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Amino Acids

, Volume 50, Issue 12, pp 1719–1727 | Cite as

The fractional synthesis rates of plasma proteins as determined using deuterated water are sensitive to dietary intake of lysine in rats

  • Ying TianEmail author
  • Minghui Shi
  • Qianqian Dai
  • Chanfang Meng
  • Ruixia Gu
  • Jing Peng
  • Yu Chen
  • Yunsheng Jiang
Original Article
  • 164 Downloads

Abstract

Traditionally, the effect of dietary lysine upon health is determined through the concentrations of plasma proteins, but sometimes they are not responsive to lysine intake. We hypothesized that the fractional synthesis rates (FSRs) of plasma proteins may be more sensitive to dietary intake of lysine than protein concentrations in plasma. Seventy-two male Sprague–Dawley rats were divided randomly into three groups based on their diets provided for 18 weeks: low lysine (LG), normal lysine (NG) and high lysine (HG). Rats underwent labeling with deuterated water, a more reliable tracer than amino-acid tracers. The FSRs of albumin and immunoglobulin (Ig) G in plasma increased with increasing dietary intake of lysine. However, the albumin concentration in plasma in rats in the LG did not decrease significantly compared with that in the NG, and a similar result was shown for the IgG concentration between the NG and HG. These results suggested that the FSRs of albumin and IgG in plasma were more sensitive to dietary intake of lysine than their concentrations, and could be useful as sensitive indicators of the effect of dietary lysine upon health.

Keywords

Lysine Albumin Immunoglobulin G Concentration Fractional synthesis rate Deuterated water 

Notes

Acknowledgements

This study was funded by the National Natural Science Foundation of China (81472963). The authors are very grateful to Professor Xiaoguang Yang (National Institute for Nutrition and Health, Chinese Center for Disease Control and Prevention) for his invaluable suggestions on study design, and to Dr. Juan Liu (Analysis Center of Yangzhou University) for her skilled technical assistance.

Compliance with ethical standards

Conflict of interest

The authors declare that they have no conflict of interest.

Ethical approval

This study was approved by the Animal Care and Use Committees of Yangzhou University. All applicable international, national, and/or institutional guidelines for the care and use of animals were followed.

