Table of Contents Author Guidelines Submit a Manuscript
Evidence-Based Complementary and Alternative Medicine
Volume 2015, Article ID 430271, 12 pages
http://dx.doi.org/10.1155/2015/430271
Research Article

Scutellarin Reduces Endothelium Dysfunction through the PKG-I Pathway

1School of Pharmaceutical Science and Yunnan Key Laboratory of Pharmacology for Natural Products, Kunming Medical University, Kunming 650500, China
2Department of Respiratory Medicine, First Affiliated Hospital of Kunming Medical University, Kunming 650032, China
3Pharmacy Department, First Affiliated Hospital of Kunming Medical University, Kunming 650032, China
4Department of Clinical Pharmacy, First Affiliated Hospital of Kunming Medical University, Kunming 650032, China

Received 4 May 2015; Revised 25 July 2015; Accepted 4 August 2015

Academic Editor: Dan Hu

Copyright © 2015 Xiaohua Du 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. A. R. Pries and W. M. Kuebler, “Normal endothelium,” in The Vascular Endothelium I, vol. 176 of Handbook of Experimental Pharmacology, part 1, pp. 1–40, Springer, Berlin, Germany, 2006. View at Publisher · View at Google Scholar
  2. T. W. Hein, C. Zhang, W. Wang, C.-I. Chang, N. Thengchaisri, and L. Kuo, “Ischemia-reperfusion selectively impairs nitric oxide-mediated dilation in coronary arterioles: counteracting role of arginase,” The FASEB Journal, vol. 17, no. 15, pp. 2328–2330, 2003. View at Publisher · View at Google Scholar · View at Scopus
  3. H. Xie, P. E. Ray, and B. L. Short, “NF-κB activation plays a role in superoxide-mediated cerebral endothelial dysfunction after hypoxia/reoxygenation,” Stroke, vol. 36, no. 5, pp. 1047–1052, 2005. View at Publisher · View at Google Scholar · View at Scopus
  4. H. K. Eltzschig and C. D. Collard, “Vascular ischaemia and reperfusion injury,” British Medical Bulletin, vol. 70, no. 1, pp. 71–86, 2004. View at Publisher · View at Google Scholar · View at Scopus
  5. K. Laude, P. Beauchamp, C. Thuillez, and V. Richard, “Endothelial protective effects of preconditioning,” Cardiovascular Research, vol. 55, no. 3, pp. 466–473, 2002. View at Publisher · View at Google Scholar · View at Scopus
  6. R. K. Kharbanda, M. Peters, B. Walton et al., “Ischemic preconditioning prevents endothelial injury and systemic neutrophil activation during ischemia-reperfusion in humans in vivo,” Circulation, vol. 103, no. 12, pp. 1624–1630, 2001. View at Publisher · View at Google Scholar · View at Scopus
  7. S. H. Francis, J. L. Busch, and J. D. Corbin, “cGMP-dependent protein kinases and cGMP phosphodiesterases in nitric oxide and cGMP action,” Pharmacological Reviews, vol. 62, no. 3, pp. 525–563, 2010. View at Publisher · View at Google Scholar · View at Scopus
  8. H. Sellak, C.-S. Choi, N. B. Dey, and T. M. Lincoln, “Transcriptional and post-transcriptional regulation of cGMP-dependent protein kinase (PKG-I): pathophysiological significance,” Cardiovascular Research, vol. 97, no. 2, pp. 200–207, 2013. View at Publisher · View at Google Scholar · View at Scopus
  9. E. Cairrão, A. J. Santos-Silva, and I. Verde, “PKG is involved in testosterone-induced vasorelaxation of human umbilical artery,” European Journal of Pharmacology, vol. 640, no. 1–3, pp. 94–101, 2010. View at Publisher · View at Google Scholar · View at Scopus
