Rho proteins and the p38-MAPK pathway are important mediators for LPS- induced interleukin-8 expression in human endothelial cells

Blood

Volumn 95, Issue 10, 2000, Pages 3044-3051

  Hippenstiel, Stefan ^b   Soeth, Saskia ^b   Kellas, Birgit ^b   Fuhrmann, Oliver ^b   Seybold, Joachim ^b   Krüll, Matthias ^b   V Eichel Streiber, Christoph ^b   Goebeler, Matthias ^b   Ludwig, Stephan ^b   Suttorp, Norbert ^a  

^a HUMBOLDT UNIVERSITY   (Germany)

^b NONE

Author keywords

[No Author keywords available]

Indexed keywords

4 (4 FLUOROPHENYL) 2 (4 HYDROXYPHENYL) 5 (4 PYRIDYL)IMIDAZOLE; CLOSTRIDIUM TOXIN; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 8; LIPOPOLYSACCHARIDE; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE KINASE; RHO FACTOR; SYNAPTOPHYSIN;

ARTICLE; DOSE TIME EFFECT RELATION; ENDOTHELIUM CELL; ENZYME INACTIVATION; ENZYME MECHANISM; HUMAN; HUMAN CELL; PRIORITY JOURNAL; PROTEIN EXPRESSION; PROTEIN PHOSPHORYLATION; PROTEIN PROTEIN INTERACTION; REGULATORY MECHANISM; UMBILICAL VEIN;

EID: 0034658332     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v95.10.3044.010k21_3044_3051     Document Type: Article

References (57)