References

  1. Belloto E, Fdr Diraison, Basset A, Allain G, Abdallah P, Beylot M (2007) Determination of protein replacement rates by deuterated water: validation of underlying assumptions. Am J Physiol Endocrinol Metab 292:1340–1347CrossRefGoogle Scholar
  2. Bonjour J (2005) Dietary protein: an essential nutrient for bone health. J Am Coll Nutr 24:526–536CrossRefGoogle Scholar
  3. Busch R et al (2006) Measurement of protein turnover rates by heavy water labeling of nonessential amino acids. Biochem Biophys Acta 1760:730–744CrossRefGoogle Scholar
  4. Canfield LM, Chytil F (1978) Effect of low lysine diet on rat protein metabolism. J Nutr 108:1343–1347CrossRefGoogle Scholar
  5. Chen Y-Y, Lin S-Y, Yeh Y-Y, Hsiao H-H, Wu C-Y, Chen S-T, Wang AH-J (2005) A modified protein precipitation procedure for efficient removal of albumin from serum. Electrophoresis 26:2117–2127CrossRefGoogle Scholar
  6. Debro J, Korner A (1956) Solubility of albumin in alcohol after precipitation by trichloroacetic acid: a simplified procedure for separation of albumin. Nature 178:1067PubMedGoogle Scholar
  7. Dufner DA et al (2005) Using 2H2O to study the influence of feeding on protein synthesis: effect of isotope equilibration in vivo vs. in cell culture. Am J Physiol Endocrinol Metab 288:1277–1283CrossRefGoogle Scholar
  8. Gasier HG, Riechman SE, Wiggs MP, Previs SF, Fluckey JD (2009) A comparison of 2H2O and phenylalanine flooding dose to investigate muscle protein synthesis with acute exercise in rats. Am J Physiol Endocrinol Metab 297:252–259CrossRefGoogle Scholar
  9. Gasier HG, Fluckey JD, Previs SF (2010) The application of 2H2O to measure skeletal muscle protein synthesis. Nutr Metab 7:31–38CrossRefGoogle Scholar
  10. Ghosh S, Pellett PL, Aw-Hassan A, Mouneime Y, Smriga M, Scrimshaw NS (2008) Impact of lysine-fortified wheat flour on morbidity and immunologic variables among members of rural families in northwest Syria. Food Nutr Bull 29:163–171CrossRefGoogle Scholar
  11. Gietzen D, Rogers Q (2006) Nutritional homeostasis and indispensable amino acid sensing: a new solution to an old puzzle. Trends Neurosci 29:91–99CrossRefGoogle Scholar
  12. Goto S, Nagao K, Bannai M, Takahashi M, Nakahara K, Kangawa K, Murakami N (2010) Anorexia in rats caused by a valine-deficient diet is not ameliorated by systemic ghrelin treatment. Neuroscience 166:333–340CrossRefGoogle Scholar
  13. Hao S et al (2005) Uncharged tRNA and sensing of amino acid deficiency in mammalian piriform cortex. Science 307:1776–1778CrossRefGoogle Scholar
  14. Holm L et al (2013) Determination of steady-state protein breakdown rate in vivo by the disappearance of protein-bound tracer-labeled amino acids: a method applicable in humans. Am J Physiol Endocrinol Metab 304:895–907CrossRefGoogle Scholar
  15. Hrupka BJ, Lin Y, Gietzen DW, Rogers QR (1999) Lysine deficiency alters diet selection without depressing food intake in rats. J Nutr 129:424–430CrossRefGoogle Scholar
  16. Huang L et al (2011) Lysine requirement of the enterally fed term infant in the first month of life. Am J Clin Nutr 94:1496–1503CrossRefGoogle Scholar
  17. Jackson AA, Phillips G, Mcclelland I, Jahoor F (2001) Synthesis of hepatic secretory proteins in normal adults consuming a diet marginally adequate in protein. Am J Physiol Gastrointest Liver Physiol 281:1179–1187CrossRefGoogle Scholar
  18. James WP, Hay AM (1968) Albumin metabolism: effect of the nutritional state and the dietary protein intake. J Clin Invest 47:1958–1972CrossRefGoogle Scholar
  19. Jeffay H, Winzler RJ (1958) The metabolism of serum proteins. II. The effect of dietary protein on the turnover of rat serum protein. J Biol Chem 231:111–116PubMedGoogle Scholar
  20. Khan L, Bamji M (1979) Tissue carnitine deficiency due to dietary lysine deficiency: triglyceride accumulation and concomitant impairment in fatty acid oxidation. J Nutr 109:24–31CrossRefGoogle Scholar
  21. Li P, Yin YL, Li D, Kim SW, Wu G (2007) Amino acids and immune function. Br J Nutr 98:237–252CrossRefGoogle Scholar
