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BioMed Research International
Volume 2015, Article ID 815210, 8 pages
http://dx.doi.org/10.1155/2015/815210
Research Article

Quercetin Increases Hepatic Homocysteine Remethylation and Transsulfuration in Rats Fed a Methionine-Enriched Diet

1Tianjin Institute of Health and Environmental Medicine, Tianjin 300050, China
2Tianjin Key Laboratory for Prevention and Control of Occupational and Environmental Hazard, Tianjin 300309, China

Received 2 May 2015; Revised 24 August 2015; Accepted 1 September 2015

Academic Editor: Betti Giusti

Copyright © 2015 Bin Meng et al. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. Selhub, “Homocysteine metabolism,” Annual Review of Nutrition, vol. 19, pp. 217–246, 1999. View at Publisher · View at Google Scholar · View at Scopus
  2. J. D. Finkelstein, “Methionine metabolism in mammals,” The Journal of Nutritional Biochemistry, vol. 1, no. 5, pp. 228–237, 1990. View at Publisher · View at Google Scholar · View at Scopus
  3. J. D. Finkelstein, “The metabolism of homocysteine: pathways and regulation,” European Journal of Pediatrics, vol. 157, supplement 2, pp. S40–S44, 1998. View at Publisher · View at Google Scholar
  4. K. S. McCully, “Vascular pathology of homocysteinemia: implications for the pathogenesis of arteriosclerosis,” American Journal of Pathology, vol. 56, no. 1, pp. 111–128, 1969. View at Google Scholar · View at Scopus
  5. S. Seshadri, A. Beiser, J. Selhub et al., “Plasma homocysteine as a risk factor for dementia and Alzheimer's disease,” The New England Journal of Medicine, vol. 346, no. 7, pp. 476–483, 2002. View at Publisher · View at Google Scholar · View at Scopus
  6. E. C. Dinleyici, B. Kirel, O. Alatas, H. Muslumanoglu, Z. Kilic, and N. Dogruel, “Plasma total homocysteine levels in children with type 1 diabetes: relationship with vitamin status, methylene tetrahydrofolate reductase genotype, disease parameters and coronary risk factors,” Journal of Tropical Pediatrics, vol. 52, no. 4, pp. 260–266, 2006. View at Publisher · View at Google Scholar · View at Scopus
  7. L. Agoston-Coldea, T. Mocan, M. Gatfosse, S. Lupu, and D. L. Dumitrascu, “Plasma homocysteine and the severity of heart failure in patients with previous myocardial infarction,” Cardiology Journal, vol. 18, no. 1, pp. 55–62, 2011. View at Google Scholar · View at Scopus
  8. T. Szasz, K. Thakali, G. D. Fink, and S. W. Watts, “A comparison of arteries and veins in oxidative stress: producers, destroyers, function, and disease,” Experimental Biology and Medicine, vol. 232, no. 1, pp. 27–37, 2007. View at Google Scholar · View at Scopus
  9. N. Chen, Y. Liu, C. D. Greiner, and J. L. Holtzman, “Physiologic concentrations of homocysteine inhibit the human plasma GSH peroxidase that reduces organic hydroperoxides,” Journal of Laboratory and Clinical Medicine, vol. 136, no. 1, pp. 58–65, 2000. View at Publisher · View at Google Scholar · View at Scopus
  10. P. Yi, S. Melnyk, M. Pogribna, I. P. Pogribny, R. J. Hine, and S. J. James, “Increase in plasma homocysteine associated with parallel increases in plasma S-adenosylhomocysteine and lymphocyte DNA hypomethylation,” The Journal of Biological Chemistry, vol. 275, no. 38, pp. 29318–29323, 2000. View at Publisher · View at Google Scholar · View at Scopus
  11. A. J. Martí-Carvajal, I. Solà, D. Lathyris, D. E. Karakitsiou, and D. Simancas-Racines, “Homocysteine-lowering interventions for preventing cardiovascular events,” Cochrane Database of Systematic Reviews, vol. 1, Article ID CD006612, 2013. View at Google Scholar · View at Scopus
  12. Y. M. Smulders and H. J. Blom, “The homocysteine controversy,” Journal of Inherited Metabolic Disease, vol. 34, no. 1, pp. 93–99, 2011. View at Publisher · View at Google Scholar · View at Scopus
  13. W. M. Loke, J. M. Proudfoot, A. J. Mckinley et al., “Quercetin and its in vivo metabolites inhibit neutrophil-mediated low-density lipoprotein oxidation,” Journal of Agricultural and Food Chemistry, vol. 56, no. 10, pp. 3609–3615, 2008. View at Publisher · View at Google Scholar · View at Scopus
  14. U. Kukongviriyapan, K. Sompamit, P. Pannangpetch, V. Kukongviriyapan, and W. Donpunha, “Preventive and therapeutic effects of quercetin on lipopolysaccharide-induced oxidative stress and vascular dysfunction in mice,” Canadian Journal of Physiology and Pharmacology, vol. 90, no. 10, pp. 1345–1353, 2012. View at Publisher · View at Google Scholar · View at Scopus
