Journal of Nutritional Biochemistry 5, 28–38.CrossRefGoogle Scholar
Fuller, MF and Garlick, PJ (1994) Human amino acid requirements: Can the controversy be resolved?. Annual Review of Nutrition 14, 217–241.CrossRefGoogle ScholarPubMed
Galbraith, H (1998) Nutritional and hormonal regulation of hair follicle growth and development. Proceedings of the Nutrition Society 57, 195–205.CrossRefGoogle ScholarPubMed
Harris, PM, Dellow, DW and Sinclair, BR (1989) Preliminary. 'in vivo' measurements of protein and energy metabolism in the skin of sheep. Australian Journal of Agricultural Research 40, 879–888.CrossRefGoogle Scholar
Hynd, PI and Nancarrow, MJ (1996) Inhibition of polyamine synthesis alters hair follicle function and fibre composition. Journal of Investigative of Dermatology 106, 249–253.CrossRefGoogle Scholar
Liu, SM, Mata, G, O'Donoghue, H and 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
Liu, SM and Figliomeni, S (1998) GC/MS analyses of [2,3,3-d3]serine, [2,3,3-d3]cysteine and [3-13C]cysteine in plasma and skin protein: measurement of transsulphuration in young sheep. Rapid Communications in Mass Spectrometry 12, 1–5.3.0.CO;2-D>CrossRefGoogle Scholar
Lobley, GE, Harris, PM, Skene, PA, Brown, D, Milne, E, Calder, AG, Anderson, SE, Garlick, PJ, Nevison, I and Connell, A (1992) Responses in tissue synthesis to sub- and supra-maintenance intake in young growing sheep: comparison of large-dose and continuous-infusion techniques. British Journal of Nutrition 68, 373–388.CrossRefGoogle ScholarPubMed
Lobley, GE, Connell, A and Revell, D (1996) The importance of transmethylation reactions to methionine metabolism in sheep: effects of supplementation with creatine and choline. British Journal of Nutrition 75, 47–56.CrossRefGoogle ScholarPubMed
MacRae, JC, Walker, A, Brown, D and 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
Masters, DG, Mata, G, Liu, SM and O'Dea, TJ (1998) Influence of type and timing of protein feeding on wool growth and staple strength in young sheep. Animal Production in Australia 22, 367.Google Scholar
Mata, G, Masters, DG, Buscall, D, Street, K and Schlink, AC (1995) Responses in wool growth, liveweight, glutathione and amino acids, in Merino wethers fed increasing amounts of methionine protected from degradation in the rumen. Australian Journal of Agricultural Research 46, 1189–1204.CrossRefGoogle Scholar
Muramatsu, T, Hatano, T, Ueda, Y, Furuse, M and Okumura, J (1994) Whole-body protein turnover in goats enhanced by supplementing a diet with rumen protected methionine. Asian–Australian Journal of Animal Sciences 7, 279–288.CrossRefGoogle Scholar
Nash, JE, Rocha, HJG, Buchan, V, Calder, GA, Milne, E, Quirke, JF and Lobley, GE (1994) The effect of acute and chronic administration of the β-agonist, cimaterol, on protein synthesis in ovine skin and muscle. British Journal of Nutrition 71, 501–513.CrossRefGoogle ScholarPubMed
Pisulewski, PM and Buttery, PJ (1985) The effect of increasing methionine supply on the methionine conversion to cyst(e)ine in sheep. British Journal of Nutrition 54, 121–129.CrossRefGoogle ScholarPubMed
Powell, BC & Rogers, GE (1997) The role of keratin proteins and their genes in the growth, structure and properties of hair. In Formation and Structure of Human Hair, pp. 59–148 [Jolles, P, Zahn, H and Hocker, H, editors]. Basel: Birkhauser Verlag.CrossRefGoogle Scholar
Reis, PJ (1979) Effects of amino acids on the growth and properties of wool. In Physiological and Environmental Limitations to Wool Growth, pp. 223–243 [Black, JL, and Reis, PJ, editors]. Armidale: University of New England Publishing Unit.Google Scholar
Reis, PJ and Hynd, PI (1989) The influence of alpha-difluoromethylornithine on the activity of wool follicles. Asian–Australian Journal of Animal Sciences 2, 204–205.CrossRefGoogle Scholar
Reis, PJ, Tunks, DA and Munro, SG (1990) Effects of the infusion of amino acids into the abomasum of sheep, with emphasis on the relative value of methionine, cysteine and homocysteine for wool growth. Journal of Agricultural Science, Cambridge 114, 59–68.CrossRefGoogle Scholar
Sambrook, J, Fritsch, EF & Maniatis, T (1989) Molecular Cloning: A Laboratory Manual, 2nd ed. New York NY: Cold Spring Harbor Laboratory Press.Google Scholar
Slater, C, Preston, T, McMillan, DC, Falconer, JS and Fearon, KCH (1995) GC/MS analysis of [2H5]phenylalanine at very low enrichment: measurement of protein synthesis in health and disease. Journal of Mass Spectrometry 30, 1325–1332.CrossRefGoogle Scholar
Williams, AJ, Murison, R and Padgett, J (1988) Metabolism of sulphur-containing amino acids by pregnant Merino ewes. Australian Journal of Biological Sciences 41, 247–259.CrossRefGoogle Scholar