Table of Contents
ISRN Pharmacology
Volume 2011 (2011), Article ID 975048, 7 pages
http://dx.doi.org/10.5402/2011/975048
Review Article

Potential Agents against Plasma Leakage

Department of Histology, Faculty of Medicine, University of Indonesia, Jl. Salemba 6, Jakarta 10430, Indonesia

Received 17 January 2011; Accepted 21 February 2011

Academic Editors: C. Rouillard and A. Suzuki

Copyright © 2011 Jeanne Adiwinata Pawitan. 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. M. B. Nathan, R. Dayal-Drager, and M. Guzman, “Epidemiology, burden of disease and transmission,” in WHO. Dengue Guidelines for Diagnosis, Treatment, Prevention and Control, pp. 1–21, WHO, Geneva, Switzerland, 2009. View at Google Scholar
  2. W. L. Lee and A. S. Slutsky, “Sepsis and endothelial permeability,” New England Journal of Medicine, vol. 363, no. 7, pp. 689–691, 2010. View at Publisher · View at Google Scholar · View at PubMed
  3. D. Mehta and A. B. Malik, “Signaling mechanisms regulating endothelial permeability,” Physiological Reviews, vol. 86, no. 1, pp. 279–367, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  4. B. Geiger, A. Bershadsky, R. Pankov, and K. M. Yamada, “Transmembrane extracellular matrix-cytoskeleton crosstalk,” Nature Reviews Molecular Cell Biology, vol. 2, no. 11, pp. 793–805, 2001. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  5. J. R. Gamble, J. Drew, L. Trezise et al., “Angiopoietin-1 is an antipermeability and anti-inflammatory agent in vitro and targets cell junctions,” Circulation Research, vol. 87, no. 7, pp. 603–607, 2000. View at Google Scholar · View at Scopus
  6. Q. G. Medley, E. G. Buchbinder, K. Tachibana, H. Ngo, C. Serra-Pagès, and M. Streuli, “Signaling between focal adhesion kinase and Trio,” Journal of Biological Chemistry, vol. 278, no. 15, pp. 13265–13270, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  7. J. Zhai, H. Lin, Z. Nie et al., “Direct interaction of focal adhesion kinase with p190RhoGEF,” Journal of Biological Chemistry, vol. 278, no. 27, pp. 24865–24873, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  8. G. P. Van Nieuw Amerongen, C. M. L. Beckers, I. D. Achekar, S. Zeeman, R. J. P. Musters, and V. W. M. Van Hinsbergh, “Involvement of Rho kinase in endothelial barrier maintenance,” Arteriosclerosis, Thrombosis, and Vascular Biology, vol. 27, no. 11, pp. 2332–2339, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  9. N. K. Noren, W. T. Arthur, and K. Burridge, “Cadherin engagement inhibits RhoA via p190RhoGAP,” Journal of Biological Chemistry, vol. 278, no. 16, pp. 13615–13618, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  10. W. T. Arthur, L. A. Petch, and K. Burridge, “Integrin engagement suppresses RhoA activity via a c-Src-dependent mechanism,” Current Biology, vol. 10, no. 12, pp. 719–722, 2000. View at Publisher · View at Google Scholar · View at Scopus
  11. D. Mehta, C. Tiruppathi, R. Sandoval, R. D. Minshall, M. Holinstat, and A. B. Malik, “Modulatory role of focal adhesion kinase in regulating human pulmonary arterial endothelial barrier function,” Journal of Physiology, vol. 539, no. 3, pp. 779–789, 2002. View at Publisher · View at Google Scholar · View at Scopus
  12. M. H. Wu, “Endothelial focal adhesions and barrier function,” Journal of Physiology, vol. 569, no. 2, pp. 359–366, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  13. M. Gröger, W. Pasteiner, G. Ignatyev et al., “Peptide Bβ preserves endothelial barrier function in shock,” PLoS ONE, vol. 4, no. 4, Article ID e5391, 2009. View at Publisher · View at Google Scholar · View at PubMed
  14. S. A. Tahir, S. Park, and T. C. Thompson, “Caveolin-1 regulates VEGF-stimulated angiogenic activities in prostate cancer and endothelial cells,” Cancer Biology and Therapy, vol. 8, no. 23, pp. 2286–2296, 2009. View at Google Scholar · View at Scopus
  15. S. A. Wickström, K. Alitalo, and J. Keski-Oja, “Endostatin associates with integrin αβ and caveolin-1, and activates Src via a tyrosyl phosphatase-dependent pathway in human endothelial cells,” Cancer Research, vol. 62, no. 19, pp. 5580–5589, 2002. View at Google Scholar · View at Scopus
  16. W. Schubert, P. G. Frank, S. E. Woodman et al., “Microvascular hyperpermeability in caveolin-1 (-/-) knock-out mice. Treatment with a specific nitric-oxide synthase inhibitor, L-name, restores normal microvascular permeability in Cav-1 null mice,” Journal of Biological Chemistry, vol. 277, no. 42, pp. 40091–40098, 2002. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  17. B. Wojciak-Stothard and A. J. Ridley, “Rho GTPases and the regulation of endothelial permeability,” Vascular Pharmacology, vol. 39, no. 4-5, pp. 187–199, 2002. View at Publisher · View at Google Scholar · View at Scopus
