Table of Contents Author Guidelines Submit a Manuscript
Journal of Diabetes Research
Volume 2013, Article ID 593672, 12 pages
http://dx.doi.org/10.1155/2013/593672
Research Article

Boldine Prevents Renal Alterations in Diabetic Rats

1Departamento de Fisiología, Pontificia Universidad Católica de Chile, Alameda Bernardo O’Higgins, No. 340, 6513677 Santiago, Chile
2Instituto Milenio, Centro Interdisciplinario de Neurociencias de Valparaíso, Valparaíso, Chile

Received 22 September 2013; Accepted 6 November 2013

Academic Editor: Raffaele Marfella

Copyright © 2013 Romina Hernández-Salinas 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. T. Nakagawa, K. Tanabe, B. P. Croker et al., “Endothelial dysfunction as a potential contributor in diabetic nephropathy,” Nature Reviews Nephrology, vol. 7, no. 1, pp. 36–44, 2011. View at Publisher · View at Google Scholar · View at Scopus
  2. M. C. Thomas, “Advanced glycation end products,” Contributions to Nephrology, vol. 170, pp. 66–74, 2011. View at Publisher · View at Google Scholar · View at Scopus
  3. R. Choi, B. H. Kim, J. Naowaboot et al., “Effects of ferulic acid on diabetic nephropathy in a rat model of type 2 diabetes,” Experimental and Molecular Medicine, vol. 43, no. 12, pp. 676–683, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. J. Kang, X.-S. Dai, T.-B. Yu, B. Wen, and Z.-W. Yang, “Glycogen accumulation in renal tubules, a key morphological change in the diabetic rat kidney,” Acta Diabetologica, vol. 42, no. 2, pp. 110–119, 2005. View at Publisher · View at Google Scholar · View at Scopus
  5. K. Alexandraki, C. Piperi, C. Kalofoutis, J. Singh, A. Alaveras, and A. Kalofoutis, “Inflammatory process in type 2 diabetes: the role of cytokines,” Annals of the New York Academy of Sciences, vol. 1084, pp. 89–117, 2006. View at Publisher · View at Google Scholar · View at Scopus
  6. J.-W. Yoon and H.-S. Jun, “Cellular and molecular pathogenic mechanisms of insulin-dependent diabetes mellitus,” Annals of the New York Academy of Sciences, vol. 928, pp. 200–211, 2001. View at Google Scholar · View at Scopus
  7. M. Fernandez-Cobo, C. Gingalewski, and A. de Maio, “Expression of the connexin 43 gene is increased in the kidneys and the lungs of rats injected with bacterial lipopolysaccharide,” Shock, vol. 10, no. 2, pp. 97–102, 1998. View at Google Scholar · View at Scopus
  8. J. H.-C. Lin, N. Lou, N. Kang et al., “A central role of connexin 43 in hypoxic preconditioning,” The Journal of Neuroscience, vol. 28, no. 3, pp. 681–695, 2008. View at Publisher · View at Google Scholar · View at Scopus
  9. H. E. González, E. A. Eugenín, G. Garcés et al., “Regulation of hepatic connexins in cholestasis: possible involvement of Kupffer cells and inflammatory mediators,” American Journal of Physiology: Gastrointestinal and Liver Physiology, vol. 282, no. 6, pp. G991–G1001, 2002. View at Google Scholar · View at Scopus
  10. W. Même, C.-F. Calvo, N. Froger et al., “Proinflammatory cytokines released from microglia inhibit gap junctions in astrocytes: potentiation by β-amyloid,” The FASEB Journal, vol. 20, no. 3, pp. 494–496, 2006. View at Publisher · View at Google Scholar · View at Scopus
  11. J. E. Contreras, H. A. Sánchez, E. A. Eugenin et al., “Metabolic inhibition induces opening of unapposed connexin 43 gap junction hemichannels and reduces gap junctional communication in cortical astrocytes in culture,” Proceedings of the National Academy of Sciences of the United States of America, vol. 99, no. 1, pp. 495–500, 2002. View at Publisher · View at Google Scholar · View at Scopus
  12. M. A. Retamal, N. Froger, N. Palacios-Prado et al., “Cx43 hemichannels and gap junction channels in astrocytes are regulated oppositely by proinflammatory cytokines released from activated microglia,” The Journal of Neuroscience, vol. 27, no. 50, pp. 13781–13792, 2007. View at Publisher · View at Google Scholar · View at Scopus
  13. L. Vergara, X. Bao, E. Bello-Reuss, and L. Reuss, “Do connexin 43 gap-junctional hemichannels activate and cause cell damage during ATP depletion of renal-tubule cells?” Acta Physiologica Scandinavica, vol. 179, no. 1, pp. 33–38, 2003. View at Publisher · View at Google Scholar · View at Scopus
