Effects of Oxidative Stress Induced by Diquat on Arginine Metabolism of Postweaning Pigs

  • Zheng, Ping (Institute of Animal Nutrition, Sichuan Agricultural University) ;
  • Yu, Bing (Institute of Animal Nutrition, Sichuan Agricultural University) ;
  • Lv, Mei (Institute of Animal Nutrition, Sichuan Agricultural University) ;
  • Chen, Daiwen (Institute of Animal Nutrition, Sichuan Agricultural University)
  • Received : 2009.05.05
  • Accepted : 2009.07.09
  • Published : 2010.01.01


A total of 16 crossbred post-weaning pigs (10.64${\pm}$0.27 kg BW) were individually penned and assigned to one of two treatments to investigate the influences of diquat-induced oxidative stress on performance and arginine metabolism. Pigs in the oxidative stress group were injected intra-peritoneally with 10 mg/kg BW of diquat, while the control group were injected with isotonic saline. All pigs were fed ad libitum. The experiment lasted for 7 days. The results indicated that compared with control treatment, oxidative stress induced by diquat significantly decreased average daily gain, intake and feed conversion. The treatment decreased activities of antioxidant enzymes, increased concentration of malondialdehyde in plasma, increased cationic amino acid transporter-1 mRNA level and activity of ornithine aminotransferase and concentrations of arginine and citrulline in the jejunum, decreased the concentrations of arginine in plasma and kidney, and decreased induced nitric oxide synthase mRNA level. It is concluded that oxidative stress induced by diquat can influence absorption and metabolism of arginine and consequently modify the requirement of arginine for post-weaning pigs.


