Asian-Australasian Journal of Animal Sciences

Asian Australasian Association of Animal Production Societies (아세아태평양축산학회)
권호 표지
DOI QR코드

DOI QR Code

Comparison of the [$^2H_5$]Phenylalanine Model with the [1-$^{13}C$]Leucine Method to Determine Whole Body Protein Synthesis and Degradation in Sheep Fed at Two Levels

  • Al-Mamun, M. (Department of Animal Science, Faculty of Agriculture, Iwate University) ;
  • Ito, C. (Department of Animal Science, Faculty of Agriculture, Iwate University) ;
  • Fujita, T. (Department of Animal Science, Faculty of Agriculture, Iwate University) ;
  • Sano, H. (Department of Animal Science, Faculty of Agriculture, Iwate University) ;
  • Sato, A. (Department of Animal Science, Faculty of Agriculture, Iwate University)
  • Received : 2007.02.01
  • Accepted : 2007.04.17
  • Published : 2007.10.01
Download PDF
⟨ Previous Next ⟩

Abstract

The [$^2H_5$]phenylalanine model was compared with the [1-$^{13}C$]leucine method to determine whole body protein synthesis (WBPS) and degradation (WBPD) in sheep fed at two levels. The animals were fed either 103 (M-diet) or 151 (H-diet) kcal $ME/kg^{0.75}/day$ once daily in a crossover design for 21 days each. The isotope dilutions were simultaneously conducted as a primed-continuous infusion of [$^2H_5$]phenylalanine, [$^2H_2$]tyrosine and [1-$^{13}C$]leucine on each dietary treatment. The WBPS and WBPD calculated from the [$^2H_5$]phenylalanine model were lower (p = 0.009 and p = 0.003, respectively) than those calculated from the [1-$^{13}C$]leucine method. The WBPS tended to be higher (p = 0.08) and WBPD was numerically higher (p = 0.33) for H-diet than M-diet in the [$^2H_5$]phenylalanine model, whereas the WBPS was numerically higher (p = 0.37) for H-diet and WBPS remained similar (p = 0.79) between diets in the [1-$^{13}C$]leucine method. However, the absolute values and the directions of WBPS as well as WBPD from M-diet to H-diet were comparable between the [$^2H_5$]phenylalanine model and [1-$^{13}C$]leucine method. Moreover, the values vary depending on the use of the respective amino acid contents in the carcass protein when calculating WBPS and WBPD. Therefore, it is concluded that the [$^2H_5$]phenylalanine model could be used as an alternative to the [1-$^{13}C$]leucine method for the determination of WBPS and WBPD in sheep.

