[Seite 99↓]

Literaturverzeichnis

1. Alberts, B., Bray, D., Lewis, J., Raff, M., Roberts, K., Watson, J.D. Das Cytoskelett. In: Lehrbuch der molekularen Zellbiologie 2. Auflage, VCH-Verlagsgesellschaft, Weinheim, Germany. 734-812 (2001)

2. Alexander, JS., Hechtmann, HB, Shepro, D. Phalloidin enhances endothelial barrier function and reduces inflammatory permeability in vitro. Microvasc Res 35: 308-315 (1988)

3. Ashbaugh, D.G., Bigelow, D.B., Petty, T.L., Levine, B.E. Acute respiratory distress in adults. Lancet 2: 319-323 (1967)

4. Barnard, J.W., Malik, A.B. Control of endothelial permeability. Intern. Soc. Heart Res.: 109-115 (1994)

5. Bashur, A.M., Fullerton, A.T., Hart, M.J., Bloom, G.S. IQGAP1, a Rac- and Cdc42-binding protein, directly binds and cross-links microfilaments. J. Cell Biol. 13: 1555-1566 (1997)

6. Bershadsky, A., Chausovsky, A., Becker, E., Lyubimova, A., Geiger, B. Involvement of microtubules in the control of adhesion-dependent signal transduction. Curr. Biol. 6: 1279-1289 (1996)

7. Bloom, G. S., Valle, R.B. Association of microtubule-associated protein 2 (MAP 2) with microtubules and intermediate filaments in cultured brain cells. J. Cell Biol. 96: 1523-1531 (1983)

8. Boge, T.C., Himes, R.H., Vander Velde, D.G., George, G.I. The effect of the aromatic rings of taxol on biological activity and solution conformation: synthesis and evaluation of saturated taxol and taxotere analogues. J. Med. Chem. 37: 3337-3343 (1994)

9. Bradford, M.M. A rapid and sensitive method for the quantification of microgram quantities of protein utilizing the principal of protein-dye binding. Anal. Biochem. 72: 248-254 (1976)


[Seite 100↓]

10. Bradley, J.R., Thiru, S., Pober, J.S. Hydrogen peroxide-induced endothelial retraction is accompanied by a loss of the normal spatial organisation of endothelial cell adhesion molecules. Am. J. Path. 147: 627-641 (1995)

11. Brenner, S.L., Korn, E.D. The effects of cytochalasins on actin polymerisation and actin ATPase provide insights into the mechanism of polymerisation. J. Biol. Chem. 255: 841-844 (1980)

12. Burridge, K. Are stress fibers contractile? Nature 294: 691-692 (1981)

13. Carlier, M.-F., Criquet, P., Pantaloni, D., Korn, E.D. Interaction of cytochalasin D with actin filaments in the presence of ADP and ATP. J. Biol. Chem. 261: 2041-2050 (1986)

14. Cook, T.A., Nagasaki, T., Gundersen, G.G. Rho guanosin triphosphatase mediates the selective stabilisation of microtubules induced by lysophosphatidic acid. J. Cell Biol. 141: 175-185 (1998)

15. Cooper, J.A. Effects of cytochalasin and phalloidin on actin. J. Cell Biol. 105: 1473-1478 (1987)

16. Cooper, J.A., Del Vecchio, P.J., Minnear, K.E., Burhop, K.E., Selig, W.M., Garcia, J.N., Malik, A.B. Measurement of albumin permeability across endothelial monolayers in vitro. J. Appl. Physiol. 62: 1076-1083 (1983)

17. Cronstein, B.N., Molad,Y., Reibmann, J., Balakhane, E., Levine, R.I., Weissmann, G. Colchicine alters the quantitative and qualitative display of selectins on endothelial cells and neutrophils. J. Clin. Invest. 96: 994-1002 (1995)

18. Cross, D., Vial, C., Maccioni, R.B. A tau-like protein interacts with stress fibers and microtubules in human and rodent cultured cell lines. J. Cell Sci. 105: 51-60 (1993)


[Seite 101↓]

19. Danowski, B.A. Fibroblast contractility and actin organisation are stimulated by microtubule inhibitors. J. Cell Sci. 93: 255-266 (1989)

20. Dennerll, T.J., Joshi, H.C., Steel, V.L., Buxbaum, R.E., Heidemann, S.R. Tension and compression in the cytosceleton of PC-12 neurites II: quantitative measurements. J. Cell Biol. 107: 665-674 (1988)