1. Martin MA. Epidemiology and clinical aspects of Gram-negative sepsis. Infect Dis Clin North Am. 1991;5:739.
2. Raetz CRH. Biochemistry of endotoxins. Annu Rev Biochem. 1990;59:129.
3. Carlos TM, Harlan JM. Leukocyte-endothelial adhesion molecules. Blood. 1994;84:2068.
4. McCuskey RS, Urbaschek R, Urbaschek B. The microcirculation during endotoxemia. Cardiovasc Res. 1996;32:752.
5. Berman RS, Frew JD, Martin W. Endotoxin-induced arterial endothelial barrier dysfunction assessed by an in vitro model. Br J Pharmacol. 1993;110:1282.
6. Baggiolini M, Dewald B, Moser B. Human chemokines: an update. Annu Rev Immunol. 1997;15: 675.
7. Smart SJ, Casale TB. TNF-α-induced transendothelial neutrophil migration is IL-8 dependent. Am J Physiol. 1994;266:L238.
8. Smith WB, Gamble JR, Clark-Lewis I, Vadas MA. Interleukin-8 induces neutrophil transendothelial migration. Immunology. 1991;72:65.
9. Mukaida N, Matsumoto T, Yokoi K, Harada A, Matsushima K. Inhibition of neutrophil-mediated acute inflammation injury by an antibody against interleukin-8 (IL-8). Inflamm Res. 1998;47:151.
10. Munoz C, Pascual-Salcedo D, Castellanos MC, et al. Pyrrolidine dithiocarbamate inhibits the production of interleukin-6, interleukin-8, and granulocyte-macrophage colony-stimulating factor by human endothelial cells in response to inflammatory mediators: modulation of NF-κB and AP-1 transcription factors activity. Blood. 1996;88:3480.
11. Utgaard JO, Jahnsen FL, Bakka A, Brandtzaeg P, Haraldsen G. Rapid secretion of prestored interleukin 8 from Weibel-Palade bodies of microvascular endothelial cells. J Exp Med. 1998;188:1751.
12. Wolff B, Burns AR, Middleton J, Rot A. Endothelial cell 'memory' of inflammatory stimulation: human venular endothelial cells store interleukin 8 in Weibel-Palade bodies. J Exp Med. 1998;188: 1757.
13. Arditi M, Zhou J, Torres M, Durden DL, Stins M, Kim KS. Lipopolysaccharide stimulates the tyrosine phosphorylation of mitogen-activated protein kinases p44, p42, and p41 in vascular endothelial cells in a soluble CD14-dependent manner. Role of protein tyrosine phosphorylation in lipopolysaccaride-induced stimulation of endothelial cells. J Immunol. 1995;155:3994.
14. Schumann RR, Pfeil D, Lamping N, et al. Lipopolysaccaride induces the rapid tyrosine phosphorylation of the mitogen-activated protein kinases erk-1 and p38 in cultured human vascular endothelial cells requiring the presence of soluble CD14. Blood. 1996;87:2805.
15. Yang RB, Mark MR, Gray A, et al. Toll-like receptor-2 mediates lipopolysaccharide-induced cellular signaling. Nature. 1998;17:284.
16. Kirschning CJ, Wesche H, Merrill Ayres T, Rothe M. Human toll-like receptor 2 confers responsiveness to bacterial lipopolysaccharide. J Exp Med. 1998;7:2091.
17. Zhang FX, Kirschning CJ, Mancinelli R, et al. Bacterial lipopolysaccharide activates nuclear factor-κB through interleukin-1 signaling mediators in cultured human dermal endothelial cells and mononuclear phagocytes. J Biol Chem. 1999;274:7611.
18. Tamura DY, Moore EE, Johnson JL, Zallen G, Aiboshi J, Silliman CC. p38 mitogen-activated protein kinase inhibition attenuates intercellular adhesion molecule-1 up-regulation on human pulmonary microvascular endothelial cells. Surgery. 1998;124:403.
19. Dérijard B, Raingeaud J, Barret T, et al. Independent human MAP-kinase signal transduction pathways defined by MEK and MKK isoforms. Science. 1995;267:682.
20. Han J, Lee JD, Jiang Y, Li Z, Feng L, Ulevitch RJ. Characterization of the structure and function of a novel MAP kinase kinase (MKK6) J Biol Chem. 1996;271:2886.
21. Ludwig S, Engel K, Hoffmeyer A, et al. 3pK, a novel mitogen-activated protein (MAP) kinase-activated protein kinase, is targeted by three MAP kinase pathways. Mol Cell Biol. 1996;16:6687.
22. Whitmarsh AJ, Yang SH, Su MS, Sharrocks AD, Davies RJ. Role of p38 and JNK mitogen-activated protein kinases in the activation of ternary complex factors. Mol Cell Biol. 1997;17:2360.
23. Han J, Jiang Y, Li Z, Kravchenko W, Ulevitch RJ. Activation of the transcription factor MEF2C by the MAP kinase p38 in inflammation. Nature. 1997;386:296.
24. Goebeler M, Kilian K, Gillitzer R, et al. The MKK6/ p38 stress kinase cascade is critical for tumor necrosis factor-α-induced expression of monocyte-chemoattractant protein-1 in endothelial cells. Blood. 1999;93:857.
25. Wesselborg, S, Bauer MKA, Vogt M, Schmitz ML, Schulze-Osthoff K. Activation of transcription factor NF-κB and p38 mitogen-activated protein kinase is mediated by distinct and separate stress effector pathways. J Biol Chem. 1997;272:12,422.
26. Da Silva J, Pierrat B, Mary JL, Lesslauer W. Blockade of p38 mitogen-activated protein kinase pathway inhibits inducible nitric oxide synthase expression in mouse astrocytes. J Biol Chem. 1997;272:28,373.
27. Dean JLE, Brook M, Clark AR, Saklatval J. p38 mitogen-activated protein kinase regulates cyclooxygenase-2 mRNA stability and transcription in lipopolysaccharide-treated human monocytes. J Biol Chem. 1999;274:264.
28. Craxton A, Shu G, Graves JD, Saklatvala J, Krebs EG, Clark EA. p38 MAPK is required for CD40-induced gene expression and proliferation in B lymphocytes. J Immunol. 1998;161:3225.
