메뉴 건너뛰기




Volumn 116, Issue 5, 2003, Pages 813-822

Microtubule-disruption-induced and chemotactic-peptide-induced migration of human neutrophils: Implications for differential sets of signalling pathways

Author keywords

Microtubule; Migration; Neutrophil; Phosphatidylinositol 3 kinase; Rho; Rho kinase

Indexed keywords

4 (1 AMINOETHYL) N (4 PYRIDYL)CYCLOHEXANECARBOXAMIDE; ACTIN; ALPHA ACTININ; CHEMOTACTIC PEPTIDE; COLCHICINE; F ACTIN; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; MYOSIN LIGHT CHAIN; PACLITAXEL; PERTUSSIS TOXIN; PHOSPHATIDYLINOSITOL 3 KINASE; RHO KINASE; WORTMANNIN;

EID: 0037350970     PISSN: 00219533     EISSN: None     Source Type: Journal    
DOI: 10.1242/jcs.00306     Document Type: Review
Times cited : (96)

References (40)
  • 1
    • 0019184392 scopus 로고
    • Prevention of degradation of human polymorphonuclear leukocyte proteins by diisopropyl-fluorophosphate
    • Amrein, P. C. and Stossel, T. P. (1980). Prevention of degradation of human polymorphonuclear leukocyte proteins by diisopropyl-fluorophosphate. Blood 56, 442-447.
    • (1980) Blood , vol.56 , pp. 442-447
    • Amrein, P.C.1    Stossel, T.P.2
  • 2
    • 0000539176 scopus 로고
    • Separation of leukocytes from blood and bone marrow
    • Böyum, A. (1968). Separation of leukocytes from blood and bone marrow. Scand. J. Clin. Lab. Invest. 21, 1-89.
    • (1968) Scand. J. Clin. Lab. Invest. , vol.21 , pp. 1-89
    • Böyum, A.1
  • 3
    • 0035449609 scopus 로고    scopus 로고
    • Signaling pathways controlling cell polarity and chemotaxis
    • Chung, C. Y., Funamoto, S. and Firtel, R. A. (2001). Signaling pathways controlling cell polarity and chemotaxis. Trends Biochem. Sci. 26, 557-566.
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 557-566
    • Chung, C.Y.1    Funamoto, S.2    Firtel, R.A.3
  • 4
    • 0029864685 scopus 로고    scopus 로고
    • Mechanisms of NADPH oxidase activation: Translocation of p40phox, Rac1 and Rac2 from the cytosol to the membranes in human neutrophils lacking p47phox or p67phox
    • Dusi, S., Donini, M. and Rossi, F. (1996). Mechanisms of NADPH oxidase activation: translocation of p40phox, Rac1 and Rac2 from the cytosol to the membranes in human neutrophils lacking p47phox or p67phox. Biochem. J 314, 409-412.
    • (1996) Biochem. J. , vol.314 , pp. 409-412
    • Dusi, S.1    Donini, M.2    Rossi, F.3
  • 5
    • 0019230472 scopus 로고
    • Effect of antitubulins of spontaneous and chemotactic migration of neutrophils under agarose
    • Dziezanowski, M. A., DeStefano, M. J. and Rabinovitch, M. (1980). Effect of antitubulins of spontaneous and chemotactic migration of neutrophils under agarose. J. Cell Sci. 42, 379-388.
    • (1980) J. Cell Sci. , vol.42 , pp. 379-388
    • Dziezanowski, M.A.1    DeStefano, M.J.2    Rabinovitch, M.3
  • 6
    • 0029089841 scopus 로고
    • ADP-ribosylation of Rho enhances actin polymerization-coupled shape oscillations in human neutrophils
    • Ehrengruber, M. U., Boquet, P., Coates, T. D. and Deranleau, D. A. (1995). ADP-ribosylation of Rho enhances actin polymerization-coupled shape oscillations in human neutrophils. FEBS Lett. 372, 161-164.
    • (1995) FEBS Lett. , vol.372 , pp. 161-164
    • Ehrengruber, M.U.1    Boquet, P.2    Coates, T.D.3    Deranleau, D.A.4
  • 7
    • 0030462929 scopus 로고    scopus 로고
    • Microtubule disruption induces the formation of actin stress fibers and focal adhesions in cultured cells: Possible involvement of the Rho signal cascade
    • Enomoto, T. (1996). Microtubule disruption induces the formation of actin stress fibers and focal adhesions in cultured cells: possible involvement of the Rho signal cascade. Cell Struct. Funct. 21, 317-326.
    • (1996) Cell Struct. Funct. , vol.21 , pp. 317-326
    • Enomoto, T.1
  • 8
    • 0018902785 scopus 로고