  1. Jang, H. Y., H. S. Kong, J. D. Oh, B. K. Park, B. K. Yang, G. J. Jeon and H. K. Lee. 2008. Maintenance of sperm characteristics and in vitro developmental rate of embryos against oxidative stress through antioxidants in pig. Asian-Aust. J. Anim. Sci. 21(3):340-345
  2. Inoue, Y., B. P. Bode and W. W. Souba. 1994. Hepatic Na$^{+}$-independent amino acid transport in endotoxemia rats: evidence for selective stimulation of arginine transport. Shock 2:164-170
  3. Loscalzo, J. 2004. L-Arginine and atherothrombosis. J. Nutr. 134(10):2798S-2800S
  4. Nappi, A. J. and E. Vass. 1998. Hydroxyl radical formation via iron-mediated fenton chemistry is inhibited by methylated catechols. Biochim. Biophys. Acta. 1425(1):159-167
  5. Wu, G., F. W. Bazer, J. B. Hu, G. A. Johnson and T. E. Spencer. 2005. Polyamine synthesis from proline in the developing porcine placenta. Biol. Report 72:842-850
  6. Rafferty, J. F., Y. Noguchi, J .E. Fischer and P. O. Hasselgren. 1994. Sepsis in rats stimulates cellular proliferation in the mucosa of the small intestine. Gastroenterology 107:121-127
  7. Wu, G., P. K. Davis, N. E. Flynn, D. A. Knabe and J. T. Davidson. 1997. Endogenous synthesis of arginine plays an important role in maintaining arginine homeostasis in postweaning growing pigs. J. Nutr. 127(12):2342-2349
  8. Wu, G. 1998. Intestinal mucosal amino acid catabolism. J. Nutr. 128:1249-1252
  9. Pan, M., H. A. Choudry, M. J. Epler, Q. H. Meng, A. Karinch, C. M. Lin and W. Souba. 2004 Arginine transport in catabolic disease states. J. Nutr. 134:2826S-2829S
  10. Aulak, K. S., R. Mishra, L. Zhou, S. L. Hyatt, W. Jonge, W. Lamers, M. Snider and M. Hatzoglou. 1999. Posttranscriptional regulation of the arginine transporter Cat-1 by amino acid availability. J. Biol. Chem. 274:30424-30432
  11. Closs, E. I., A. Simon, N. Vekony and A. Rotmann. 2004. Plasma membrane transporters for arginine. J. Nutr. 134:2752s-2759s
  12. Liang, H. Y., H. V. Remmen, V. Frohlich, J. Lechleiter, A. Richardson and Q. T. Ran. 2007. Gpx4 protects mitochondrial ATP generation against oxidative damage. Biochem. Biophys. Res. Commun. 356:893-898
  13. Wu, G. and S. M. Morris Jr. 1998. Arginine metabolism: nitric oxide and beyond. Biochem. J. 336:1-17
  14. Dillon, E. L., D. A. Knabe and G. Wu. 1999. Lactate inhibits citrulline and arginine synthesis from proline in pig enterocytes. Am. J. Physiol. Gastrointest. Liver Physiol. 276:1079-1086
  15. Knight, S. A. B. and R. A. Sunde. 1987. The effect of progressive selenium deficiency on anti-glutathione peroxidase antibody reactive protein in rat liver. J. Nutr. 117:732-738
  16. Pacitti, A. J., E. M. Copeland and W. W. Souba. 1992. Stimulation of hepatocyte System y (+)-mediated L-arginine transport by an inflammatory agent. Surgery 112:403-411
  17. Luiking, Y. C., M. M. Hallemeesch, Y. L. Vissers, W. H. Lamers and N. E. Deutz. 2004. In vivo whole body and organ arginine metabolism during endotoxemia (sepsis) is dependent on mouse strain and gender J. Nutr. 134:2768S-2774S
  18. Inoue, Y. and W. W. Souba. 1993. Cyclooxygenase blockage abrogates hepatic arginine uptake in endotoxemic rats. Surg. Forum 44:7-10
  19. White, M. F. 1985. The transport of cationic amino acids across the plasma membrane of mammalian cells. Biochem. Biophys. Acta. 822:355-374
  20. Pfaffl, M. W. 2001. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29:2002-2007
  21. Yang, Z. H. and X. F. Ming. 2006. Recent advances in understudy endothelial dysfunction in atherosclerosis. Clin. Med. Res. 4(1):53-65
  22. Pan, M., A. M. Karinch, C. M. Lin and W. W. Souba. 2001. Interferon-$\gamma$ stimulates arginine transport in intestinal epithelium. Surg. Forum 52:159-162
  23. Crespo, E., M. Macias, D. Pozo, G. Escames, M. Martín, F. Vives, J. M. Guerrero and D. Acuna-Castroviejo. 1999. Melatonin inhibits expression of the inducible no synthase ii in liver and lung and prevents endotoxemia in lipopolysaccharide-induced multiple organ dysfunction syndrome in rats. FASEB J. 13:1537-1546
  24. Wang, T., A. M. Lawler, G. Steel, I. Sipila, A. H. Milam and D. Valle. 1995. Mice lacking ornithine-delta-aminotransferase have paradoxical neonatal hypoornithinaemia and retinal degeneration. Nat. Genet. 11(2):185-190
  25. Fu, Y., W. H. Cheng, J. M. Porres, D. A. Ross and X. G. Lei. 1999. Knockout of cellular glutathione peroxidase gene renders mice susceptible to diquat-induced oxidative stress. Free Radic. Biol. Med. 27:605-611
  26. Wu, G. 1997. Synthesis of citrulline and arginine from proline in enterocytes of postnatal pigs. Am. J. Physiol. Gastrointest. Liver Physiol. 272:G1382-G1390
  27. Fernandez, J., A. B. Lopez, C. Wang, R. Mishra, L. Zhou, I. Yaman, M. D. Snider and M. Hatzolgou. 2003. Transcriptional control of the arginine/lysine transporter, cat-1, by physiological stress. J. Biol. Chem. 278:50000-50009
  28. Spalding, D. J., J. R. Mitchell, H. Jaeschke and C. V. Smith. 1989. Diquat hepatotoxicity in the Fischer-344 rat: the role of covalent binding to tissue proteins and lipids. Toxicol. Appl. Pharmacol. 101(2):319-327
  29. Peled-Kamar, M., J. Lotem, I. Wirguin, L. Weiner, A. Hermalin and Y. Groner. 1997. Oxidative stress mediates impairment of muscle function in transgenic mice with elevated level of wildtype Cu/Zn superoxide dismutase. Proc. Natl. Acad. Sci. 94:3883-3887
  30. Wu, G. and C. J. Meininger. 2008. Analysis of citrulline, arginine, and methylarginines using high-performance liquid chromatography. Meth. Enzymol. 440:177-189
  31. El-Gayar, S., H. Thuring-Nahler, J. Pfeilschifter, M. Rollinghoff and C. Bogdan. 2003. Translational control of inducible nitric oxide synthase by IL-13 and arginine availability in inflammatory macrophages. J. Immunol. 171:4561-4568
  32. Yuan, S. B., D. W. Chen, K. Y. Zhang and B. Yu. 2007. Effects of oxidative stress on growth performance, nutrient digestibilities and activities of antioxidative enzymes of weanling pigs. Asian-Aust. J. Anim. Sci. 20(10):1600-1605

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