Table of Contents Author Guidelines Submit a Manuscript
Oxidative Medicine and Cellular Longevity
Volume 2017, Article ID 1716701, 8 pages
https://doi.org/10.1155/2017/1716701
Review Article

Multifarious Beneficial Effect of Nonessential Amino Acid, Glycine: A Review

1Department of Biochemistry, Rayalaseema University, Kurnool 518002, India
2Department of Zoology, K.V.R. Govt College for Women, Kurnool 518002, India
3Department of Bionanotechnology, Gachon University, San 65, Bokjeong Dong, Sujeong Gu, Seongnam Si, Gyeonggi Do 461 701, Republic of Korea

Correspondence should be addressed to Senthilkumar Rajagopal; moc.oohay@lanalihtnes

Received 3 November 2016; Revised 7 February 2017; Accepted 7 February 2017; Published 1 March 2017

Academic Editor: Musthafa Mohamed Essa

Copyright © 2017 Meerza Abdul Razak 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. W. Wang, Z. Wu, Z. Dai, Y. Yang, J. Wang, and G. Wu, “Glycine metabolism in animals and humans: implications for nutrition and health,” Amino Acids, vol. 45, no. 3, pp. 463–477, 2013. View at Publisher · View at Google Scholar · View at Scopus
  2. G. Wu, Z. Wu, Z. Dai et al., “Dietary requirements of 'nutritionally non-essential amino acids' by animals and humans,” Amino Acids, vol. 44, no. 4, pp. 1107–1113, 2013. View at Publisher · View at Google Scholar · View at Scopus
  3. G. Wu, “Functional amino acids in growth, reproduction, and health,” Advances in Nutrition, vol. 1, no. 1, pp. 31–37, 2010. View at Publisher · View at Google Scholar · View at Scopus
  4. R. M. Lewis, K. M. Godfrey, A. A. Jackson, I. T. Cameron, and M. A. Hanson, “Low serine hydroxymethyltransferase activity in the human placenta has important implications for fetal glycine supply,” The Journal of Clinical Endocrinology and Metabolism, vol. 90, no. 3, pp. 1594–1598, 2005. View at Publisher · View at Google Scholar · View at Scopus
  5. B. X. Yan and Y. Sun Qing, “Glycine residues provide flexibility for enzyme active sites,” Journal of Biological Chemistry, vol. 272, no. 6, pp. 3190–3194, 1997. View at Publisher · View at Google Scholar · View at Scopus
  6. S. Rajendra, J. W. Lynch, and P. R. Schofield, “The glycine receptor,” Pharmacology and Therapeutics, vol. 73, no. 2, pp. 121–146, 1997. View at Publisher · View at Google Scholar · View at Scopus
  7. Z. Zhong, M. D. Wheeler, X. Li et al., “L-glycine: a novel antiinflammatory, immunomodulatory, and cytoprotective agent,” Current Opinion in Clinical Nutrition and Metabolic Care, vol. 6, no. 2, pp. 229–240, 2003. View at Publisher · View at Google Scholar · View at Scopus
  8. O. Ballevre, A. Cadenhead, A. G. Calder et al., “Quantitative partition of threonine oxidation in pigs, effect of dietary threonine,” Americian Journal of Physiology—Endocrinology and Metabolism, vol. 25, no. 4, pp. E483–E491, 1990. View at Google Scholar
  9. G. Wu, F. W. Bazer, R. C. Burghardt et al., “Proline and hydroxyproline metabolism: implications for animal and human nutrition,” Amino Acids, vol. 40, no. 4, pp. 1053–1063, 2011. View at Publisher · View at Google Scholar · View at Scopus
  10. E. Meléndez-Hevia, P. De Paz-Lugo, A. Cornish-Bowden, and M. L. Cárdenas, “A weak link in metabolism: the metabolic capacity for glycine biosynthesis does not satisfy the need for collagen synthesis,” Journal of Biosciences, vol. 34, no. 6, pp. 853–872, 2009. View at Publisher · View at Google Scholar · View at Scopus