Keywords

References

  1. Borel, M. J., P. E. Williams, K. Jabbour, J. C. Hibbard and P. J. Flakoll. 1997. Maintaining muscle protein anabolism after a metabolic stress: role of dextrose vs. amino acid availability. Am. J. Physiol. Endocrinol. Metab. 272:E36-E44.
  2. Bregendahl, K., L. Liu, J. P. Cant, H. S. Bayley, B. W. McBride, L. P. Milligan, J. T. Yen and M. Z. Fan. 2004. Fractional protein synthesis rates measured by an intraperitoneal injection of a flooding dose of L-[ring-2H5]phenylalanine in pigs. J. Nutr. 134:2722-2728.
  3. Brouwer, E. 1965. Report on sub-committee on constants and factors. In: Energy Metabolism. (Ed. K. L. Blaxter). Academic Press, London. pp. 302-304.
  4. Calder, A. G. and A. Smith. 1988. Stable isotope ratio analysis of leucine and ketoisocaproic acid in blood plasma by gas chromatography/mass spectrometry. Use of tertiary butyldimethylsilyl derivatives. Rapid Commun. Mass Spectrom. 2:14-16. https://doi.org/10.1002/rcm.1290020105
  5. Clark, S. E., C. A. Karn, J. A. Ahlrichs, J. Wang, C. A. Leitch, E. A. Leitchty and S. C. Denne. 1997. Acute changes in leucine and phenylalanine kinetics produced by parenteral nutrition in premature infants. Pediatr. Res. 41:568-574. https://doi.org/10.1203/00006450-199704000-00019
  6. Clarke, J. T. R. and D. M. Bier. 1982. The conversion of phenylalanine to tyrosine in man. Direct measurement by continuous intravenous tracer infusions of L-[ring-$^2H_5$]phenylalanine and L-[1-$^{13}C$]tyrosine in the post absorptive state. Metabol. 31:999-1005. https://doi.org/10.1016/0026-0495(82)90142-1
  7. Connell, A., A. G. Calder, S. E. Anderson and G. E. Lobley. 1997. Hepatic protein synthesis in sheep: effect of intake as monitored by use of stable-isotope-labelled glycine, leucine and phenylalanine. Br. J. Nutr. 77:255-271. https://doi.org/10.1079/BJN19970028
  8. Fujita, T., M. Kajita and H. Sano. 2007. Effects of non-protein energy intake on whole body protein synthesis, nitrogen retention and glucose turnover in goats. Asian-Aust. J. Anim. Sci. 20:536-542. https://doi.org/10.5713/ajas.2007.536
  9. Fujita, T., M. Kajita and H. Sano. 2006. Responses of whole body protein synthesis, nitrogen retention and glucose kinetics to supplemental starch in goats. Comp. Biochem. Physiol. B. 144:180-187. https://doi.org/10.1016/j.cbpb.2006.02.004
  10. Gibson, N. R., F. Jahoor, L. Ware and A. A. Jackson. 2002. Endogenous glycine and tyrosine production is maintained in adults consuming a marginal-protein diet. Am. J. Clin. Nutr. 75:511-518. https://doi.org/10.1093/ajcn/75.3.511
  11. Harris, P. M., P. A. Skene, V. Buchan, E. Milne, A. G. Calder, S. E. Anderson, A. Connell and G. E. Lobley. 1992. Effect of food intake on hind-limb and whole-body protein metabolism in young growing sheep: chronic studies based on arterio-venous techniques. Br. J. Nutr. 68:389-407. https://doi.org/10.1079/BJN19920097
  12. Kita, K., T. Muramatsu, I. Tasaki and J. Okumura. 1989. Influence of dietary non-protein energy intake on whole-body protein turnover in chicks. Br. J. Nutr. 61:235-244. https://doi.org/10.1079/BJN19890112
  13. Krishnamurti, C. R. and S. M. Janssens. 1988. Determination of leucine metabolism and protein turnover in sheep, using gasliquid chromatography-mass spectrometry. Br. J. Nutr. 59:155-164. https://doi.org/10.1079/BJN19880019
  14. Lapierre, H., J. P. Blouin, J. F. Bernier, C. K. Reynolds, P. Dubreuil and G. E. Lobley. 2002. Effect of supply of metabolizable protein on whole body and splanchnic leucine metabolism in lactating cows. J. Dairy Sci. 85:2631-2641. https://doi.org/10.3168/jds.S0022-0302(02)74348-8
  15. Lobley, G. E., X. Shen, G. Le, D. M. Bremner, E. Milne, A. G. Calder, S. E. Anderson and N. Dennison. 2003. Oxidation of essential amino acids by the ovine gastrointestinal tract. Br. J. Nutr. 89:617-629. https://doi.org/10.1079/BJN2003831
  16. Marchini, J. S., L. Castillo, T. E. Chapman, J. A. Vogt, A. Ajami and V. R. Young. 1993. Phenylalanine conversion to tyrosine: comparative determination with L-[Ring-$^2H_5$]phenylalanine and L-[1-$^{13}C$]phenylalanine as tracers in man. Metabol. 42:1316-1322. https://doi.org/10.1016/0026-0495(93)90131-7
  17. Matthews, D. E., H. P. Schwarz, R. D. Yang, K. J. Motil, V. R. Young and D. M. Bier. 1982. Relationship of plasma leucine and alpha-ketoisocaproate during a L-[1-$^{13}C$]leucine infusion in man: a method for measuring human intracellular leucine tracer enrichment. Metabol. 31:1105-1112. https://doi.org/10.1016/0026-0495(82)90160-3