  14. J. M. Garré, M. A. Retamal, P. Cassina et al., “FGF-1 induces ATP release from spinal astrocytes in culture and opens pannexin and connexin hemichannels,” Proceedings of the National Academy of Sciences of the United States of America, vol. 107, no. 52, pp. 22659–22664, 2010. View at Publisher · View at Google Scholar · View at Scopus
  15. K. A. Schalper, N. Palacios-Prado, M. A. Retamal, K. F. Shoji, A. D. Martínez, and J. C. Sáez, “Connexin hemichannel composition determines the FGF-1-induced membrane permeability and free [Ca2+]i responses,” Molecular Biology of the Cell, vol. 19, no. 8, pp. 3501–3513, 2008. View at Publisher · View at Google Scholar · View at Scopus
  16. J. Toubas, S. Beck, A.-L. Pageaud et al., “Alteration of connexin expression is an early signal for chronic kidney disease,” American Journal of Physiology: Renal Physiology, vol. 301, no. 1, pp. F24–F32, 2011. View at Publisher · View at Google Scholar · View at Scopus
  17. M. A. Retamal, C. J. Cortés, L. Reuss, M. V. L. Bennett, and J. C. Sáez, “S-nitrosylation and permeation through connexin 43 hemichannels in astrocytes: induction by oxidant stress and reversal by reducing agents,” Proceedings of the National Academy of Sciences of the United States of America, vol. 103, no. 12, pp. 4475–4480, 2006. View at Publisher · View at Google Scholar · View at Scopus
  18. M. A. Retamal, K. A. Schalper, K. F. Shoji, M. V. L. Bennett, and J. C. Sáez, “Opening of connexin 43 hemichannels is increased by lowering intracellular redox potential,” Proceedings of the National Academy of Sciences of the United States of America, vol. 104, no. 20, pp. 8322–8327, 2007. View at Publisher · View at Google Scholar · View at Scopus
  19. A. A. Taylor, H. Siragy, and S. Nesbitt, “Angiotensin receptor blockers: pharmacology, efficacy, and safety,” Journal of Clinical Hypertension, vol. 13, no. 9, pp. 677–686, 2011. View at Publisher · View at Google Scholar · View at Scopus
  20. H. Speisky and B. K. Cassels, “Boldo and boldine: an emerging case of natural drug development,” Pharmacological Research, vol. 29, no. 1, pp. 1–12, 1994. View at Publisher · View at Google Scholar · View at Scopus
  21. A. Urzúa and P. Acuña, “Alkaloids from the bark of Peumus boldus,” Fitoterapia, vol. 54, no. 4, pp. 175–177, 1983. View at Google Scholar · View at Scopus
  22. H. Speisky, B. K. Cassels, S. Nieto, A. Valenzuela, and L. J. Nunez-Vergara, “Determination of boldine in plasma by high-performance liquid chromatography,” Journal of Chromatography, vol. 612, no. 2, pp. 315–319, 1993. View at Publisher · View at Google Scholar · View at Scopus
  23. M. M. Bradford, “A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein dye binding,” Analytical Biochemistry, vol. 72, no. 1-2, pp. 248–254, 1976. View at Google Scholar · View at Scopus
  24. L. Ramanathan, N. P. Das, and Q.-T. Li, “Studies on lipid oxidation in fish phospholipid liposomes,” Biological Trace Element Research, vol. 40, no. 1, pp. 59–70, 1994. View at Google Scholar · View at Scopus
  25. O. H. Lowry, N. J. Roserbrough, A. L. Farr, and R. J. Randall, “Protein measurement with the Folin phenol reagent,” The Journal of Biological Chemistry, vol. 193, no. 1, pp. 265–275, 1951. View at Google Scholar · View at Scopus
  26. A. Mathew, R. Cunard, and K. Sharma, “Antifibrotic treatment and other new strategies for improving renal outcomes,” Contributions to Nephrology, vol. 170, pp. 217–227, 2011. View at Publisher · View at Google Scholar · View at Scopus
  27. M. Essawy, O. Soylemezoglu, E. C. Muchaneta-Kubara, J. Shortland, C. B. Brown, and A. M. El Nahas, “Myofibroblasts and the progression of diabetic nephropathy,” Nephrology Dialysis Transplantation, vol. 12, no. 1, pp. 43–50, 1997. View at Publisher · View at Google Scholar · View at Scopus