21. Drenckhahn, D., Ness, W. The endothelial contractile cytoskeleton. In: Vascular endothelium: Physiology, pathology, and therapeutic opportunities. Editors: Born, G.V.R., and C.V. Schwartz. F.K. Schattauer, Stuttgart, Germany. 1-26 (1997)

22. Drenckhahn, D., Wagner, J. Stressfibers in the splenic sinus endothelium in situ: molecular structure, relationship to the extracellular matrix and contractility. J. Cell Biol. 102: 1738-1747 (1986)

23. Enomoto, T. Microtubule disruptions induces the formation of actin stress fibers and focal adhesions in cultured cells: possible involvement of the Rho signal cascade. Cell Struc. Func. 21: 317-326 (1996)

24. Ermert, L., Bruckner, H., Walmrath, D., Grimminger, F., Aktories, K., Suttorp, N., Duncker, HR., Seeger, W. Role of endothelial cytoskeleton in high-permeability edema due to botulinum C2 toxin in perfused rabbit lungs. Am. J. Physiol. 268: L753-L761 (1995)

25. Estes, J.E., Selden, L.A., Gershman, L.C. Mechanism of action of phalloidin on the polymerisation of muscle actin. Biochem. 20: 708-712 (1981)

26. Estler, C.J. Spindelgifte. In: Pharmakologie und Toxikologie. Herausgeber: C.J. Estler., F.K. Schattauer, Stuttgart, Germany. 620-621 (1995)


[Seite 102↓]

27. Farrel, K.W., Wilson, L. Proposed mechanism for colchicine poisoning of microtubules reassembled in vitro from Strongylocentrotus purpuratus sperm tail outer doublet tubulin. Biochem. 19: 3048-3054 (1980)

28. Florin, I., Thelestam, M. Lysosomal involvement in cellular intoxication with Clostridium difficile toxin B. Microb. Pathog. 1: 373-385 (1986)

29. Franke, R.P., Gräfe, M., Schnittler, H., Seiffge, D., Mittermayer, C. Induction of human vascular endothelial stress fibers by fluid shear stress. Nature 307: 648-649 (1984)

30. Füchtbauer, A.B., Jokusch, M., Maruta, H., Kiliman, M.W., Isenberg, G. Disruption of microfilaments organisation after injection of F-actin capping proteins into living tissue cultured cells. Nature 304: 361-364 (1983)

31. Füssle, R., Bhakdi, S., Sziegoleit, A., Tranumjensen, J., Kranz, T., Wellensiek, H-J. On the mechanism of membrane damage by Staphylococcus aureus α -Toxin. J. Cell Biol. 91: 83-94 (1981)

32. Fukata, M., Watanabe, T., Noritake, J., Nakagawa, M., Yamaga, M., Kuroda, S., Matsuura, Y., Iwamatsu, A., Perez, F., Kaibuchi, K. Rac1 and Cdc42 capture microtubules through IQGAP1 and CLIP-170 Cell 109: 873-885 (2002)

33. Gail, M.H., Boone, C.W. Effect of colcemid on fibroblast motility. Exp. Cell res. 65: 221-227 (1971)

34. Garcia, J.G.N, Davis, H.W., Patterson, C.E. Regulation of endothelial gap formation and barrier dysfunction: role of myosin light chain phosphorylation. J. Cell Physiol. 163: 510-522 (1995)

35. Gelfand, V. I., Bershadsky, A. D. Microtubule dynamics: mechanism, regulation and function. Annu. Rev. Cell Biol. 7: 93-116 (1991)


[Seite 103↓]

36. Gill, S.R., Schroer, T.A., Szilak, I., Steuer, E.R., Sheetz, M.P. Dynactin, a conserved, ubiquitously expressed component of an activator of vesicle motility mediated by cytoplasmatic dynein. J. Cell Biol. 115: 1639-1650 (1991)

37. Goeckenjan, G. Erkrankungen der Atmungsorgane, Akutes Lungenversagen (ARDS). In: Innere Medizin. Hippokrates Verlag im Georg Thieme Verlag, Stuttgart, Germany, S. 543-547 (1999)

38. Goldblum, S.E., Ding, X., and J. Campbell-Washington. TNF alpha induces endothelial cell F-actin depolymerisation, new actin synthesis, and barrier dysfunction. Am. J. Physiol. 264: C894-C905 (1993)