  18. J. W. Erickson and R. A. Cerione, “Multiple roles for Cdc42 in cell regulation,” Current Opinion in Cell Biology, vol. 13, no. 2, pp. 153–157, 2001. View at Publisher · View at Google Scholar · View at Scopus
  19. T. H. Millard, S. J. Sharp, and L. M. Machesky, “Signalling to actin assembly via the WASP (Wiskott-Aldrich syndrome protein)-family proteins and the Arp2/3 complex,” Biochemical Journal, vol. 380, no. 1, pp. 1–17, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  20. P. Kouklis, M. Konstantoulaki, S. Vogel, M. Broman, and A. B. Malik, “Cdc42 regulates the restoration of endothelial barrier function,” Circulation Research, vol. 94, no. 2, pp. 159–166, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  21. T. H. Loo, Y. W. Ng, L. Lim, and ED. Manser, “GIT1 activates p21-activated kinase through a mechanism independent of p21 binding,” Molecular and Cellular Biology, vol. 24, no. 9, pp. 3849–3859, 2004. View at Publisher · View at Google Scholar · View at Scopus
  22. Z. M. Goeckeler, R. A. Masaracchia, Q. Zeng, T. L. Chew, P. Gallagher, and R. B. Wysolmerski, “Phosphorylation of myosin light chain kinase by p21-activated kinase PAK2,” Journal of Biological Chemistry, vol. 275, no. 24, pp. 18366–18374, 2000. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  23. Q. Zeng, D. Lagunoff, R. Masaracchia, Z. Goeckeler, G. Côté, and R. Wysolmerski, “Endothelial cell retraction is induced by PAK2 monophosphorylation of myosin II,” Journal of Cell Science, vol. 113, no. 3, pp. 471–482, 2000. View at Google Scholar · View at Scopus
  24. T. E. B. Stradal, K. Rottner, A. Disanza, S. Confalonieri, M. Innocenti, and G. Scita, “Regulation of actin dynamics by WASP and WAVE family proteins,” Trends in Cell Biology, vol. 14, no. 6, pp. 303–311, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  25. H. Miki and T. Takenawa, “Regulation of actin dynamics by WASP family proteins,” Journal of Biochemistry, vol. 134, no. 3, pp. 309–313, 2003. View at Publisher · View at Google Scholar · View at Scopus
  26. J. Gavard and J. S. Gutkind, “VEGF controls endothelial-cell permeability by promoting the â-arrestindependent endocytosis of VE-cadherin,” Nature Cell Biology, vol. 8, pp. 1223–1234, 2006. View at Google Scholar
  27. T. A. Garrett, J. D. Van Buul, and K. Burridge, “VEGF-induced Rac1 activation in endothelial cells is regulated by the guanine nucleotide exchange factor Vav2,” Experimental Cell Research, vol. 313, no. 15, pp. 3285–3297, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  28. S. L. Sayner, D. W. Frank, J. King, H. Chen, J. VandeWaa, and T. Stevens, “Paradoxical cAMP-induced lung endothelial hyperpermeability revealed by pseudomonas aeruginosa ExoY,” Circulation Research, vol. 95, no. 2, pp. 196–203, 2004. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  29. J. Qiao, F. Huang, and H. Lum, “PKA inhibits RhoA activation: a protection mechanism against endothelial barrier dysfunction,” American Journal of Physiology, vol. 284, no. 6, pp. L972–L980, 2003. View at Google Scholar · View at Scopus
  30. X. Cullere, S. K. Shaw, L. Andersson, J. Hirahashi, F. W. Luscinskas, and T. N. Mayadas, “Regulation of vascular endothelial barrier function by Epac, a cAMP-activated exchange factor for Rap GTPase,” Blood, vol. 105, no. 5, pp. 1950–1955, 2005. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  31. S. M. Ellerbroek, K. Wennerberg, and K. Burridge, “Serine phosphorylation negatively regulates RhoA in vivo,” Journal of Biological Chemistry, vol. 278, no. 21, pp. 19023–19031, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  32. S. Spiegel and S. Milstien, “Exogenous and intracellularly generated sphingosine 1-phosphate can regulate cellular processes by divergent pathways,” Biochemical Society Transactions, vol. 31, no. 6, pp. 1216–1219, 2003. View at Google Scholar · View at Scopus
  33. J. G. N. Garcia, F. Liu, A. D. Verin et al., “Sphingosine 1-phosphate promotes endothelial cell barrier integrity by Edg-dependent cytoskeletal rearrangement,” Journal of Clinical Investigation, vol. 108, no. 5, pp. 689–701, 2001. View at Publisher · View at Google Scholar · View at Scopus