  15. S. Mosawy, D. E. Jackson, O. L. Woodman, and M. D. Linden, “Treatment with quercetin and 3′,4′-dihydroxyflavonol inhibits platelet function and reduces thrombus formation in vivo,” Journal of Thrombosis and Thrombolysis, vol. 36, no. 1, pp. 50–57, 2013. View at Publisher · View at Google Scholar · View at Scopus
  16. B. Meng, W. Gao, J. Wei et al., “Quercetin reduces serum homocysteine level in rats fed a methionine-enriched diet,” Nutrition, vol. 29, no. 4, pp. 661–666, 2013. View at Publisher · View at Google Scholar · View at Scopus
  17. P. G. Reeves, F. H. Nielsen, and G. C. Fahey Jr., “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,” Journal of Nutrition, vol. 123, no. 11, pp. 1939–1951, 1993. View at Google Scholar · View at Scopus
  18. W. Velez-Carrasco, M. Merkel, C. O. Twiss, and J. D. Smith, “Dietary methionine effects on plasma homocysteine and HDL metabolism in mice,” Journal of Nutritional Biochemistry, vol. 19, no. 6, pp. 362–370, 2008. View at Publisher · View at Google Scholar · View at Scopus
  19. S. Toue, R. Kodama, M. Amao, Y. Kawamata, T. Kimura, and R. Sakai, “Screening of toxicity biomarkers for methionine excess in rats,” Journal of Nutrition, vol. 136, no. 6, supplement, pp. 1716s–1721s, 2006. View at Google Scholar · View at Scopus
  20. J. Krijt, M. Vacková, and V. Kožich, “Measurement of homocysteine and other aminothiols in plasma: advantages of using tris(2-carboxyethyl)phosphine as reductant compared with tri-n-butylphosphine,” Clinical Chemistry, vol. 47, no. 10, pp. 1821–1828, 2001. View at Google Scholar · View at Scopus
  21. Q. B. She, I. Nagao, T. Hayakawa, and H. Tsuge, “A simple HPLC method for the determination of S-adenosylmethionine and S-adenosylhomocysteine in rat tissues: the effect of vitamin B6 deficiency on these concentrations in rat liver,” Biochemical and Biophysical Research Communications, vol. 205, no. 3, pp. 1748–1754, 1994. View at Publisher · View at Google Scholar · View at Scopus
  22. J. T. Drummond, J. Jarrett, J. C. González, S. Huang, and R. G. Matthews, “Characterization of nonradioactive assays for cobalamin-dependent and cobalamin-independent methionine synthase enzymes,” Analytical Biochemistry, vol. 228, no. 2, pp. 323–329, 1995. View at Publisher · View at Google Scholar · View at Scopus
  23. M. Yagisawa, N. Shigematsu, and R. Nakata, “Effects of chronic betaine ingestion on methionine-loading induced plasma homocysteine elevation in rats,” Journal of Nutritional Science and Vitaminology, vol. 52, no. 3, pp. 194–199, 2006. View at Publisher · View at Google Scholar · View at Scopus
  24. C. G. Zou and R. Banerjee, “Tumor necrosis factor-α-induced targeted proteolysis of cystathionine β-synthase modulates redox homeostasis,” The Journal of Biological Chemistry, vol. 278, no. 19, pp. 16802–16808, 2003. View at Publisher · View at Google Scholar · View at Scopus
  25. E. Bravo, S. Palleschi, P. Aspichueta et al., “High fat diet-induced non alcoholic fatty liver disease in rats is associated with hyperhomocysteinemia caused by down regulation of the transsulphuration pathway,” Lipids in Health and Disease, vol. 10, article 60, 2011. View at Publisher · View at Google Scholar · View at Scopus
  26. J. D. Finkelstein and J. J. Martin, “Methionine metabolism in mammals. Adaptation to methionine excess,” The Journal of Biological Chemistry, vol. 261, no. 4, pp. 1582–1587, 1986. View at Google Scholar · View at Scopus
  27. B. A. Graf, C. Ameho, G. G. Dolnikowski, P. E. Milbury, C. Y. Chen, and J. B. Blumberg, “Rat gastrointestinal tissues metabolize quercetin,” Journal of Nutrition, vol. 136, no. 1, pp. 39–44, 2006. View at Google Scholar · View at Scopus
  28. R. Cermak, S. Landgraf, and S. Wolffram, “The bioavailability of quercetin in pigs depends on the glycoside moiety and on dietary factors,” Journal of Nutrition, vol. 133, no. 9, pp. 2802–2807, 2003. View at Google Scholar · View at Scopus
  29. N. C. Chen, F. Yang, L. M. Capecci et al., “Regulation of homocysteine metabolism and methylation in human and mouse tissues,” The FASEB Journal, vol. 24, no. 8, pp. 2804–2817, 2010. View at Publisher · View at Google Scholar · View at Scopus