39. Goldstein, L.S.B., Vale, R.D. New cytoskeletal liasons. Nature 359: 193-194 (1992)

40. Goode, B.L., Drubin, D.G., Barnes, G. Functional cooperation between the microtubule and actin cytoskeletons. Cell Biol. 12: 63-71 (2000)

41. Gottlieb, A.I., Lowell Langille, B., Wong, M.K.K., Kim, D.W. Structure and function of endothelial cytosceleton. Lab. Invest. 65: 123-136 (1991)

42. Gozes, I., Barnstable, C.J. Monoclonal antibodies that recognize discrete forms of tubulin. Proc. Natl. Acad. Sci. 79: 2579-2583 (1982)

43. Griffith, L. M., Pollard, T.D. Evidence for actin filament-microtubule interaction mediated by microtubule-associated proteins. J. Cell Biol. 78: 958-965 (1978)

44. Griffith, L. M., Pollard, T.D. The interaction of actin filaments with microtubules and microtubule-associated proteins. J. Biol. Chem. 257: 9143-9151 (1982)


[Seite 104↓]

45. Gröschel-Stewart, U., Drenckhahn, D. Muscular and cytoplasmic contractile proteins. Biochemistry, Immunology, structural organisation. J. Collagen Rel. Res. 2: 381-463 (1982)

46. Gundersen, G.G., Khawaja, S., Bulinsky, J.C. Generation of a stable, posttranslationally modified microtubule array is an early event in myogenic differentiation. J. Cell Biol. 109: 2275-2288 (1989)

47. Hall, A. Small GTP-binding proteins and the regulation of the actin cytoskeleton. Annu. Rev. Cell Biol. 10: 31-54 (1994)

48. Herman, B., Albertini, D.F. A time-lapse video image intensification analysis of cytoplasmic organelle movements during endosome translocation. J. Cell Biol. 98: 565-576 (1984)

49. Hinsberb, van, V.W.M., Nieuw Amerongen, van, G.P., Draijer, R. Regulation of the permeability of human endothelial cell monolayers. In: Vascular endothelium: Physiology, pathology, and therapeutic opportunities. Editors: Born, G.V.R., and C.V. Schwartz. F.K. Schattauer, Stuttgart, Germany. 6 1-76 (1997)

50. Hippenstiel, S. Bedeutung von Stickstoffmonoxid (NO) und des Phosphodiesterase-Isoenzyms 2 für die Regulation der endothelialen Barriere in vitro. Dissertationsschrift, Giessen 1998

51. Hippenstiel, S., Tannert-Otto, S., Vollrath, N., Krüll, M., Just, I., Aktories, K., von Eichel-Streiber, C., Suttorp, N. Glucosylation of small GTP-binding Rho proteins disrupts endothelial barrier function. Am. J. Physiol. 272: L38-L43 (1997)

52. Hirokawa, N., Pfister, K.K., Yorifuji, H., Wagner, M.C., Brady, S.T., Bloom, G.S. Submolecular domains of bovine brain kinesin identified by electron microscopy and monoclonal antibody decoration. Cell 56: 867-878 (1989)


[Seite 105↓]

53. Hitt, A.L., Cross, A.R., Williams, R.C. Microtubule solutions display nematic liquid crystalline structure. J. Biol. Chem. 265: 1639-1647 (1990)

54. Holzbauer, E.L.F., Hammarback, J.A., Paschal, B.M., Kravit, N.G., Pfister, K.K., Vallee, R.B. Homology of a 150 K cytoplasmatic dynein-associatetd polypeptide with the Drosophila gene Glued. Nature 351: 579-583 (1991)

55. Horwitz, S.B. Mechanism of action of taxol. Trends Pharm. Sci. 13: 134-136 (1992)

56. Ingber, D.E. Cellular tensegrity: defining new rules of biological design that govern the cytoskeleton. J. Cell Sci. 104: 613-627 (1993)

57. Ishizaki, T., Morishima, Y., Okamoto, M., Furuyashiki, T., Kato, T., Narumiya, S. Coordination of microtubules and the actin cytoskeleton by the Rho effector mDia1. Nat. Cell Biol. 3: 8-14 (2001)

58. Jordan, M.A., Himes, R.H., Wilson, L. Comparison of the effects of vinblastine, vincristine, vindesine, and vinepidine on microtubule dynamics and cell proliferation in vitro. Cancer Res. 45: 2741-2747 (1985)

59. Joshi, H.C., Chu, D., Buxbaum, R.E., Heidemann, S. R. Tension and compression in the cytosceleton of PC12 neurites. J. Cell Biol. 101: 697-705 (1985)