  10. Y.-L. Lin, Z.-K. Dai, R.-J. Lin et al., “Baicalin, a flavonoid from Scutellaria baicalensis Georgi, activates large-conductance Ca2+-activated K+ channels via cyclic nucleotide-dependent protein kinases in mesenteric artery,” Phytomedicine, vol. 17, no. 10, pp. 760–770, 2010. View at Publisher · View at Google Scholar · View at Scopus
  11. E. Schulz, N. Tsilimingas, R. Rinze et al., “Functional and biochemical analysis of endothelial (Dys)function and NO/cGMP signaling in human blood vessels with and without nitroglycerin pretreatment,” Circulation, vol. 105, no. 10, pp. 1170–1175, 2002. View at Publisher · View at Google Scholar · View at Scopus
  12. M. Gao, W. Huang, and C.-Z. Liu, “Separation of scutellarin from crude extracts of Erigeron breviscapus (vant.) Hand. Mazz. by macroporous resins,” Journal of Chromatography B: Analytical Technologies in the Biomedical and Life Sciences, vol. 858, no. 1-2, pp. 22–26, 2007. View at Publisher · View at Google Scholar · View at Scopus
  13. H. Guo, L.-M. Hu, S.-X. Wang et al., “Neuroprotective effects of scutellarin against hypoxic-ischemic-induced cerebral injury via augmentation of antioxidant defense capacity,” Chinese Journal of Physiology, vol. 54, no. 6, pp. 399–405, 2011. View at Publisher · View at Google Scholar · View at Scopus
  14. X.-M. Hu, M.-M. Zhou, X.-M. Hu, and F.-D. Zeng, “Neuroprotective effects of scutellarin on rat neuronal damage induced by cerebral ischemia/reperfusion,” Acta Pharmacologica Sinica, vol. 26, no. 12, pp. 1454–1459, 2005. View at Publisher · View at Google Scholar · View at Scopus
  15. Y. Su, W. Liu, L. Ma, X. Liu, Z. Liu, and B. Zhu, “Scutellarin inhibits translocation of protein kinase C in diabetic thoracic aorta of the rat,” Clinical and Experimental Pharmacology and Physiology, vol. 39, no. 2, pp. 136–140, 2012. View at Publisher · View at Google Scholar · View at Scopus
  16. W. Yang, A. Bofferding, R. M. Lust, and C. J. Wingard, “Effect of scutellarin on contractile behavior of isolated thoracic aorta rings of the mouse,” The FASEB Journal, vol. 21, no. 6, Article ID A1160, 2007. View at Google Scholar
  17. W. Yang, R. M. Lust, A. Bofferding, and C. J. Wingard, “Nitric oxide and catalase-sensitive relaxation by scutellarin in the mouse thoracic aorta,” Journal of Cardiovascular Pharmacology, vol. 53, no. 1, pp. 66–76, 2009. View at Publisher · View at Google Scholar · View at Scopus
  18. D. S. Burley, P. Ferdinandy, and G. F. Baxter, “Cyclic GMP and protein kinase-G in myocardial ischaemia-reperfusion: opportunities and obstacles for survival signaling,” British Journal of Pharmacology, vol. 152, no. 6, pp. 855–869, 2007. View at Publisher · View at Google Scholar · View at Scopus
  19. Z. Wang, T. Liu, L. Gan et al., “Shikonin protects mouse brain against cerebral ischemia/reperfusion injury through its antioxidant activity,” European Journal of Pharmacology, vol. 643, no. 2-3, pp. 211–217, 2010. View at Publisher · View at Google Scholar · View at Scopus
  20. X. Zeng, S. Zhang, L. Zhang, K. Zhang, and X. Zheng, “A study of the neuroprotective effect of the phenolic glucoside gastrodin during cerebral ischemia in vivo and in vitro,” Planta Medica, vol. 72, no. 15, pp. 1359–1365, 2006. View at Publisher · View at Google Scholar · View at Scopus