  30. Y. I. Kim, “Folate and DNA methylation: a mechanistic link between folate deficiency and colorectal cancer?” Cancer Epidemiology, Biomarkers & Prevention, vol. 13, no. 4, pp. 511–519, 2004. View at Google Scholar · View at Scopus
  31. J. Tao, M. Yang, Z. Chen et al., “Decreased DNA methyltransferase 3A and 3B mRNA expression in peripheral blood mononuclear cells and increased plasma SAH concentration in adult patients with idiopathic thrombocytopenic purpura,” Journal of Clinical Immunology, vol. 28, no. 5, pp. 432–439, 2008. View at Publisher · View at Google Scholar · View at Scopus
  32. M. S. Jamaluddin, I. Chen, F. Yang et al., “Homocysteine inhibits endothelial cell growth via DNA hypomethylation of the cyclin A gene,” Blood, vol. 110, no. 10, pp. 3648–3655, 2007. View at Publisher · View at Google Scholar · View at Scopus
  33. C. Kutzbach and E. L. R. Stokstad, “Mammalian methylenetetrahydrofolate reductase. Partial purification, properties, and inhibition by S-adenosylmethionine,” Biochimica et Biophysica Acta, vol. 250, no. 3, pp. 459–477, 1971. View at Publisher · View at Google Scholar · View at Scopus
  34. J. D. Finkelstein and J. J. Martin, “Inactivation of betaine-homocysteine methyltransferase by adenosylmethionine and adenosylethionine,” Biochemical and Biophysical Research Communications, vol. 118, no. 1, pp. 14–19, 1984. View at Publisher · View at Google Scholar · View at Scopus
  35. M. Di Buono, L. J. Wykes, D. E. C. Cole, R. O. Ball, and P. B. Pencharz, “Regulation of sulfur amino acid metabolism in men in response to changes in sulfur amino acid intakes,” Journal of Nutrition, vol. 133, no. 3, pp. 733–739, 2003. View at Google Scholar · View at Scopus
  36. K. T. Williams and K. L. Schalinske, “New insights into the regulation of methyl group and homocysteine metabolism,” Journal of Nutrition, vol. 137, no. 2, pp. 311–314, 2007. View at Google Scholar · View at Scopus
  37. Y. C. Wang, Y. M. Chen, Y. J. Lin, S. P. Liu, and E. P. I. Chiang, “GNMT expression increases hepatic folate contents and folate-dependent methionine synthase-mediated homocysteine remethylation,” Molecular Medicine, vol. 17, no. 5-6, pp. 486–494, 2011. View at Publisher · View at Google Scholar · View at Scopus
  38. S. H. Mudd, R. Cerone, M. C. Schiaffino et al., “Glycine N-methyltransferase deficiency: a novel inborn error causing persistent isolated hypermethioninaemia,” Journal of Inherited Metabolic Disease, vol. 24, no. 4, pp. 448–464, 2001. View at Publisher · View at Google Scholar · View at Scopus
  39. A. L. Pey, T. Majtan, J. M. Sanchez-Ruiz, and J. P. Kraus, “Human cystathionine β-synthase (CBS) contains two classes of binding sites for S-adenosylmethionine (SAM): complex regulation of CBS activity and stability by SAM,” Biochemical Journal, vol. 449, no. 1, pp. 109–121, 2013. View at Publisher · View at Google Scholar · View at Scopus
  40. K. J. Meyers, J. L. Rudolf, and A. E. Mitchell, “Influence of dietary quercetin on glutathione redox status in mice,” Journal of Agricultural and Food Chemistry, vol. 56, no. 3, pp. 830–836, 2008. View at Publisher · View at Google Scholar · View at Scopus
  41. A. W. Boots, N. Kubben, G. R. M. M. Haenen, and A. Bast, “Oxidized quercetin reacts with thiols rather than with ascorbate: implication for quercetin supplementation,” Biochemical and Biophysical Research Communications, vol. 308, no. 3, pp. 560–565, 2003. View at Publisher · View at Google Scholar · View at Scopus
  42. A. W. Boots, H. Li, R. P. F. Schins et al., “The quercetin paradox,” Toxicology and Applied Pharmacology, vol. 222, no. 1, pp. 89–96, 2007. View at Publisher · View at Google Scholar · View at Scopus
  43. R. Banerjee, R. Evande, Ö. Kabil, S. Ojha, and S. Taoka, “Reaction mechanism and regulation of cystathionine β-synthase,” Biochimica et Biophysica Acta, vol. 1647, no. 1-2, pp. 30–35, 2003. View at Publisher · View at Google Scholar · View at Scopus
  44. P. Verhoef, T. van Vliet, M. R. Olthof, and M. B. Katan, “A high-protein diet increases postprandial but not fasting plasma total homocysteine concentrations: a dietary controlled, crossover trial in healthy volunteers,” American Journal of Clinical Nutrition, vol. 82, no. 3, pp. 553–558, 2005. View at Google Scholar · View at Scopus