    • Optimal conditions for simultaneous purification of mononuclear and polymorphonuclear leucocytes from human blood by the Hypaque-Ficoll method
    • Ferrante, A. and Thong, Y. H. (1980). Optimal conditions for simultaneous purification of mononuclear and polymorphonuclear leucocytes from human blood by the Hypaque-Ficoll method. J. Immunol. Methods 36, 109-117.
    • (1980) J. Immunol. Methods , vol.36 , pp. 109-117
    • Ferrante, A.1    Thong, Y.H.2
  • 10
    • 0027221483 scopus 로고
    • Cellular tensegrity: Defining new rules of biological design that govern the cytoskeleton
    • Ingber, D. E. (1993). Cellular tensegrity: defining new rules of biological design that govern the cytoskeleton. J. Cell Sci. 106, 613-627.
    • (1993) J. Cell Sci. , vol.106 , pp. 613-627
    • Ingber, D.E.1
  • 12
    • 0027258699 scopus 로고
    • Colchicine-induced stimulation of PMN motility related to cytoskeletal changes in actin, α-actinin, and myosin
    • Keller, H. U. and Niggli, V. (1993). Colchicine-induced stimulation of PMN motility related to cytoskeletal changes in actin, α-actinin, and myosin. Cell Motil. Cytoskel. 25, 10-18.
    • (1993) Cell Motil. Cytoskel. , vol.25 , pp. 10-18
    • Keller, H.U.1    Niggli, V.2
  • 13
    • 0021164914 scopus 로고
    • Effects of colchicine, vinblastine and nocodazole on polarity, motility, chemotaxis and cAMP levels of human polymorphonuclear leukocytes
    • Keller, H. U., Naef, A. and Zimmermann, A. (1984). Effects of colchicine, vinblastine and nocodazole on polarity, motility, chemotaxis and cAMP levels of human polymorphonuclear leukocytes. Exp. Cell Res. 153, 173-185.
    • (1984) Exp. Cell Res. , vol.153 , pp. 173-185
    • Keller, H.U.1    Naef, A.2    Zimmermann, A.3
  • 14
    • 0030903025 scopus 로고    scopus 로고
    • Interleukin 8-stimulated phosphatidylinositol-3-kinase activity regulates the migration of human neutrophils independent of extracellular signal-regulated kinase and p38 mitogen-activated protein kinases
    • Knall, C., Worthen, G. S. and Johnson, G. L. (1997). Interleukin 8-stimulated phosphatidylinositol-3-kinase activity regulates the migration of human neutrophils independent of extracellular signal-regulated kinase and p38 mitogen-activated protein kinases. Proc. Natl. Acad. Sci. USA 94, 3052-3057.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3052-3057
    • Knall, C.1    Worthen, G.S.2    Johnson, G.L.3
  • 15
    • 0028800221 scopus 로고
    • Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain
    • Kolodney, M. S. and Elson, E. L. (1995). Contraction due to microtubule disruption is associated with increased phosphorylation of myosin regulatory light chain. Proc. Natl. Acad. Sci. USA 92, 10252-10256.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 10252-10256
    • Kolodney, M.S.1    Elson, E.L.2
  • 16
    • 0036228955 scopus 로고    scopus 로고
    • Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton
    • Krendel, M., Zenke, F. T. and Bokoch, G. M. (2002). Nucleotide exchange factor GEF-H1 mediates cross-talk between microtubules and the actin cytoskeleton. Nat. Cell Biol. 4, 294-301.
    • (2002) Nat. Cell Biol. , vol.4 , pp. 294-301
    • Krendel, M.1    Zenke, F.T.2    Bokoch, G.M.3
  • 17
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. (1970). Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 18
    • 0032454273 scopus 로고    scopus 로고
    • Microtubule depolymerization induces stress fibers, focal adhesions, and DNA synthesis via the GTP-binding protein Rho
    • Liu, B. P., Chrzanowska-Wodnicka, M. and Burridge, K. (1998). Microtubule depolymerization induces stress fibers, focal adhesions, and DNA synthesis via the GTP-binding protein Rho. Cell Adhes. Commun. 5, 249-255.
    • (1998) Cell Adhes. Commun. , vol.5 , pp. 249-255