60. Just, I., Fritz, G., Aktories, K., Giry, M., Popoff, M.R., Boquet, P., Hegenbarth, S., von Eichel-Streiber, C. Clostridium difficile toxin B acts on the GTP-binding protein Rho. J. Biol. Chem. 269: 10706-10712 (1994)

61. Just, I., Selzer, J., Wilm, M., von Eichel-Streiber, C., Mann, M., Aktories, K. Glucosylation of Rho proteins by Clostridium difficile toxin B. Nature 375: 500-503 (1995)


[Seite 106↓]

62. Knops, J., Kosik, K.S., Lee, G., Pardee, J.D., Cohen-Gould, L., Mc Conlogue, L. Overexpression of tau in a nonneuronal cell induces long cellular processes. J. Cell Biol. 114: 725-733 (1991)

63. Kolodney, M.S., Elson, E.L. Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain. Proc. Natl. Acad. Sci. USA 92: 10252-10256 (1995)

64. Korn, E.D. Actin polymerisation and its regulation by proteins from nonmuscle cells. Physiol. Rev. 62: 672-737 (1982)

65. Krendel, M., Zenke, F.T., Bokoch, G.M. Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton. Nature Cell Biol. 4: 294-301 (2002)

66. Kujpers, T.W., Raleigh, M., Kavanagh, T. Cytokine-activated endothelial cells internalize E-selectin into a lysosomal compartment of vesiculo-tubular shape: a tubulin-driven process. J. Immunol. 152: 5060-5069 (1994)

67. Langanger, G., Moeremans, M., Daneels, G., Sobieszek, A., De Brabander, M., De Mey, J. The molecular organisation of myosin in stress fibers of cultured cells. J. Cell Biol. 102: 200-209 (1986)

68. Lees-Miller, J.P., Helman, D.M., Schroer, T.A. A vertebrate actin-related protein is a component of a multisubunit complex involved in microtubule-based vesicle motility. Nature 359: 244-246 (1992)

69. Lewis, S.A., Cowan, N. Microtubule bundling. Nature 345: 674 (1990)

70. Liu, P.B., Chrzanowska-Wodnicka, M., Burridge, K. Microtubule depolymerisation induces stress fibers, focal adhesions, and DNA synthesis via the GTP-binding protein Rho. Cell Adhes. Commun. 5: 249-255 (1998)


[Seite 107↓]

71. Liu, S.M., Magnusson, K.E., Sundqvist, T. Microtubules are involved in transport of macromolecules by vesicles in cultured bovine aortic endothelial cells. J. Cell Phys. 156: 311-316 (1993)

72. Lodish, H., Baltimore, D., Berk, A., Zipursky, S.L., Matsudaira, P., Darnell, J. Mikrotubuli und Intermediärfilamente. In: Molekulare Zellbiologie. Hrsg. d. Übersetzung: de Gruyter, W., 2. Auflage, Berlin, New York. 1079-1147 (1996)

73. Lodish, H., Baltimore, D., Berk, A., Zipursky, S.L., Matsudaira, P., Darnell, J. Mikrofilamente: Zellbewegung und Zellgestalt. In: Molekulare Zellbiologie. Hrsg. d. Übersetzung: de Gruyter, W., 2. Auflage, Berlin, New York. 1019-1076 (1996)

74. Lum, H., Malik, A.B. Regulation of vascular endothelial barrier function. Am. J. Physiol. 267: L223-L241 (1994)

75. Maccioni, R.B., Cambiazo,V. Role of microtubule-associated proteins in the control of microtubule assembly. Am. Physiol. Soc. 75: 835-864 (1995)

76. Machesky, L.M. , Hall, A. Role of actin polymerisation and adhesion to extracellular matrix in rac- and rho-induced cytosceletal reorganisation. J. Cell Biol. 138: 913-926 (1997)

77. MacRae, T.H. Towards an understanding of microtubule function and cell organisation: an overview. Biochem. Cell Biol. 70: 835-841 (1992)

78. MacRae, T.H., Langdon, C.M. Tubuline synthesis, structure and function: what are the relationships? Biochem. Cell Biol. 67: 770-790 (1989)

79. Mareel, M.M., Storme, G.A., Bruyne, G.K., van Cauwenberge, R.M. Vinblasine, Vincristine and Vindesine: anti-invasive effect on MO4 mouse fibrosarcoma cells in vitro. Eur. J. Cancer Clin. Oncol. 18: 199-210 (1982)