  22. Nagao K, Bannai M, Seki S, Kawai N, Mori M, Takahashi M (2010) Voluntary wheel running is beneficial to the amino acid profile of lysine-deficient rats. Am J Physiol Endocrinol Metab 298:1170–1178CrossRefGoogle Scholar
  23. Nielsen K, Nansen P (1967) Metabolism of bovine immunoglobulin II. Metabolism of bovine igg in cattle with secondary hypoimmunoglobulinemia. Can J Comp Med Vet Sci 31:106–110PubMedPubMedCentralGoogle Scholar
  24. Petro TM, Bhattacharjee JK (1980) Effect of dietary essential amino acid limitations upon native levels of murine serum immunoglobulins, transferrin, and complement. Infect Immun 27:513–518PubMedPubMedCentralGoogle Scholar
  25. Pillai RR, Elango R, Ball RO, Kurpad AV, Pencharz PB (2015) Lysine requirements of moderately undernourished school-aged indian children are reduced by treatment for intestinal parasites as measured by the indicator amino acid oxidation technique. J Nutr 145:954–959CrossRefGoogle Scholar
  26. Previs SF, Fatica R, Chandramouli V, Alexander JC, Brunengraber H, Landau BR (2004) Quantifying rates of protein synthesis in humans by use of 2H2O: application to patients with end-stage renal disease. Am J Physiol Endocrinol Metab 286:665–672CrossRefGoogle Scholar
  27. Reeves PG, Nielsen FH, Fahey GC (1993) AIN-93 purified diets for laboratory rodents: final report of the American Institute of Nutrition ad hoc writing committee on the reformulation of the AIN-76A rodent diet. J Nutr 123:1939–1951CrossRefGoogle Scholar
  28. Regmi N, Wang T, Crenshaw M, Rude BJ, Liao SF (2017) Effects of dietary lysine levels on the concentrations of selected nutrient metabolites in blood plasma of late-stage finishing pigs. J Anim Physiol Anim Nutr 102:1–12Google Scholar
  29. Schwert GW (1957) Recovery of native bovine serum albumin after precipitation with trichloroacetic acid and solution in organic solvents. J Am Chem Soc 79:139–141CrossRefGoogle Scholar
  30. Shimomura A et al (2014) Dietary l-lysine prevents arterial calcification in adenine-induced uremic rats. J Am Soc Nephrol 25:1954–1965CrossRefGoogle Scholar
  31. Smriga M, Kameishi M, Uneyama H, Torii K (2002) Dietary l-lysine deficiency increases stress-induced anxiety and fecal excretion in rats. J Nutr 132:3744–3746CrossRefGoogle Scholar
  32. Volpi E et al (1996) Contribution of amino acids and insulin to protein anabolism during meal absorption. Diabetes 45:1245–1252CrossRefGoogle Scholar
  33. Wada Y, Sato Y, Miyazakia K, Takedaa Y, Kuwahatac M (2017) The reduced/oxidized state of plasma albumin is modulated by dietary protein intake partly via albumin synthesis rate in rats. Nutr Res 37:46–57CrossRefGoogle Scholar
  34. Wei Z, Peebles E, Wang X, Gerard P, Olanrewaju H, Mercier Y (2016) Effects of dietary lysine and methionine supplementation on Ross 708 male broilers from 21 to 42 d of age (III): serum metabolites, hormones, and their relationship with growth performance. J Appl Poultry Res 25:223–231CrossRefGoogle Scholar
  35. Wen Z, Rasolofomanana T, Tang J, Jiang Y, Xie M, Yang P, Hou S (2017) Effects of dietary energy and lysine levels on growth performance and carcass yields of Pekin ducks from hatch to 21 days of age. Poult Sci 96:3361–3366CrossRefGoogle Scholar
  36. Wilson W, Roach P (2002) Nutrient-regulated protein kinases in budding yeast. Cell 111:155–158CrossRefGoogle Scholar
  37. Zhao W et al (2004) Lysine-fortified wheat flour improves the nutritional and immunological status of wheat-eating families in northern China. Food Nutr Bull 25:123–129CrossRefGoogle Scholar

Copyright information

© Springer-Verlag GmbH Austria, part of Springer Nature 2018

Authors and Affiliations

  1. 1.Department of Nutrition, School of Food Science and EngineeringYangzhou UniversityYangzhouChina
  2. 2.Department of Food Science and Engineering, School of Food Science and EngineeringYangzhou UniversityYangzhouChina
  3. 3.Jiangsu Provincial Key Laboratory of Dairy Biotechnology and Safety Control, School of Food Science and EngineeringYangzhou UniversityYangzhouChina

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