    • Liu, B.P.1    Chrzanowska-Wodnicka, M.2    Burridge, K.3
  • 19
    • 0033555288 scopus 로고    scopus 로고
    • Monosodium urate-crystal-stimulated phospholipase D in human neutrophils
    • Marcil, J., Harbour, D., Houle, M. G., Naccache, P. H. and Bourgoin, S. (1999). Monosodium urate-crystal-stimulated phospholipase D in human neutrophils. Biochem. J. 337, 185-192.
    • (1999) Biochem. J. , vol.337 , pp. 185-192
    • Marcil, J.1    Harbour, D.2    Houle, M.G.3    Naccache, P.H.4    Bourgoin, S.5
  • 20
    • 0032991828 scopus 로고    scopus 로고
    • Rho-kinase in human neutrophils: A role in signalling for myosin light chain phosphorylation and cell migration
    • Niggli, V. (1999). Rho-kinase in human neutrophils: a role in signalling for myosin light chain phosphorylation and cell migration. FEBS Lett. 445, 69-72.
    • (1999) FEBS Lett. , vol.445 , pp. 69-72
    • Niggli, V.1
  • 21
    • 0034640350 scopus 로고    scopus 로고
    • 3) is an activator of human neutrophil migration
    • 3) is an activator of human neutrophil migration. FEBS Lett. 473, 217-221.
    • (2000) FEBS Lett. , vol.473 , pp. 217-221
    • Niggli, V.1
  • 22
    • 0030823258 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitor wortmannin markedly reduces chernotactic peptide-induced locomotion and increases in cytoskeletal actin in human neutrophils
    • Niggli, V. and Keller, H. U. (1997). The phosphatidylinositol 3-kinase inhibitor wortmannin markedly reduces chernotactic peptide-induced locomotion and increases in cytoskeletal actin in human neutrophils. Eur. J. Pharmacol. 335, 43-52.
    • (1997) Eur. J. Pharmacol. , vol.335 , pp. 43-52
    • Niggli, V.1    Keller, H.U.2
  • 23
    • 0030614363 scopus 로고    scopus 로고
    • Tubulin, Gq, and phosphatidylinositol 4,5-bisphosphate interact to regulate phospholipase Cβ1 signaling
    • Popova, J. S., Garrison, J. C., Rhee, S. G. and Rasenick, M. M. (1997). Tubulin, Gq, and phosphatidylinositol 4,5-bisphosphate interact to regulate phospholipase Cβ1 signaling. J. Biol. Chem. 272, 6760-6765.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6760-6765
    • Popova, J.S.1    Garrison, J.C.2    Rhee, S.G.3    Rasenick, M.M.4
  • 24
    • 0033104860 scopus 로고    scopus 로고
    • Dephosphorylation of the catenins p120 and p100 in endothelial cells in response to inflammatory stimuli
    • Ratcliffe, M. J., Smales, C. and Staddon, J. M. (1999). Dephosphorylation of the catenins p120 and p100 in endothelial cells in response to inflammatory stimuli. Biochem. J. 338, 471-478.
    • (1999) Biochem. J. , vol.338 , pp. 471-478
    • Ratcliffe, M.J.1    Smales, C.2    Staddon, J.M.3
  • 25
    • 0033081753 scopus 로고    scopus 로고
    • Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton
    • Ren, X. D., Kiosses, W. B. and Schwartz, M. A. (1999). Regulation of the small GTP-binding protein Rho by cell adhesion and the cytoskeleton. EMBO J. 18, 578-585.
    • (1999) EMBO J. , vol.18 , pp. 578-585
    • Ren, X.D.1    Kiosses, W.B.2    Schwartz, M.A.3
  • 26
    • 0034332904 scopus 로고    scopus 로고
    • Leukocytes navigate by compass: Roles of PI3Kγ and its lipid products
    • Rickert, P., Weiner, O. D., Wang, F., Bourne, H. R. and Servant, G. (2000). Leukocytes navigate by compass: roles of PI3Kγ and its lipid products. Trends Cell Biol. 10, 466-473.
    • (2000) Trends Cell Biol. , vol.10 , pp. 466-473
    • Rickert, P.1    Weiner, O.D.2    Wang, F.3    Bourne, H.R.4    Servant, G.5
  • 28
    • 0032488925 scopus 로고    scopus 로고
    • Microtubule integrity regulates Src-like and extracellular signal-regulated kinase activities in human pro-monocytic cells
    • Schmid-Alliana, A., Menou, L., Manié, S., Schmid-Antomarchi, H., Millet, M., Giuriato, S., Ferrua, B. and Rossi, B. (1998). Microtubule integrity regulates Src-like and extracellular signal-regulated kinase activities in human pro-monocytic cells. J. Biol. Chem. 273, 3394-3400.