[Seite 108↓]

80. Matteoni, R., Kreis, E. Translocation and clustering of endosomes and lysosomes depends on microtubules. J. Cell Biol. 105: 1253-1265 (1987)

81. McIntosh, J.R., Euteneuer, U. Tubulin hooks as probes for microtubule polarity: an analysis of the method and an evaluation of data on microtubule polarity in the mitotic spindle. J. Cell. Biol. 98: 525-533 (1984)

82. McIntosh, J.R., Porter, M.E. Enzymes for microtubule-dependent motility. J. Biol. Chem. 264: 6001-6004 (1989)

83. Miller, R.H., Lasek, R.J. Cross-bridges mediate anterograde and retrograde vesicle transport along microtubules in squid axoplasm. J. Cell Biol. 101: 2181-2193 (1985)

84. Mitchison, T., Kirschner, M. Dynamic instability of microtubule growth. Nature 312: 237-242 (1984)

85. Mitchison, T., Kirschner, M. Microtubule assembly nucleated by isolated centrosomes. Nature 312: 232-237 (1984)

86. Nishida, E., Kuwaki, T., Sakai, H. Phosphorylation of microtubule-associated proteins (MaPs) and pH of the medium control interaction between MaPs and actin filaments. J. Biochem. 90: 575-578 (1981)

87. Oakley, C.E., Oakley, B.R. Identification of γ-tubuline, a new member of the tubuline superfamily encoded by mipA gene of Aspergillus nidulans. Nature 338: 662-664 (1989)

88. Ohba, S., Kamata, K., Noumura, T.M. Stabilisation of microtubules by dynein-binding in vitro. Stability of microtubule-dynein complex. Biochim. Biophys. Acta 1158: 323-332 (1993)


[Seite 109↓]

89. Oksche, A., Nakov, R., Habermann, E. Morphological and biochemical study of cytosceletal changes in cultured cells after extracellular application of Clostridium novyi alpha-toxin. Infect. Immun. 60: 3002-3006 (1992)

90. Olmsted, J.B. Microtubule-associated Proteins. Annu. Rev. Cell Biol. 2: 421-457 (1986)

91. Olmsted, J.B., Borisy, G.G. Microtubules. Annu. Rev. Biochem. 42: 507-534 (1973)

92. Pelham, H.R.B. Green light for Golgi traffic. Nature 389: 17-19 (1997)

93. Peterson, M.W., Stone, P., Shasby, D.M. Cationic neutrophil proteins increase transendothelial albumin movement. J. Appl. Physiol. 62: 1521-1530 (1987)

94. Pfister, K.K., Wagner, M.C., Stenoien, D.L., Brady, S.T., Bloom, G.S. Monoclonal antibodies to kinesin heavy and light chains stain vesicle-like structures, but not microtubules, in cultured cells. J. Cell Biol. 108: 1453-1463 (1989)

95. Pierre, P., Pepperkok, R. and Kreis, T.E. Molecular characterisation of two functional domains of CLIP-170 in vivo. J. Cell Sci. 107: 1909-1920 (1994)

96. Pierre, P., Scheel, J., Rickard, J.E., Kreis, T.E. CLIP-170 links endocytic vesicles to microtubules. Cell 70: 887-900 (1992)

97. Pletjushkina, O.J., Belkin, A.M., Ivanova, O.J., Oliver, T., Vasiliev, J.M., Jacobson, K. Maturation of cell-substratum focal adhesions induced by depolymerization of microtubules is mediated by increased cortical tension. Cell Adhes. Comm. 5: 121-135 (1996)


[Seite 110↓]

98. Pollard, T.D. Actin and actin-binding proteins. A critical evaluation of mechanisms and functions. Ann. Rev. Biochem. 55: 987-1035 (1986)

99. Pollard, T.D. Assembly and dynamics of the actin filament system in nonmuscle cells. J. Cell Biochem. 31: 87-95 (1986)

100. Pollard, T.D., Selden, S. C., Maupin, P. Interaction of actin filaments with microtubules. J. Cell Biol. 99: 33s-37s (1984)

101. Polley, M. Bedeutung des Zytoskeletts für die Regulation der endothelialen Permeabilität. Dissertationsschrift Gießen 1992

102. Preiß, J., Dornoff, W., Hagmann, F.-G., Schmieder, A. Mammakarzinom. In: Onkologie 2000, Empfehlung zur Therapie. 10. Auflage , Onkologische Arbeits-gemeinschaft Saar-Pfalz-Mosel-E.V., Germany. 152-159 (2000)