  11. J. Zhang, J. K. Blustzjn, and S. H. Zeisel, “Measurement of the formation of betaine aldehyde and betaine in rat liver mitochondria by a high pressure liquid chromatography-radioenzymatic assay,” BBA—General Subjects, vol. 1117, no. 3, pp. 333–339, 1992. View at Publisher · View at Google Scholar · View at Scopus
  12. E.-J. Yeo and C. Wagner, “Tissue distribution of glycine N-methyltransferase, a major folate-binding protein of liver,” Proceedings of the National Academy of Sciences of the United States of America, vol. 91, no. 1, pp. 210–214, 1994. View at Publisher · View at Google Scholar · View at Scopus
  13. H. Ogawa, T. Gomi, and M. Fujioka, “Serine hydroxymethyltransferase and threonine aldolase: are they identical?” International Journal of Biochemistry and Cell Biology, vol. 32, no. 3, pp. 289–301, 2000. View at Publisher · View at Google Scholar · View at Scopus
  14. J. D. House, B. N. Hall, and J. T. Brosnan, “Threonine metabolism in isolated rat hepatocytes,” American Journal of Physiology - Endocrinology and Metabolism, vol. 281, no. 6, pp. E1300–E1307, 2001. View at Google Scholar · View at Scopus
  15. V. A. Hammer, Q. R. Rogers, and R. A. Freedland, “Threonine is catabolized by L-threonine 3-dehydrogenase and threonine dehydratase in hepatocytes from domestic cats (Felis domestica),” Journal of Nutrition, vol. 126, no. 9, pp. 2218–2226, 1996. View at Google Scholar · View at Scopus
  16. P. B. Darling, J. Grunow, M. Rafii, S. Brookes, R. O. Ball, and P. B. Pencharz, “Threonine dehydrogenase is a minor degradative pathway of threonine catabolism in adult humans,” American Journal of Physiology - Endocrinology and Metabolism, vol. 278, no. 5, pp. E877–E884, 2000. View at Google Scholar · View at Scopus
  17. P. S. Parimi, L. L. Gruca, and S. C. Kalhan, “Metabolism of threonine in newborn infants,” American Journal of Physiology—Endocrinology and Metabolism, vol. 289, no. 6, pp. E981–E985, 2005. View at Publisher · View at Google Scholar · View at Scopus
  18. N. Le Floc'h, C. Obled, and B. Seve, “In vivo threonine oxidation rate is dependent on threonine dietary supply in growing pigs fed low to adequate levels,” Journal of Nutrition, vol. 125, no. 10, pp. 2550–2562, 1995. View at Google Scholar · View at Scopus
  19. S. Girgis, I. M. Nasrallah, J. R. Suh et al., “Molecular cloning, characterization and alternative splicing of the human cytoplasmic serine hydroxymethyltransferase gene,” Gene, vol. 210, no. 2, pp. 315–324, 1998. View at Publisher · View at Google Scholar · View at Scopus
  20. P. J. Stover, L. H. Chen, J. R. Suh, D. M. Stover, K. Keyomarsi, and B. Shane, “Molecular cloning, characterization, and regulation of the human mitochondrial serine hydroxymethyltransferase gene,” Journal of Biological Chemistry, vol. 272, no. 3, pp. 1842–1848, 1997. View at Publisher · View at Google Scholar · View at Scopus
  21. M. R. Narkewicz, P. J. Thureen, S. D. Sauls, S. Tjoa, N. Nikolayevsky, and P. V. Fennessey, “Serine and glycine metabolism in hepatocytes from mid gestation fetal lambs,” Pediatric Research, vol. 39, no. 6, pp. 1085–1090, 1996. View at Publisher · View at Google Scholar · View at Scopus
  22. A. J. MacFarlane, X. Liu, C. A. Perry et al., “Cytoplasmic serine hydroxymethyltransferase regulates the metabolic partitioning of methylenetetrahydrofolate but is not essential in mice,” Journal of Biological Chemistry, vol. 283, no. 38, pp. 25846–25853, 2008. View at Publisher · View at Google Scholar · View at Scopus
  23. J. Wang, Z. Wu, D. Li et al., “Nutrition, epigenetics, and metabolic syndrome,” Antioxidants and Redox Signaling, vol. 17, no. 2, pp. 282–301, 2012. View at Publisher · View at Google Scholar · View at Scopus