  21. L.-L. Lin, A.-J. Liu, J.-G. Liu, X.-H. Yu, L.-P. Qin, and D.-F. Su, “Protective effects of scutellarin and breviscapine on brain and heart ischemia in rats,” Journal of Cardiovascular Pharmacology, vol. 50, no. 3, pp. 327–332, 2007. View at Publisher · View at Google Scholar · View at Scopus
  22. Z. Pan, W. Zhao, X. Zhang et al., “Scutellarin alleviates interstitial fibrosis and cardiac dysfunction of infarct rats by inhibiting TGFβ1 expression and activation of p38-MAPK and ERK1/2,” British Journal of Pharmacology, vol. 162, no. 3, pp. 688–700, 2011. View at Publisher · View at Google Scholar · View at Scopus
  23. H. Hong and G.-Q. Liu, “Scutellarin protects PC12 cells from oxidative stress-induced apoptosis,” Journal of Asian Natural Products Research, vol. 8, no. 6, pp. 471–479, 2006. View at Publisher · View at Google Scholar · View at Scopus
  24. S. Wang, H. Wang, H. Guo, L. Kang, X. Gao, and L. Hu, “Neuroprotection of Scutellarin is mediated by inhibition of microglial inflammatory activation,” Neuroscience, vol. 185, pp. 150–160, 2011. View at Publisher · View at Google Scholar · View at Scopus
  25. Z.-X. Gao, D.-Y. Huang, H.-X. Li et al., “Scutellarin promotes in vitro angiogenesis in human umbilical vein endothelial cells,” Biochemical and Biophysical Research Communications, vol. 400, no. 1, pp. 151–156, 2010. View at Publisher · View at Google Scholar · View at Scopus
  26. H. Dai, J. Gu, L.-Z. Li, L.-M. Yang, H. Liu, and J.-Y. Li, “Scutellarin benzyl ester partially secured the ischemic injury by its anti-apoptosis mechanism in cardiomyocytes of neonatal rats,” Journal of Chinese Integrative Medicine, vol. 9, no. 9, pp. 1014–1021, 2011. View at Publisher · View at Google Scholar · View at Scopus
  27. L.-L. Guo, Z.-Z. Guan, Y. Huang, Y.-L. Wang, and J.-S. Shi, “The neurotoxicity of β-amyloid peptide toward rat brain is associated with enhanced oxidative stress, inflammation and apoptosis, all of which can be attenuated by scutellarin,” Experimental and Toxicologic Pathology, vol. 65, no. 5, pp. 579–584, 2013. View at Publisher · View at Google Scholar · View at Scopus
  28. H.-F. Zhang, X.-M. Hu, L.-X. Wang, S.-Q. Xu, and F.-D. Zeng, “Protective effects of scutellarin against cerebral ischemia in rats: evidence for inhibition of the apoptosis-inducing factor pathway,” Planta Medica, vol. 75, no. 2, pp. 121–126, 2009. View at Publisher · View at Google Scholar · View at Scopus
  29. D.-P. Jiang, Q. Li, J. Yang, J. M. Perelman, V. P. Kolosov, and X.-D. Zhou, “Scutellarin attenuates human-neutrophil-elastase-induced mucus production by inhibiting the PKC-ERK signaling pathway in vitro and in vivo,” The American Journal of Chinese Medicine, vol. 39, no. 6, pp. 1193–1206, 2011. View at Publisher · View at Google Scholar · View at Scopus
  30. P. Luo, Z.-H. Tan, Z.-F. Zhang, H. Zhang, X.-F. Liu, and Z.-J. Mo, “Scutellarin isolated from Erigeron multiradiatus inhibits high glucose-mediated vascular inflammation,” Yakugaku Zasshi, vol. 128, no. 9, pp. 1293–1299, 2008. View at Publisher · View at Google Scholar · View at Scopus
  31. H. Xu and S. Zhang, “Scutellarin-induced apoptosis in HepG2 hepatocellular carcinoma cells via a STAT3 pathway,” Phytotherapy Research, vol. 27, no. 10, pp. 1524–1528, 2013. View at Publisher · View at Google Scholar · View at Scopus