103. Pytela, R., and G. Wiche. High molecular weight polypeptides (270,000-340,000) from cultured cells are related to hog brain microtubule-associated proteins but copurify with intermediate filaments. Proc. Natl. Acad. Sci. U.S.A. 77: 4808-4812 (1980)

104. Ren Y., Li, R., Zheng, Y. Busch, H. Cloning and characterisation of GEF-H1, a microtubule-associated guanine nucleotide exchange factor for Rac and Rho GTPases. J. Biol. Chem. 273: 34954-34960 (1998)

105. Rinnerthaler, G., Geiger, B., Small, J.V. Contact formation during fibroblast locomotion: involvement of membran ruffles and microtubules. J. Cell Biol. 106: 747-760 (1988)

106. Ridley, A. J., Hall, A. The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stress fibers in response of growth factors. Cell 70: 389-399 (1992)


[Seite 111↓]

107. Rivera-Fillat, M.P., Pallare-Trujillo, J., Domenech, C., Grau-Oliete, M.R. Comparative uptake, retention and action of vincristine, vinblastine and vindesin on murine leukaemic lymphoblasts sensitive and resistant to vincristine. Br. J. Pharmacol. 93: 902-908 (1988)

108. Rodionov, V.I., Gyoeva, F.K., Tanaka, E., Bershadsky, A.D., Vasiliev, J.M., Gelfand, V.L. Microtubule-dependent control of cell shape and pseudopodial activity is inhibited by the antibody to kinesin motor domain. J. Cell Biol. 123: 1811-1820 (1993)

109. Root, R.K. The adult respiratory distress syndrom. West. J. Med. 150: 187-194 (1989)

110. Roth, P. Wirkungsweise von H2O2 auf das Zytoskelett von pulmonalen Endothelzellen. Dissertationsschrift (1997)

111. Rowinsky, E.K., Cazenave, L.A., Donehower, R.C. Taxol: a novel investigational antimicrotubule agent. J. Natl Cancer Inst. 82: 1247-1259 (1990)

112. Rungger-Brändle, E., Gabbiani, G. The role of cytosceletal and cytocontractile elements in pathologic processes. Am. J. Path. 110: 361-392 (1983)

113. Sattillaro, R.F. Interaction of microtubule-associated protein 2 with actin filaments. Biochemistry 25: 2003-2009 (1986)

114. Schliwa, M. Action of cytochalasin D on cytosceletal networks. J. Cell Biol. 92: 79-91 (1982)

115. Schliwa, M., Blerkom, van, J., Structural interaction of cytosceletal components. J. Cell Biol. 90: 222-235 (1981)

116. Schnittler, H.J., Wilke, A., Gress, T., Suttorp, N., Drenckhahn, D. Role of actin and myosin in the control of paracellular permeability in pig, rat and human vascular endothelium. J. Physiol. 431: 379-401 (1990)


[Seite 112↓]

117. Schroeder, C.C., Fok, A.K., Allen, D. Vesicle transport along microtubule ribbons and isolation of cytoplasmic dynein from Paramecium. J. Cell Biol. 111: 2553-2562 (1990)

118. Schroer, T.A., Sheetz, M.P. Two activators of microtubule-based vesicle transport. J. Cell Biol. 115: 1309-1318 (1991)

119. Schuster, J., Brune, K., Estler, C.J. Colchicin, Stoffeigenschaften und Pharmakodynamik. In: Pharmakologie und Toxikologie. Herausgeber: C.J. Estler, F.K. Schattauer, Stuttgart, Germany. S. 522, (1995)

120. Seeger, W., Bauer, M., Bhakdi, S. Staphylococcal alpha-toxin elicits hypertension in isolated rabbit lungs. Evidence for thromboxan formation and the role of extracellular calcium. J. Clin. Invest. 74: 849-858 (1984)

121. Seeger, W., Lasch, H.G. Respiratorische Insuffizienz. Internist 36: 318-326 (1995)

122. Selden, S.C., Pollard, T.D. Phosphorylation of microtubule-associated proteins regulates their interaction with actin filaments. J. Biol. Chem. 258: 7064-7071 (1983)

123. Seybold, J. Das Zytoskelett der Endothelzelle: Regulation der Aktinfilamente unter dem Einfluss von bakteriellen Toxinen und Tumor-Nekrose-Faktor. Dissertationsschrift (1994)

