Table of Contents Author Guidelines Submit a Manuscript
Evidence-Based Complementary and Alternative Medicine
Volume 2016, Article ID 1961327, 7 pages
http://dx.doi.org/10.1155/2016/1961327
Research Article

In Vitro Protective Effect of Phikud Navakot Extraction on Erythrocyte

1Academic Services Office, National Laboratory Animal Center, Mahidol University, 999 Salaya, Puttamonthon, Nakorn Pathom 73170, Thailand
2Department of Tropical Pathology, Faculty of Tropical Medicine, Mahidol University, 420/6 Ratchawithi Road, Ratchathewi, Bangkok 10400, Thailand

Received 2 August 2016; Accepted 3 November 2016

Academic Editor: Yoshiji Ohta

Copyright © 2016 Kanchana Kengkoom and Sumate Ampawong. 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. S. M. H. Sadrazadeh, E. Graf, S. S. Panter, P. E. Hallaway, and J. W. Eaten, “Hemoglobin, a biological Fenton reagent,” Journal of Biological and Chemistry, vol. 26, pp. 403–414, 1984. View at Google Scholar
  2. P. K. Maurya, P. Kumar, and P. Chandra, “Biomarkers of oxidative stress in erythrocytes as a function of human age,” World Journal of Methodology, vol. 5, no. 4, pp. 216–222, 2015. View at Google Scholar
  3. I. V. Buko, L. Z. Polonetskii, A. G. Mrochek, and A. G. Moǐseenok, “Antioxidant status and glutathione redox potential of erythrocytes in patients with acute coronary syndrome,” Ukrainian Biochemical Journal, vol. 86, no. 3, pp. 114–124, 2014. View at Google Scholar · View at Scopus
  4. G. D. O. Lowe, A. J. Lee, A. Rumley, J. F. Price, and F. G. R. Fowkes, “Blood viscosity and risk of cardiovascular events: the Edinburgh Artery Study,” British Journal of Haematology, vol. 96, no. 1, pp. 168–173, 1997. View at Publisher · View at Google Scholar · View at Scopus
  5. R. Schnabel, K. J. Lackner, H. J. Rupprecht et al., “Glutathione peroxidase-1 and homocysteine for cardiovascular risk prediction: results from the atherogene study,” Journal of the American College of Cardiology, vol. 45, no. 10, pp. 1631–1637, 2005. View at Publisher · View at Google Scholar · View at Scopus
  6. N. Grossin, M.-P. Wautier, and J.-L. Wautier, “Red blood cell adhesion in diabetes mellitus is mediated by advanced glycation end product receptor and is modulated by nitric oxide,” Biorheology, vol. 46, no. 1, pp. 63–72, 2009. View at Publisher · View at Google Scholar · View at Scopus
  7. M. Abudayyak, S. Ozden, B. Alpertunga, and G. Özhan, “Effects of bentazone on lipid peroxidation and antioxidant systems in human erythrocytesin vitro,” Drug and Chemical Toxicology, vol. 37, no. 4, pp. 410–414, 2014. View at Publisher · View at Google Scholar · View at Scopus
  8. G. Cavallini, M. Dachà, L. Potenza et al., “Use of red blood cell membranes to evaluate the antioxidant potential of plant extracts,” Plant Foods for Human Nutrition, vol. 69, no. 2, pp. 108–114, 2014. View at Publisher · View at Google Scholar · View at Scopus
  9. S.-P. Li, W.-L. Xie, H.-H. Cai, J.-Y. Cai, and P.-H. Yang, “Hydroxyl radical scavenging mechanism of human erythrocytes by quercetin-germanium (IV) complex,” European Journal of Pharmaceutical Sciences, vol. 47, no. 1, pp. 28–34, 2012. View at Publisher · View at Google Scholar · View at Scopus
  10. M. Suwalsky and M. Avello, “Antioxidant capacity of Ugni molinae fruit extract on human erythrocytes: an in vitro study,” The Journal of Membrane Biology, vol. 247, no. 8, pp. 703–712, 2014. View at Publisher · View at Google Scholar · View at Scopus