  18. Millward, D. J., G. M. Price, P. J. H. Pacy and D. Halliday. 1991. Whole-body protein and amino acid turnover in man: what can we measure with confidence? Proc. Nutr. Soc. 50:197-216. https://doi.org/10.1079/PNS19910030
  19. National Research Council. 1985. Nutrient Requirements of Sheep. 6th rev. ed. National Academy Press, Washington, DC.
  20. Pacy, P. J., G. M. Price, D. Halliday, M. R. Quevedo and D. J. Millward. 1994. Nitrogen homeostasis in man: the diurnal responses of protein synthesis and degradation and amino acid oxidation to diets with increasing protein intakes. Clin. Sci. 86:103-118. https://doi.org/10.1042/cs0860103
  21. Pen, B., T. Iwama, M. Ooi, T. Saitoh, K. Kida, T. Iketaki, J. Takahashi and H. Hidari. 2006. Effect of potato by-products based silage on rumen fermentation, methane production and nitrogen utilization in holstein steers. Asian-Aust. J. Anim. Sci. 19:1283-1290. https://doi.org/10.5713/ajas.2006.1283
  22. Reeds, P. J., M. F. Fuller, A. Cadenhead and G. E. Lobley. 1981. Effects of changes in the intakes of protein and non-protein energy on whole-body protein turnover in growing pigs. Br. J. Nutr. 45:539-546. https://doi.org/10.1079/BJN19810132
  23. Rocchiccioli, F., J. P. Leroux and P. Cartier. 1981. Quantitation of 2-ketoacids in biological fluids by gas chromatography chemical ionization mass spectrometry of o-trimethylsilylquinoxalinol derivatives. Biomed. Mass Spectrom. 8:160-164. https://doi.org/10.1002/bms.1200080406
  24. Sano, H., M. Kajita and T. Fujita. 2004. Effect of dietary protein intake on plasma leucine flux, protein synthesis, and degradation in sheep. Comp. Biochem. Physiol. B 139:163-168. https://doi.org/10.1016/j.cbpc.2004.06.018
  25. SAS. 1996. $SAS/STAT^{\circledR}$ Software: Changes and Enhancements through Release 6.11. SAS Inst. Inc. Cary, NC.
  26. Savary-Auzeloux, I., S. O. Hoskin and G. E. Lobley. 2003. Effect of intake on whole body plasma amino acid kinetics in sheep. Reprod. Nutr. Dev. 43:117-129. https://doi.org/10.1051/rnd:2003010
  27. Schroeder, G. F., E. C. Titgemeyer, M. S. Awawdeh, J. S. Smith and D. P. Gnad. 2006. Effects of energy level on methionine utilization by growing steers. J. Anim. Sci. 84:1497-1504.
  28. Thompson, G. N., P. J. Pacy, H. Merritt, G. C. Ford, M. A. Read, K. N. Cheng and D. Halliday. 1989. Rapid measurement of whole body and forearm protein turnover using a [$^2H_5$]phenylalanine model. Am. J. Physiol. 256:E631-E639.
  29. Weatherburn, M. W. 1967. Phenol-hypochloride reaction for determination of ammonia. Anal. Chem. 39:971-974. https://doi.org/10.1021/ac60252a045
  30. Whittaker, P. G., C. H. Lee, B. G. Cooper and R. Taylor. 1999. Evaluation of phenylalanine and tyrosine metabolism in late human pregnancy. Metabol. 48:849-852. https://doi.org/10.1016/S0026-0495(99)90217-2
  31. Wolfe, R. R. 1984. Tracers in metabolic research. Radioisotope and stable isotope/mass spectrometry methods. Alan R. Liss, Inc., New York.
  32. Young, B. A., B. Kerrigan and R. J. Christopherson. 1975. A versatile respiratory pattern analyzer for studies of energy metabolism of livestock. Can. J. Anim. Sci. 55:17-22. https://doi.org/10.4141/cjas75-003
  33. Zello, G. A., L. Marai, A. S. F. Tung, R. O. Ball and P. B. Pencharz. 1994. Plasma and urine enrichments following infusion of L- [1-$^{13}C$]phenylalanine and L-[ring-$^2H_5$]phenylalanine in humans: evidence for an isotope effects in renal tubular reabsorption. Metabol. 43:487-491. https://doi.org/10.1016/0026-0495(94)90082-5

Cited by

  1. Responses of whole body protein synthesis and degradation to plantain herb in sheep exposed to heat vol.62, pp.3, 2008, https://doi.org/10.1080/17450390801892633
  2. Effect of feeding garlic leaf on microbial nitrogen supply, kinetics of plasma phenylalanine, tyrosine and protein synthesis in sheep vol.85, pp.5, 2014, https://doi.org/10.1111/asj.12190
  3. Effect of Chinese herbal medicine on kinetics of plasma phenylalanine, tyrosine and whole body protein synthesis in sheep pp.13443941, 2019, https://doi.org/10.1111/asj.13180
  4. The effect of the source of nitrogen supplementation on nitrogen balance, rates of plasma leucine turnover, protein synthesis and degradation in sheep vol.63, pp.5, 2009, https://doi.org/10.1080/17450390903052698
  5. Intermediary Metabolism of Plasma Acetic Acid, Glucose and Protein in Sheep Fed a Rice Straw-based Diet vol.23, pp.10, 2007, https://doi.org/10.5713/ajas.2010.10077
  6. Effects of dietary energy intake and cold exposure on kinetics of plasma phenylalanine, tyrosine and protein synthesis in sheep vol.64, pp.1, 2010, https://doi.org/10.1080/17450390903461253