    • (1998) J. Biol. Chem. , vol.273 , pp. 3394-3400
    • Schmid-Alliana, A.1    Menou, L.2    Manié, S.3    Schmid-Antomarchi, H.4    Millet, M.5    Giuriato, S.6    Ferrua, B.7    Rossi, B.8
  • 29
    • 0034650714 scopus 로고    scopus 로고
    • Signal transduction by G-proteins, Rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II
    • Somlyo, A. F. and Somlyo, A. V. (2000). Signal transduction by G-proteins, Rho-kinase and protein phosphatase to smooth muscle and non-muscle myosin II. J. Physiol. 522, 177-185.
    • (2000) J. Physiol. , vol.522 , pp. 177-185
    • Somlyo, A.F.1    Somlyo, A.V.2
  • 30
    • 0036532121 scopus 로고    scopus 로고
    • Roles of PI3Ks in leukocyte chemotaxis and phagocytosis
    • Stephens, L., Ellson, C. and Hawkins, P. (2002). Roles of PI3Ks in leukocyte chemotaxis and phagocytosis. Curr. Opin. Cell Biol. 14, 203-213.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 203-213
    • Stephens, L.1    Ellson, C.2    Hawkins, P.3
  • 31
    • 0033603660 scopus 로고    scopus 로고
    • Cellular redistribution of PKCα, rhoA and Rokα following smooth muscle agonist stimulation
    • Taggart, M. J., Lee, Y. H. and Morgan, K. G. (1999). Cellular redistribution of PKCα, rhoA and Rokα following smooth muscle agonist stimulation. Exp. Cell Research 251, 92-101.
    • (1999) Exp. Cell Research , vol.251 , pp. 92-101
    • Taggart, M.J.1    Lee, Y.H.2    Morgan, K.G.3
  • 32
    • 0037181495 scopus 로고    scopus 로고
    • Dephosphorylation of the two regulatory components of myosin phosphatase, MBS and CPI17
    • Takizawa, N., Niiro, N. and Ikebe, M. (2002). Dephosphorylation of the two regulatory components of myosin phosphatase, MBS and CPI17. FEBS Lett. 515, 127-132.
    • (2002) FEBS Lett. , vol.515 , pp. 127-132
    • Takizawa, N.1    Niiro, N.2    Ikebe, M.3
  • 33
    • 0028836520 scopus 로고
    • The role of microtubule dynamics in growth cone motility and axonal growth
    • Tanaka, E., Ho, T., Kirschner, M. W. (1995). The role of microtubule dynamics in growth cone motility and axonal growth. I Cell Biol. 128, 139-155.
    • (1995) J. Cell Biol. , vol.128 , pp. 139-155
    • Tanaka, E.1    Ho, T.2    Kirschner, M.W.3
  • 34
    • 0031861746 scopus 로고    scopus 로고
    • Passive mechanical behavior of human neutrophils: Effects of colchicine and paclitaxel
    • Tsai, M. A., Waugh, R. E. and Keng, P. C. (1998). Passive mechanical behavior of human neutrophils: effects of colchicine and paclitaxel. Biophys. J. 74, 3282-3291.
    • (1998) Biophys. J. , vol.74 , pp. 3282-3291
    • Tsai, M.A.1    Waugh, R.E.2    Keng, P.C.3
  • 38
    • 0036532115 scopus 로고    scopus 로고
    • Regulation of cell polarity during eukaryotic chemotaxis: The chemotactic compass
    • Weiner, O. D. (2002). Regulation of cell polarity during eukaryotic chemotaxis: the chemotactic compass. Curr. Opin. Cell Biol. 14, 196-202.
    • (2002) Curr. Opin. Cell Biol. , vol.14 , pp. 196-202
    • Weiner, O.D.1
  • 39
    • 0035178210 scopus 로고    scopus 로고
    • Cell motility, can Rho GTPases and microtubules point the way?
    • Wittmann, T. and Waterman-Storer, C. M. (2001). Cell motility, can Rho GTPases and microtubules point the way? J. Cell Sci. 114, 3795-3803.
    • (2001) J. Cell Sci. , vol.114 , pp. 3795-3803
    • Wittmann, T.1    Waterman-Storer, C.M.2
  • 40
    • 0017660115 scopus 로고
    • Ability of polymorphonuclear leukocytes to orient in gradients of chemotactic factors
    • Zigmond, S. H. (1977). Ability of polymorphonuclear leukocytes to orient in gradients of chemotactic factors. J. Cell Biol. 75, 606-616.
    • (1977) J. Cell Biol. , vol.75 , pp. 606-616
    • Zigmond, S.H.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.