  11. P. Nusuetrong, U. Sotanaphun, and P. Tep-Areenan, “Effects of Phikud Navakot extract on vascular reactivity in the isolated rat aorta,” Journal of the Medical Association of Thailand, vol. 95, supplement 12, pp. S1–S7, 2012. View at Google Scholar · View at Scopus
  12. U. Sotanaphun, S. Wiyakrutta, P. Nusuctrong et al., “Development of standardized extract of Phikud Navakot, A polyherbal formula in Yahom,” in Proceedings of the 1st International Conference on Bioresources towards Wolrld Class Products, Bangkok, Thailand, 2013.
  13. N. Nalinratana, W. Kaewprem, S. Tongumpai, R. Luechapudiporn, U. Sotanaphun, and D. Meksuriyen, “Synergistic antioxidant action of Phikud Navakot ameliorates hydrogen peroxide-induced stress in human endothelial cells,” Integrative Medicine Research, vol. 3, no. 2, pp. 74–82, 2014. View at Publisher · View at Google Scholar
  14. K. Kengkoom and S. Ampawong, “Chronic ingestion of high dosed Phikud Navakot extraction induces mesangiolysis in rats with alteration of AQP1 and Hsp60 expressions,” BioMed Research International, vol. 2015, Article ID 462387, 11 pages, 2015. View at Publisher · View at Google Scholar · View at Scopus
  15. F. K. Alanazi, “Pravastatin provides antioxidant activity and protection of erythrocytes loaded Primaquine,” International Journal of Medical Sciences, vol. 7, no. 6, pp. 358–365, 2010. View at Google Scholar · View at Scopus
  16. C. M. Ajila and U. J. S. Prasada Rao, “Protection against hydrogen peroxide induced oxidative damage in rat erythrocytes by Mangifera indica L. peel extract,” Food and Chemical Toxicology, vol. 46, no. 1, pp. 303–309, 2008. View at Publisher · View at Google Scholar · View at Scopus
  17. D. Bratosin, J.-P. Tissier, H. Lapillonne et al., “A cytometric study of the red blood cells in Gaucher disease reveals their abnormal shape that may be involved in increased erythrophagocytosis,” Cytometry Part B: Clinical Cytometry, vol. 80, no. 1, pp. 28–37, 2011. View at Publisher · View at Google Scholar · View at Scopus
  18. L. Ciccoli, C. De Felice, E. Paccagnini et al., “Erythrocyte shape abnormalities, membrane oxidative damage, and β-actin alterations: an unrecognized triad in classical autism,” Mediators of Inflammation, vol. 2013, Article ID 432616, 11 pages, 2013. View at Publisher · View at Google Scholar · View at Scopus
  19. W. H. Reinhart and S. Chien, “Red cell rheology in stomatocyte-echinocyte transformation: roles of cell geometry and cell shape,” Blood, vol. 67, no. 4, pp. 1110–1118, 1986. View at Google Scholar · View at Scopus
  20. A. Shashi and G. Meenakshi, “Scanning electron microscopic study o human red blood cell abnormalities in fluoride toxicity,” International Journal of Science Innovations and Discoveries, vol. 2, no. 2, pp. 274–289, 2012. View at Google Scholar
  21. O. Singha, K. Kengkoom, K. Chaimongkolnukul et al., “Pulmonary edema due to oral gavage in a toxicological study related to aquaporin-1, -4 and -5 expression,” Journal of Toxicologic Pathology, vol. 26, no. 3, pp. 283–291, 2013. View at Publisher · View at Google Scholar · View at Scopus
  22. F. An, S. Wang, D. Yuan, Y. Gong, and S. Wang, “Attenuation of oxidative stress of erythrocytes by plant-derived flavonoids, orientin and luteolin,” Evidence-Based Complementary and Alternative Medicine, vol. 2016, Article ID 3401269, 8 pages, 2016. View at Publisher · View at Google Scholar
  23. S. Hossain, S. Bhowmick, M. Sarkar et al., “Rice germosprout extract protects erythrocytes from hemolysis and the aorta, brain, heart, and liver tissues from oxidative stress in vitro,” Evidence-Based Complementary and Alternative Medicine, vol. 2016, Article ID 9587020, 9 pages, 2016. View at Publisher · View at Google Scholar