  24. Z.-L. Dai, J. Zhang, G. Wu, and W.-Y. Zhu, “Utilization of amino acids by bacteria from the pig small intestine,” Amino Acids, vol. 39, no. 5, pp. 1201–1215, 2010. View at Publisher · View at Google Scholar · View at Scopus
  25. Z.-L. Dai, G. Wu, and W.-Y. Zhu, “Amino acid metabolism in intestinal bacteria: links between gut ecology and host health,” Frontiers in Bioscience, vol. 16, pp. 1768–1786, 2011. View at Publisher · View at Google Scholar · View at Scopus
  26. Z.-L. Dai, X.-L. Li, P.-B. Xi, J. Zhang, G. Wu, and W.-Y. Zhu, “Metabolism of select amino acids in bacteria from the pig small intestine,” Amino Acids, vol. 42, no. 5, pp. 1597–1608, 2012. View at Publisher · View at Google Scholar · View at Scopus
  27. P. J. Thureen, M. R. Narkewicz, F. C. Battaglia, S. Tjoa, and P. V. Fennessey, “Pathways of serine and glycine metabolism in primary culture of ovine fetal hepatocytes,” Pediatric Research, vol. 38, no. 5, pp. 775–782, 1995. View at Publisher · View at Google Scholar · View at Scopus
  28. Y. Lamers, J. Williamson, L. R. Gilbert, P. W. Stacpoole, and J. F. Gregory III, “Glycine turnover and decarboxylation rate quantified in healthy men and women using primed, constant infusions of [1,2-(13)C2]glycine and [(2)H3]leucine,” Journal of Nutrition, vol. 137, no. 12, pp. 2647–2652, 2007. View at Google Scholar · View at Scopus
  29. S. Shoham, D. C. Javitt, and U. Heresco-Levy, “Chronic high-dose glycine nutrition: effects on rat brain cell morphology,” Biological Psychiatry, vol. 49, no. 10, pp. 876–885, 2001. View at Publisher · View at Google Scholar · View at Scopus
  30. G. Kikuchi, Y. Motokawa, T. Yoshida et al., “Glycine cleavage system, reaction mechanism, physiological significance, and hyperglycinemia,” Proceedings of the Japan Academy, Series B, vol. 84, no. 7, pp. 246–263, 2008. View at Publisher · View at Google Scholar
  31. I. Dos Santos Fagundes, L. N. Rotta, I. D. Schweigert et al., “Glycine, serine, and leucine metabolism in different regions of rat central nervous system,” Neurochemical Research, vol. 26, no. 3, pp. 245–249, 2001. View at Publisher · View at Google Scholar · View at Scopus
  32. N. Kawai, N. Sakai, M. Okuro et al., “The sleep-promoting and hypothermic effects of glycine are mediated by NMDA receptors in the suprachiasmatic nucleus,” Neuropsychopharmacology, vol. 40, no. 6, pp. 1405–1416, 2015. View at Publisher · View at Google Scholar · View at Scopus
  33. C. Conter, M. O. Rolland, D. Cheillan, V. Bonnet, I. Maire, and R. Froissart, “Genetic heterogeneity of the GLDC gene in 28 unrelated patients with glycine encephalopathy,” Journal of Inherited Metabolic Disease, vol. 29, no. 1, pp. 135–142, 2006. View at Publisher · View at Google Scholar · View at Scopus
  34. S. Dasarathy, T. Kasumov, J. M. Edmison et al., “Glycine and urea kinetics in nonalcoholic steatohepatitis in human: effect of intralipid infusion,” American Journal of Physiology—Gastrointestinal and Liver Physiology, vol. 297, no. 3, pp. G567–G575, 2009. View at Publisher · View at Google Scholar · View at Scopus
  35. R. Senthilkumar and N. Nalini, “Glycine modulates lipids and lipoproteins levels in rats with alcohol induced liver injury,” Internet Journal of Pharmacology, vol. 2, no. 2, 2004. View at Google Scholar
  36. R. Senthilkumar, P. Viswanathan, and N. Nalini, “Glycine modulates hepatic lipid accumulation in alcohol-induced liver injury,” Polish Journal of Pharmacology, vol. 55, no. 4, pp. 603–611, 2003. View at Publisher · View at Google Scholar · View at Scopus