124. Shasby, D.M., Shasby, S., Sullivan, J.M., Peach, M.J. Role of endothelial cell cytoskeleton in control of endothelial permeability. Circ. Res. 51: 657-661 (1982)

125. Sheridan, C.B., McIntyre, R.C., jr, Meldrum, D.R., Cleveland, J.C., jr, Agrafojo, J., Banerjee, A., Harken, A.H., Fullerton, D.A. Microtubules regulate pulmonary vascular smooth muscle contraction. J. Surg. Res. 62: 284-287 (1996)


[Seite 113↓]

126. Shu,W.P., Wang, D., Stracher, A. Chemical evidence for the existence of activated G-Actin. J. Biochem. 283: 567-573 (1992)

127. Smedly, L.A., Tonnesen, M.G., Sandhaus, R.A., Haslett, C., Guthrie, L.A., Johnses, R.B., jr., Henson, P.M., Worthen, G.S. Neutrophil-mediated injury to endothelial cells. J. Clin. Invest. 77: 1233-1243 (1986)

128. Solomon, F., Magendantz, M. Cytochalasin separates microtubule disassembly from loss of asymmetric morphology. J. cell Biol. 89: 157-161 (1981)

129. Song, Y., Wong, C., Chang, D.D. Overexpression of wild-type RhoA produces growth arrest by disrupting actin cytoskeleton and mikrotubules. J. Cell Biochem. 80: 229-240 (2000)

130. Stossel,T.P., Chapponier, C., Ezzel, R.M., Hartwig, J-H., Janmey, P.A., Kwiatkowski, D.J., Lind, S.E., Smith, D.B., Southwick, F.S., Yin, H.L., Zaner, K.S. Nonmuscle actin-binding proteins. Ann. Rev. Cell Biol. 1: 353-402 (1985)

131. Suprenant, K. A., Dentler, W.L. Association between endocrine pancreatic secretory granules and in-vitro-assembled microtubules is dependent upon microtubule-associated proteins. J. Cell Biol. 93: 164-174 (1982)

132. Suttorp, N. Reaktive Sauerstoffmetabolite und pulmonale Sauerstofftoxizität. Medwelt Vol. 35: 1513-1517 (1984)

133. Suttorp, N. Zellbiologische Untersuchungen zur Pathogenese des akuten Atemnotsyndroms des Erwachsenen (ARDS). Habilitationsschrift, Gießen 1988

134. Suttorp, N., Fuhrmann, M., Tannert-Otto, S., Grimminger, F., Bhakdi, S. Pore-forming bacterial toxins potently induce release of nitric oxide in porcine endothelial cells. J. Exp. Med. 178: 337-341 (1993)


[Seite 114↓]

135. Suttorp, N., Habben, E. Effect of staphylococcal alpha-toxin on intracellular Ca2+ in polymorphonuclear leukocytes. Infect. Immun. 56: 2228-2234 (1988)

136. Suttorp, N., Hessz, T., Seeger, W., Wilke, A., Koob, R., Lutz, F., Drenckhahn, D. Bacterial exotoxins and endothelial permeability for water and albumin in vitro. Am. J. Physiol. 255: C368-C376 (1988)

137. Suttorp, N., Hippenstiel, S., Krüll, M., Seybold, J. Modulation of endothelial permeability by cytosceletal alterations and inhibition of specific phosphodiesterase-isoenzymes. Intern. Soc. Heart Res.: 95-102 (1994)

138. Suttorp, N., Nolte, A., Wilke, A., Drenckhahn, D. Human neutrophil elastase increases permeability of cultured pulmonary endothelial cell monolayers. Int. J. Microcirc. 13: 187-203 (1993)

139. Suttorp, N., Polley, M., Seybold, J., Schnittler, H.J., Seeger, W., Grimminger, F., Aktories, K. Adenosine diphosphate-ribosylation of G-Actin by botulinum C2 toxin increases endothelial permeability in vitro. J. Clin. Invest. 87: 1575-1584 (1991)

140. Suttorp, N., Seeger, W., Dewein, E., Bhakdi, S., Roka, L. Staphylococcal α -Toxin-induced PGI2 production in endothelial cells: role of calcium. Am. J. Physiol. 248: C127-C134 (1985)

141. Suttorp, N., Seeger, W., Zuckermann-Reimann, J., Roka, l., Bhakdi, S. Mechanism of leukotriene generation in polymorphonuclear leukocytes by staphylococcal Alpha-Toxin. Infect. Immun. 55: 104-110 (1987)