  24. R. Morabito, O. Romano, G. La Spada, and A. Marino, “H2O2-induced oxidative stress affects SO4= transport in human erythrocytes,” PLoS ONE, vol. 11, no. 1, Article ID e0146485, 2016. View at Publisher · View at Google Scholar
  25. L. M. Snyder, N. L. Fortier, J. Trainor et al., “Effect of hydrogen peroxide exposure on normal human erythrocyte deformability, morphology, surface characteristics, and spectrin-hemoglobin cross-linking,” The Journal of Clinical Investigation, vol. 76, no. 5, pp. 1971–1977, 1985. View at Publisher · View at Google Scholar · View at Scopus
  26. J. E. Smith, “Erythrocyte membrane: structure, function, and pathophysiology,” Veterinary Pathology, vol. 24, no. 6, pp. 471–476, 1987. View at Google Scholar · View at Scopus
  27. A. Sinha, T. T. T. Chu, M. Dao, and R. Chandramohanadas, “Single-cell evaluation of red blood cell bio-mechanical and nano-structural alterations upon chemically induced oxidative stress,” Scientific Reports, vol. 5, article 9768, 2015. View at Publisher · View at Google Scholar · View at Scopus
  28. P. Gyawali, R. S. Richards, P. T. Bwititi, and E. U. Nwose, “Association of abnormal erythrocyte morphology with oxidative stress and inflammation in metabolic syndrome,” Blood Cells, Molecules, & Diseases, vol. 54, no. 4, pp. 360–363, 2015. View at Publisher · View at Google Scholar · View at Scopus
  29. E. Pytel, P. Duchnowicz, P. Jackowska, K. Wojdan, M. Koter-Michalak, and M. Broncel, “Disorders of erythrocyte structure and function in hypertensive patients,” Medical Science Monitor, vol. 18, no. 8, pp. BR331–BR336, 2012. View at Google Scholar · View at Scopus
  30. E. Pytel, M. Olszewska-Banaszczyk, M. Koter-Michalak, and M. Broncel, “Increased oxidative stress and decreased membrane fluidity in erythrocytes of CAD patients,” Biochemistry and Cell Biology, vol. 91, no. 5, pp. 315–318, 2013. View at Publisher · View at Google Scholar · View at Scopus
  31. K. Tsuda, “Oxidative stress and membrane fluidity of red blood cells in hypertensive and normotensive men: an electron Spin resonance investigation,” International Heart Journal, vol. 51, no. 2, pp. 121–124, 2010. View at Publisher · View at Google Scholar · View at Scopus
  32. B. L. Śmith and P. Agre, “Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins,” Journal of Biological Chemistry, vol. 266, no. 10, pp. 6407–6415, 1991. View at Google Scholar · View at Scopus
  33. Y. H. Chu, Y.-J. Hsu, H. S. Lee et al., “The osmopressor response is linked to upregulation of aquaporin-1 tyrosine phosphorylation on red blood cell membranes,” Hypertension, vol. 62, no. 1, pp. 197–202, 2013. View at Publisher · View at Google Scholar · View at Scopus
  34. G. Vilas, D. Krishnan, S. K. Loganathan et al., “Increased water flux induced by an aquaporin-1/carbonic anhydrase II interaction,” Molecular Biology of the Cell, vol. 26, no. 6, pp. 1106–1118, 2015. View at Publisher · View at Google Scholar · View at Scopus
  35. A. Almasalmeh, D. Krenc, B. Wu, and E. Beitz, “Structural determinants of the hydrogen peroxide permeability of aquaporins,” The FEBS Journal, vol. 281, no. 3, pp. 647–656, 2014. View at Publisher · View at Google Scholar · View at Scopus
  36. G. P. Bienert and F. Chaumont, “Aquaporin-facilitated transmembrane diffusion of hydrogen peroxide,” Biochimica et Biophysica Acta (BBA)—General Subjects, vol. 1840, no. 5, pp. 1596–1604, 2014. View at Publisher · View at Google Scholar · View at Scopus