  32. Y. Feng, S. Zhang, J. Tu et al., “Novel function of scutellarin in inhibiting cell proliferation and inducing cell apoptosis of human Burkitt lymphoma Namalwa cells,” Leukemia and Lymphoma, vol. 53, no. 12, pp. 2456–2464, 2012. View at Publisher · View at Google Scholar · View at Scopus
  33. G.-H. Zhang, Q. Wang, J.-J. Chen, X.-M. Zhang, S.-C. Tam, and Y.-T. Zheng, “The anti-HIV-1 effect of scutellarin,” Biochemical and Biophysical Research Communications, vol. 334, no. 3, pp. 812–816, 2005. View at Publisher · View at Google Scholar · View at Scopus
  34. W. Xu, R.-P. Zha, W.-Y. Wang, and Y.-P. Wang, “Effects of scutellarin on PKCγ in PC12 cell injury induced by oxygen and glucose deprivation,” Acta Pharmacologica Sinica, vol. 28, no. 10, pp. 1573–1579, 2007. View at Publisher · View at Google Scholar · View at Scopus
  35. B. H. Neo, S. Kandhi, M. Ahmad, and M. S. Wolin, “Redox regulation of guanylate cyclase and protein kinase G in vascular responses to hypoxia,” Respiratory Physiology and Neurobiology, vol. 174, no. 3, pp. 259–264, 2010. View at Publisher · View at Google Scholar · View at Scopus
  36. A. Aicher, C. Heeschen, S. Feil et al., “CGMP-dependent protein kinase I is crucial for angiogenesis and postnatal vasculogenesis,” PLoS ONE, vol. 4, no. 3, Article ID e4879, 2009. View at Publisher · View at Google Scholar · View at Scopus
  37. B. Kemp-Harper and H. H. H. W. Schmidt, “cGMP in the vasculature,” in cGMP: Generators, Effectors and Therapeutic Implications, vol. 191 of Handbook of Experimental Pharmacology, pp. 447–467, Springer, Berlin, Germany, 2009. View at Publisher · View at Google Scholar
  38. D. Atochin, E. Buys, H. Swanson et al., “Abstract T P225: cGMP-dependent protein kinase I in smooth muscle cells protects against stroke injury in mice,” Stroke, vol. 45, supplement 1, Article ID ATP225, 2014. View at Google Scholar
  39. Y. Chai, D.-M. Zhang, and Y.-F. Lin, “Activation of cGMP-dependent protein kinase stimulates cardiac ATP-sensitive potassium channels via a ROS/calmodulin/CaMKII signaling cascade,” PLoS ONE, vol. 6, no. 3, Article ID e18191, 2011. View at Publisher · View at Google Scholar · View at Scopus
  40. J. E. Bear, J. J. Loureiro, I. Libova, R. Fässler, J. Wehland, and F. B. Gertler, “Negative regulation of fibroblast motility by Ena/VASP proteins,” Cell, vol. 101, no. 7, pp. 717–728, 2000. View at Publisher · View at Google Scholar · View at Scopus
  41. L. Chen, G. Daum, K. Chitaley et al., “Vasodilator-stimulated phosphoprotein regulates proliferation and growth inhibition by nitric oxide in vascular smooth muscle cells,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 24, no. 8, pp. 1403–1408, 2004. View at Publisher · View at Google Scholar · View at Scopus
  42. T. M. Gomez and E. Robles, “The great escape: phosphorylation of Ena/VASP by PKA promotes filopodial formation,” Neuron, vol. 42, no. 1, pp. 1–3, 2004. View at Publisher · View at Google Scholar · View at Scopus
  43. X. Wang, J. L. Pluznick, D. C. Settles, and S. C. Sansom, “Association of VASP with TRPC4 in PKG-mediated inhibition of the store-operated calcium response in mesangial cells,” American Journal of Physiology - Renal Physiology, vol. 293, no. 6, pp. F1768–F1776, 2007. View at Publisher · View at Google Scholar · View at Scopus