  37. R. Senthilkumar and N. Nalini, “Effect of glycine on tissue fatty acid composition in an experimental model of alcohol-induced hepatotoxicity,” Clinical and Experimental Pharmacology and Physiology, vol. 31, no. 7, pp. 456–461, 2004. View at Publisher · View at Google Scholar · View at Scopus
  38. A. Zeb and S. U. Rahman, “Protective effects of dietary glycine and glutamic acid toward the toxic effects of oxidized mustard oil in rabbits,” Food Funct., vol. 8, no. 1, pp. 429–436, 2017. View at Publisher · View at Google Scholar
  39. R. Senthilkumar, M. Sengottuvelan, and N. Nalini, “Protective effect of glycine supplementation on the levels of lipid peroxidation and antioxidant enzymes in the erythrocyte of rats with alcohol-induced liver injury,” Cell Biochemistry and Function, vol. 22, no. 2, pp. 123–128, 2004. View at Publisher · View at Google Scholar · View at Scopus
  40. M. Deters, O. Strubelt, and M. Younes, “Protection by glycine against hypoxia-reoxygenation induced hepatic injury,” Research Communications in Molecular Pathology and Pharmacology, vol. 97, no. 2, pp. 199–213, 1997. View at Google Scholar · View at Scopus
  41. R. F. Stachlewitz, V. Seabra, B. Bradford et al., “Glycine and uridine prevent d-galactosamine hepatotoxicity in the rat: role of Kupffer cells,” Hepatology, vol. 29, no. 3, pp. 737–745, 1999. View at Publisher · View at Google Scholar · View at Scopus
  42. R. G. Thurman, Z. Zhong, M. Von Frankenberg, R. F. Stachlewitz, and H. Bunzendahl, “Prevention of cyclosporine-induced nephrotoxicity with dietary glycine,” Transplantation, vol. 63, no. 11, pp. 1661–1667, 1997. View at Publisher · View at Google Scholar · View at Scopus
  43. K. Ikejima, Y. Iimuro, D. T. Forman, and R. G. Thurman, “A diet containing glycine improves survival in endotoxin shock in the rat,” American Journal of Physiology - Gastrointestinal and Liver Physiology, vol. 271, no. 1, pp. G97–G103, 1996. View at Google Scholar · View at Scopus
  44. G. Ruknuddin, R. Basavaiah, P. Biswajyoti, A. Krishnaiah, and P. Kumar, “Anti-inflammatory and analgesic activities of Dashanga Ghana: an ayurvedic compound formulation,” International Journal of Nutrition, Pharmacology, Neurological Diseases, vol. 3, no. 3, pp. 303–308, 2013. View at Publisher · View at Google Scholar
  45. Z. Zhong, S. Jones, and R. G. Thurman, “Glycine minimizes reperfusion injury in a low-flow, reflow liver perfusion model in the rat,” American Journal of Physiology—Gastrointestinal and Liver Physiology, vol. 270, no. 2, pp. G332–G338, 1996. View at Google Scholar · View at Scopus
  46. T. Jacob, E. Ascher, A. Hingorani, and S. Kallakuri, “Glycine prevents the induction of apoptosis attributed to mesenteric ischemia/reperfusion injury in a rat model,” Surgery, vol. 134, no. 3, pp. 457–466, 2003. View at Publisher · View at Google Scholar · View at Scopus
  47. M. A. Lee, R. D. McCauley, S.-E. Kong, and J. C. Hall, “Influence of glycine on intestinal ischemia-reperfusion injury,” Journal of Parenteral and Enteral Nutrition, vol. 26, no. 2, pp. 130–135, 2002. View at Publisher · View at Google Scholar · View at Scopus
  48. G. R. Christie, D. Ford, A. Howard, M. A. Clark, and B. H. Hirst, “Glycine supply to human enterocytes mediated by high-affinity basolateral GLYT1,” Gastroenterology, vol. 120, no. 2, pp. 439–448, 2001. View at Publisher · View at Google Scholar · View at Scopus