29. Vanden Berghe W, Plaisance S, Boone E, et al. p38 and extracellular signal-regulated kinase mitogen-activated protein kinase pathways are required for nuclear factor-κB p65 transactivation mediated by tumor necrosis factor. J Biol Chem. 1998;273:3285.
30. Montaner S, Perona R, Saniger L, Lacal JC. Multiple signalling pathways lead to the activation of the nuclear factor-κB by the Rho family of GT-Pases. J Biol Chem. 1998;273:12,779.
31. Perona R, Montaner S, Saniger S, Sánchez-Pérez I, Bravo R, Lacal, JC. Activation of the nuclear factor-κB by Rho, CDC42, and Rac-1 proteins. Genes Dev. 1997;11:463.
32. Narumiya S, Ishizaki T, Watanabe N. Rho effectors and reorganization of actin cytoskeleton. FEBS Lett. 1997;410:68.
33. Hall A. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu Rev Cell Biol. 1994;10:31.
34. Hippenstiel S, Kratz T, Krüll M, Seybold J, v Eichel-Streiber C, Suttorp N. Rho protein inhibition blocks protein kinase C translocation and activation. Biochem Biophys Res Commun. 1998; 245:830.
35. Vojtek AB, Cooper JA. Rho family members: activators of MAP kinase cascades. Cell. 1995;82: 527.
36. Coso OA, Chiariello M, Yu JC, et al. The small GTP-binding proteins rac1 and cdc42 regulate the activity of the JNK/SAPK signaling pathway. Cell. 1995;81:1137.
37. Gomez J, Garcia A, Bolando LR, et al. IL-2 signaling controls actin organization through Rho-like protein family, phosphatidylinositol 3-kinase, and protein kinase C-zeta. J Immunol. 1997;158: 1516.
38. Chong LD, Traynor-Kaplan A, Bokosch GM, Schwarte MA. The small GTP-binding protein Rho regulates a phosphatidylinositol 4-phosphate 5-kinase in mammalian cells. Cell. 1994;79:507.
39. Schmidt M, Rümenapp U, Bienek C, Keller J, v Eichel-Streiber C, Jakobs KH. Inhibition of receptor signaling to phospholipase D by Clostridium difficile toxin B. Role of Rho proteins. J Biol Chem. 1996;271:2422.
40. Itoh K, Yoshioka K, Akedo H, Uehata M, Ishizaka T, Narumiya S. An essential part for Rho-associated kinase in the transcellular invasion of tumor cells. Nat Med. 1999;5:221.
41. Essler M, Herman K, Amano M, et al. Pastorella multocida toxin increases endothelial permeability via Rho kinase and myosin light chain phosphatase. J Immunol. 1998;161:5640.
42. Just I, Selzer J, Wil M, v Eichel-Streiber C, Mann M, Aktories K. Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature. 1995; 375:500.
43. Chavez-Olarte E, Weidmann M, v Eichel-Streiber C, Thelestam M. Toxins A and B from Clostridium difficile differ with respect to enzymatic potencies, cellular substrate specificities, and surface binding to cultured cells. J Clin Invest. 1997;00:1734.
44. Hippenstiel S, Tannert-Otto S, et al. Glucosylation of small-GTP binding Rho proteins disrupts endothelial barrier function. Am J Physiol. 1997;272: L38.
45. Popoff MR, Chaves-Olarte E, Lemichez E, et al. Ras, Rap, and Rac small GTP-binding proteins are targets for Clostridium sordellii lethal toxin glucosylation. J Biol Chem. 1996;271:10,217.
46. Schwarzer N, Nöst R, Seybold J, et al. Listeria monocytogenes induce ceramide generation, nuclear factor-κB activation, and E-selectin expression in human endothelial cells. J Immunol. 1998;161:3010.
47. Krüll M, Klucken AC, Wuppermann FN, et al. Signal transduction pathways activated in endothelial cells following infection with Chlamydia pneumoniae. J Immunol. 1999;162:4834.
48. Dunn OJ, Clark VA. Applied Statistics: Analysis of Variance and Regression. New York, NY: John Wiley & Sons Inc. 1947.
49. Schmidt M, Voss M, Thiel M, Bauer B, et al. Specific inhibition of phorbol ester-stimulated phospholipase D by Clostridium sordellii lethal toxin and Clostridium difficile toxin B-1470 in HEK-293 cells. Restoration by Ral GTPases. J Biol Chem. 1998;273:7413.
50. Aktories K, Hall A. Botulinum ADP-ribosyltransferase C3: a new tool to study low molecular weight GTP-binding proteins. Trends Pharmacol Sci. 1989;10:415.
51. Lucius C, Arner A, Steusliff A, et al. Clostridium difficile toxin B inhibits carbachol-induced force and myosin light chain phosphorylation in guinea-pig smooth muscle: role of Rho proteins. J Physiol (Lond). 1998;506:83.
52. Rümenapp U, Schmidt M, Olesch S, Ott S, v Eichel-Streiber C, Jakobs KH. Tyrosine-phosphorylation-dependent and Rho-protein-mediated control of cellular phosphatidylinositol 4,5-bisphosphate levels. Biochem J. 1998; 334:625.
53. Beltman J, Erickson JR, Martin GA, Lyons JF, Cook SJ. C3 toxin activates the stress signaling pathways, JNK and p38, but antagonizes the activation of AP-1 in rat-1 cells. J Biol Chem. 1999; 274:3772.
54. Molnar A, Theodoras AM, Zon LI, Kyriakis JM. Cdc42Hs, but not Rac1, inhibits serum-stimulated cell cycle progression at G1/S through a mechanism requiring p38/RK. J Biol Chem. 1997;272: 13,229
55. Bagrodia S, Derijard B, Davies RJ, Cerione RA. Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation. J Biol Chem. 1995;270:27,995.
56. Zhang S, Han J, Sells MA, et al. Rho family GT-Pases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1. J Biol Chem. 1995;270:23,934.
57. Kotlyarov A, Neininger A, Schubert C, et al. MAPKAP kinase 2 is essential for LPS-induced TNF-α biosynthesis. Nat Cell Biol. 1999;1:94.