142. Suttorp, N., Simon, L.M. Enhancement of polymorphonuclear leukocyte-mediated cytotoxity in lung cells exposed to sustained in vitro hyperoxia. J. Clin. Invest. 70: 342-350 (1982)

143. Suttorp, N., Weber, U., Welsch, T., Schudt, C. Role of phosphodiesterases in the regulation of endothelial permeability in vitro. J. Clin. Invest. 91: 1421-1428 (1993)


[Seite 115↓]

144. Taylor, R.F., Price, T.H., Schwartz, S.M., Dale, D.C. Neutrophil-endothelial cell interactions on endothelial monolayers grown on micropore filters. J. Clin. Invest. 67: 584-587 (1981)

145. Vale, R.D., Goldstein, L.S.B. One motor, many tails: an expending repertoire of force-generating enzymes. Cell 60: 883-885 (1990)

146. Vale, R.D., Hotani, H. Formation of membrane networks in vitro by kinesin-driven microtubule-movement. J. Cell Biol. 107: 2233-2241 (1988)

147. Vallee, R.B., Shpetner, H.S. Motor proteins of cytoplasmatic microtubules. Annu. Rev. Biochem. 59: 909-932 (1990)

148. Vallee, R.B., Wall, J.S., Paschal, B.M., Shpetner, H.S. Microtubule-associated protein 1C from brain is a two-headed cytosolic dynein. Nature 332: 561-563 (1988)

149. Vasiliev, J.M., Gelfand, I.M., Domnina, L.V., Ivanova, O.J., Komm, S.G., Olshevskaja, L.V. Effect of colcemid on the locomotory behaviour of fibroblasts. J. Embryol. Exp. Morph. 24: 625-640 (1970)

150. von Wichert, P. Krankheiten des Lungenkreislaufs - Lungenödem, Lungenstauung. In: Lehrbuch der inneren Medizin. Hrsg. Siegenthaler, W., Kaufmann, W., Hornbostel, H., Waller, H.D., Thieme Verlag Stuttgart: 3. Auflage, 166-167 (1992)

151. Verin, A., Birukova, A., Wang, P., Liu, F., Becker, P., Birukov, K., Garcia, J.G.N. Microtubule disassembly increases endothelial cell barrier dysfunction: role of MLC phosphorylation. Am. J. Physiol. Lung Cell Mol. Physiol. 281: 565-574 (2001)

152. Voet, D., Voet, J. G. Molekulare Physiologie, Cilienbewegung und Vesikeltransport. In: Biochemie. Hrsg. Maelike, A. und W. Müller-Esterl. VCH Verlag, Weinheim, Germany. 1. Auflage 1151-1152 (1992)


[Seite 116↓]

153. Walmrath, D., Grimminger, F., Suttorp, N., Seeger, W. Perspektiven in der Behandlung des Akuten Respiratorischen Distress-Syndroms (ARDS). Med. Welt 45: 414-421 (1995)

154. Weber, U. Die Rolle verschiedener Phosphodiesterase-Isoenzyme für die Regulation der endothelialen Permeabilität. Dissertationsschrift Giessen 1998

155. Whorton, A.R., Montgomery, M.E., Kent, S. Effect of hydrogen peroxide on prostaglandin production and cellular integrity in cultured porcine aortic endothelial cells. J. Clin Invest. 76: 295-302, (1985)

156. Wong, A.J., Pollard, T.D. Actin filament stress fibers in vascular endothelial cells in vivo. Science 219: 867-869 (1983)

157. Wysolmerski, R.B., Lagunoff, D. Inhibition of endothelial cell retraction by ATP depletion. Am. J. Pathol. 132: 28-37 (1988)

158. Wysolmerski, R.B., Lagunoff, D. Involvement of myosin light-chain kinase in endothelial cell retraction. Proc. Natl. Acad. Sci. USA 87: 16-20 (1990)

159. Zhang, D., Wang, Z., Jin, N., Li, L., Rhoades, R.A., Yancey, K.W., Swartz, D.R. Microtubule disruption modulates the Rho-kinase pathway in vascular smooth muscle. J. Muscle Res. Cell Motil. 22: 193-200 (2001)

160. Zheng, Y., Jung, M.K., Oakley, B.R. γ—Tubuline is present in Drosophila melanogaster and Homo sapiens and is associated with the centrosome. Cell 65: 817-823 (1991)

161. Zigmond, S.H. Signal transduction and actin filament organization. Curr. Opin. Cell Biol. 8: 66-73 (1996)


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