  49. A. Howard, I. Tahir, S. Javed, S. M. Waring, D. Ford, and B. H. Hirst, “Glycine transporter GLYT1 is essential for glycine-mediated protection of human intestinal epithelial cells against oxidative damage,” Journal of Physiology, vol. 588, no. 6, pp. 995–1009, 2010. View at Publisher · View at Google Scholar · View at Scopus
  50. I. Tsune, K. Ikejima, M. Hirose et al., “Dietary glycine prevents chemical-induced experimental colitis in the rat,” Gastroenterology, vol. 125, no. 3, pp. 775–785, 2003. View at Publisher · View at Google Scholar · View at Scopus
  51. M. K. Schilling, G. Den Butter, A. Saunder, S. Lindell, F. O. Belzer, and J. H. Southard, “Membrane stabilizing effects of glycine during kidney cold storage and reperfusion,” Transplantation Proceedings, vol. 23, no. 5, pp. 2387–2389, 1991. View at Google Scholar · View at Scopus
  52. M. Yin, R. T. Currin, X.-X. Peng, H. E. Mekeel, R. Schoonhoven, and J. J. Lemasters, “Carolina rinse solution minimizes kidney injury and improves graft function and survival after prolonged cold ischemia,” Transplantation, vol. 73, no. 9, pp. 1410–1420, 2002. View at Publisher · View at Google Scholar · View at Scopus
  53. S. Bachmann, X.-X. Peng, R. T. Currin, R. G. Thurman, and J. J. Lemasters, “Glycine in Carolina rinse solution reduces reperfusion injury, improves graft function, and increases graft survival after rat liver transplantation,” Transplantation Proceedings, vol. 27, no. 1, pp. 741–742, 1995. View at Google Scholar · View at Scopus
  54. G. Den Butter, S. L. Lindell, R. Sumimoto, M. K. Schilling, J. H. Southard, and F. O. Belzer, “Effect of glycine in dog and rat liver transplantation,” Transplantation, vol. 56, no. 4, pp. 817–822, 1993. View at Publisher · View at Google Scholar · View at Scopus
  55. G. Montanari, L. Z. Lakshtanov, D. J. Tobler et al., “Effect of aspartic acid and glycine on calcite growth,” Crystal Growth & Design, vol. 16, no. 9, pp. 4813–4821, 2016. View at Publisher · View at Google Scholar
  56. P. Schemmer, N. Enomoto, B. U. Bradford et al., “Activated Kupffer cells cause a hypermetabolic state after gentle in situ manipulation of liver in rats,” American Journal Physiology Gastrointestinal Liver Physiology, vol. 280, no. 2, pp. G1076–G1082, 2001. View at Google Scholar
  57. J. E. Mangino, B. Kotadia, and M. J. Mangino, “Characterization of hypothermic intestinal ischemia-reperfusion injury in dogs: effects of glycine,” Transplantation, vol. 62, no. 2, pp. 173–178, 1996. View at Publisher · View at Google Scholar · View at Scopus
  58. P. Jain, N. K. Khanna, and J. L. Godhwani, “Modification of immune response by glycine in animals,” Indian Journal of Experimental Biology, vol. 27, no. 3, pp. 292–293, 1989. View at Google Scholar
  59. H. Bunzendahl, M. Yin, R. F. Stachlewitz et al., “Dietary glycine prolongs graft survival in transplant models,” Shock, vol. 13, no. 2, pp. 163–164, 2000. View at Google Scholar
  60. S. L. Nyberg, J. A. Hardin, L. E. Matos, D. J. Rivera, S. P. Misra, and G. J. Gores, “Cytoprotective influence of ZVAD-fmk and glycine on gel-entrapped rat hepatocytes in a bioartificial liver,” Surgery, vol. 127, no. 4, pp. 447–455, 2000. View at Publisher · View at Google Scholar · View at Scopus
  61. P. A. Abello, T. G. Buchman, and G. B. Bulkley, “Shock and multiple organ failure,” Advances of Experimental Medicine and Biology, vol. 366, no. 2, pp. 253–268, 1994. View at Publisher · View at Google Scholar