  34. K. L. Schaphorst, E. Chiang, K. N. Jacobs et al., “Role of sphingosine-1 phosphate in the enhancement of endothelial barrier integrity by platelet-released products,” American Journal of Physiology, vol. 285, no. 1, pp. L258–L267, 2003. View at Google Scholar · View at Scopus
  35. Y. Shikata, K. G. Birukov, and J. G. N. Garcia, “S1P induces FA remodeling in human pulmonary endothelial cells: role of Rac, GIT1, FAK, and paxillin,” Journal of Applied Physiology, vol. 94, no. 3, pp. 1193–1203, 2003. View at Google Scholar · View at Scopus
  36. T. Sanchez, T. Estrada-Hernandez, J. H. Paik et al., “Phosphosrylation and action of the immunomodulator FTY720 inhibits vascular endothelial cell growth factor-induced vascular permeability,” Journal of Biological Chemistry, vol. 278, no. 47, pp. 47281–47290, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  37. Y. Shikata, K. G. Birukov, A. A. Birukova, A. Verin, and J. G. N. Garcia, “Involvement of site-specific FAK phosphorylation in sphingosine-1 phosphate- and thrombin-induced focal adhesion remodeling: role of Src and GIT,” FASEB Journal, vol. 17, no. 15, pp. 2240–2249, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  38. D. Jho, R. Minshall, X. Gao et al., “Effect of vascular endothelial growth factor and angiopoietin-1 on endothelial monolayer permeability,” FASEB Journal, vol. 16, article A508, 2002. View at Google Scholar
  39. L. Pizurki, Z. Zhou, K. Glynos, C. Roussos, and A. Papapetropoulos, “Angiopoietin-1 inhibits endothelial permeability, neutrophil adherence and IL-8 production,” British Journal of Pharmacology, vol. 139, no. 2, pp. 329–336, 2003. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  40. I. Kim, S. O. Moon, K. P. Sung, W. C. Soo, and Y. K. Gou, “Angiopoietin-1 reduces VEGF-stimulated leukocyte adhesion to endothelial cells by reducing ICAM-1, VCAM-1, and E-selectin expression,” Circulation Research, vol. 89, no. 6, pp. 477–479, 2001. View at Google Scholar · View at Scopus
  41. C. A. Jones, N. Nishiya, N. R. London et al., “Slit2-Robo4 signalling promotes vascular stability by blocking Arf6 activity,” Nature Cell Biology, vol. 11, no. 11, pp. 1325–1331, 2009. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  42. C. A. Jones, N. R. London, H. Chen et al., “Robo4 stabilizes the vascular network by inhibiting pathologic angiogenesis and endothelial hyperpermeability,” Nature Medicine, vol. 14, no. 4, pp. 448–453, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  43. N. R. London, W. Zhu, F. A. Bozza et al., “Targeting Robo4-dependent slit signaling to survive the cytokine storm in sepsis and influenza,” Science Translational Medicine, vol. 2, p. 23ra19, 2010. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  44. E. Camerer, J. B. Regard, I. Cornelissen et al., “Sphingosine-1-phosphate in the plasma compartment regulates basal and inflammation-induced vascular leak in mice,” Journal of Clinical Investigation, vol. 119, no. 7, pp. 1871–1879, 2009. View at Google Scholar · View at Scopus
  45. F. Baffert, T. Le, G. Thurston, and D. M. M, “Angiopoietin-1 decreases plasma leakage by reducing number and size of endothelial gaps in venules,” American Journal of Physiology, vol. 290, no. 1, pp. H107–H118, 2006. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  46. J. S. Giuliano, P. M. Lahni, K. Harmon et al., “Admission angiopoietin levels in children with septic shock,” Shock, vol. 28, no. 6, pp. 650–654, 2007. View at Publisher · View at Google Scholar · View at Scopus
  47. M. Van Der Heijden, G. P. Van Nieuw Amerongen, P. Koolwijk, V. W. M. Van Hinsbergh, and A. B. J. Groeneveld, “Angiopoietin-2, permeability oedema, occurrence and severity of ALI/ARDS in septic and non-septic critically ill patients,” Thorax, vol. 63, no. 10, pp. 903–909, 2008. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  48. J. P. Roesner, P. Petzelbauer, A. Koch et al., “The fibrin-derived peptide Bβ15-42 is cardioprotective in a pig model of myocardial ischemia-reperfusion injury,” Critical Care Medicine, vol. 35, no. 7, pp. 1730–1735, 2007. View at Publisher · View at Google Scholar · View at PubMed · View at Scopus
  49. I. Ahrens and K. Peter, “FX-06, a fibrin-derived Bβ peptide for the potential treatment of reperfusion injury following myocardial infarction,” Current Opinion in Investigational Drugs, vol. 10, no. 9, pp. 997–1003, 2009. View at Google Scholar · View at Scopus