  28. J. Li, X. Qu, and J. F. Bertram, “Endothelial-myofibroblast transition contributes to the early development of diabetic renal interstitial fibrosis in streptozotocin-induced diabetic mice,” American Journal of Pathology, vol. 175, no. 4, pp. 1380–1388, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. J. A. Orellana, D. E. Hernández, P. Ezan et al., “Hypoxia in high glucose followed by reoxygenation in normal glucose reduces the viability of cortical astrocytes through increased permeability of connexin 43 hemichannels,” Glia, vol. 58, no. 3, pp. 329–343, 2010. View at Publisher · View at Google Scholar · View at Scopus
  30. J. A. Orellana, K. F. Shoji, V. Abudara et al., “Amyloid β-induced death in neurons involves glial and neuronal hemichannels,” The Journal of Neuroscience, vol. 31, no. 13, pp. 4962–4977, 2011. View at Publisher · View at Google Scholar · View at Scopus
  31. J. A. Orellana, X. F. Figueroa, H. A. Sánchez, S. Contreras-Duarte, V. Velarde, and J. C. Sáez, “Hemichannels in the neurovascular unit and white matter under normal and inflamed conditions,” CNS and Neurological Disorders, vol. 10, no. 3, pp. 404–414, 2011. View at Google Scholar · View at Scopus
  32. G. Kanaporis, P. R. Brink, and V. Valiunas, “Gap junction permeability: selectivity for anionic and cationic probes,” American Journal of Physiology: Cell Physiology, vol. 300, no. 3, pp. C600–C609, 2011. View at Publisher · View at Google Scholar · View at Scopus
  33. P. Klee, F. Allagnat, H. Pontes et al., “Connexins protect mouse pancreatic β cells against apoptosis,” Journal of Clinical Investigation, vol. 121, no. 12, pp. 4870–4879, 2011. View at Publisher · View at Google Scholar · View at Scopus
  34. F. Hanner, C. M. Sorensen, N.-H. Holstein-Rathlou, and J. Peti-Peterdi, “Connexins and the kidney,” American Journal of Physiology: Regulatory Integrative and Comparative Physiology, vol. 298, no. 5, pp. R1143–R1155, 2010. View at Publisher · View at Google Scholar · View at Scopus
  35. N. Backhouse, C. Delporte, M. Givernau, B. K. Cassels, A. Valenzuela, and H. Speisky, “Anti-inflammatory and antipyretic effects of boldine,” Agents and Actions, vol. 42, no. 3-4, pp. 114–117, 1994. View at Publisher · View at Google Scholar · View at Scopus
  36. T.-C. Chi, S.-S. Lee, and M.-J. Su, “Antihyperglycemic effect of aporphines and their derivatives in normal and diabetic rats,” Planta Medica, vol. 72, no. 13, pp. 1175–1180, 2006. View at Publisher · View at Google Scholar · View at Scopus
  37. Y. Y. Jang, J. H. Song, Y. K. Shin, E. S. Han, and C. S. Lee, “Protective effect of boldine on oxidative mitochondrial damage in streptozotocin-induced diabetic rats,” Pharmacological Research, vol. 42, no. 4, pp. 361–371, 2000. View at Publisher · View at Google Scholar · View at Scopus
  38. A. Mollataghi, E. Coudiere, A. H. A. Hadi et al., “Anti-acetylcholinesterase, anti-α-glucosidase, anti-leishmanial and anti-fungal activities of chemical constituents of Beilschmiedia species,” Fitoterapia, vol. 83, no. 2, pp. 298–302, 2012. View at Publisher · View at Google Scholar · View at Scopus
  39. J. Fernández, P. Lagos, P. Rivera, and E. Zamorano-Ponce, “Effect of boldo (Peumus boldus Molina) infusion on lipoperoxidation induced by cisplatin in mice liver,” Phytotherapy Research, vol. 23, no. 7, pp. 1024–1027, 2009. View at Publisher · View at Google Scholar · View at Scopus
  40. C. P. Vio, S. Loyola, and V. Velarde, “Localization of components of the kallikrein-kinin system in the kidney: relation to renal function: state of the art lecture,” Hypertension, vol. 19, no. 2, pp. II10–II16, 1992. View at Google Scholar · View at Scopus
  41. G. Lu, H. K. Haider, A. Porollo, and M. Ashraf, “Mitochondria-specific transgenic overexpression of connexin-43 simulates preconditioning-induced cytoprotection of stem cells,” Cardiovascular Research, vol. 88, no. 2, pp. 277–286, 2010. View at Publisher · View at Google Scholar · View at Scopus
  42. D. Johansen, V. Cruciani, R. Sundset, K. Ytrehus, and S.-O. Mikalsen, “Ischemia induces closure of gap junctional channels and opening of hemichannels in heart-derived cells and tissue,” Cellular Physiology and Biochemistry, vol. 28, no. 1, pp. 103–114, 2011. View at Publisher · View at Google Scholar · View at Scopus