  62. J. L. Mauriz, B. Matilla, J. M. Culebras, P. González, and J. González-Gallego, “Dietary glycine inhibits activation of nuclear factor kappa B and prevents liver injury in hemorrhagic shock in the rat,” Free Radical Biology and Medicine, vol. 31, no. 10, pp. 1236–1244, 2001. View at Publisher · View at Google Scholar · View at Scopus
  63. M. R. W. Grotz, H.-C. Pape, M. van Griensven et al., “Glycine reduces the inflammatory response and organ damage in a two-hit sepsis model in rats,” Shock, vol. 16, no. 2, pp. 116–121, 2001. View at Publisher · View at Google Scholar · View at Scopus
  64. S. Yang, D. J. Koo, I. H. Chaudry, and P. Wang, “Glycine attenuates hepatocellular depression during early sepsis and reduces sepsis-induced mortality,” Critical Care Medicine, vol. 29, no. 6, pp. 1201–1206, 2001. View at Publisher · View at Google Scholar · View at Scopus
  65. M. Tariq and A. R. Al Moutaery, “Studies on the antisecretory, gastric anti-ulcer and cytoprotective properties of glycine,” Research Communications in Molecular Pathology and Pharmacology, vol. 97, no. 2, pp. 185–198, 1997. View at Google Scholar · View at Scopus
  66. X. Li, B. U. Bradford, M. D. Wheeler et al., “Dietary glycine prevents peptidoglycan polysaccharide-induced reactive arthritis in the rat: role for glycine-gated chloride channel,” Infection and Immunity, vol. 69, no. 9, pp. 5883–5891, 2001. View at Publisher · View at Google Scholar · View at Scopus
  67. I. Rusyn, M. L. Rose, H. K. Bojes, and R. G. Thurman, “Novel role of oxidants in the molecular mechanism of action of peroxisome proliferators,” Antioxidants and Redox Signaling, vol. 2, no. 3, pp. 607–621, 2000. View at Publisher · View at Google Scholar · View at Scopus
  68. M. L. Rose, I. Rusyn, H. K. Bojes, D. R. Germolec, M. Luster, and R. G. Thurman, “Role of kupffer cells in peroxisome proliferator-induced hepatocyte proliferation,” Drug Metabolism Reviews, vol. 31, no. 1, pp. 87–116, 1999. View at Publisher · View at Google Scholar · View at Scopus
  69. M. L. Rose, J. Madren, H. Bunzendahl, and R. G. Thurman, “Dietary glycine inhibits the growth of B16 melanoma tumors in mice,” Carcinogenesis, vol. 20, no. 5, pp. 793–798, 1999. View at Publisher · View at Google Scholar · View at Scopus
  70. P. Schemmer, Z. Zhong, U. Galli et al., “Glycine reduces platelet aggregation,” Amino Acids, vol. 44, no. 3, pp. 925–931, 2013. View at Publisher · View at Google Scholar · View at Scopus
  71. X. Zhong, X. Li, L. Qian et al., “Glycine attenuates myocardial ischemia-reperfusion injury by inhibiting myocardial apoptosis in rats,” Journal of Biomedical Research, vol. 26, no. 5, pp. 346–354, 2012. View at Publisher · View at Google Scholar · View at Scopus
  72. M. Ruiz-Meana, P. Pina, D. Garcia-Dorado et al., “Glycine protects cardiomyocytes against lethal reoxygenation injury by inhibiting mitochondrial permeability transition,” Journal of Physiology, vol. 558, no. 3, pp. 873–882, 2004. View at Publisher · View at Google Scholar · View at Scopus
  73. R. V. Sekhar, S. G. Patel, A. P. Guthikonda et al., “Deficient synthesis of glutathione underlies oxidative stress in aging and can be corrected by dietary cysteine and glycine supplementation,” American Journal of Clinical Nutrition, vol. 94, no. 3, pp. 847–853, 2011. View at Publisher · View at Google Scholar · View at Scopus
  74. F. U. Amin, S. A. Shah, and M. O. Kim, “Glycine inhibits ethanol-induced oxidative stress, neuroinflammation and apoptotic neurodegeneration in postnatal rat brain,” Neurochemistry International, vol. 96, pp. 1–12, 2016. View at Publisher · View at Google Scholar · View at Scopus