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Volumn 161, Issue 12, 1998, Pages 6885-6895

Isolation and characterization of a variant HL60 cell line defective in the activation of the NADPH oxidase by phorbol myristate acetate

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; ENZYME INHIBITOR; MITOGEN ACTIVATED PROTEIN KINASE INHIBITOR; PHORBOL 13 ACETATE 12 MYRISTATE; PHOSPHATIDYLINOSITOL 3 KINASE; POLYPEPTIDE; PROTEIN KINASE C; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE FERRIHEMOPROTEIN REDUCTASE; SUPEROXIDE; WORTMANNIN;

EID: 0032534597     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (36)

References (75)
  • 1
    • 0029171088 scopus 로고
    • The respiratory burst oxidase
    • Babior, B. M. 1995. The respiratory burst oxidase. Curr. Opin. Hematol. 2:55.
    • (1995) Curr. Opin. Hematol. , vol.2 , pp. 55
    • Babior, B.M.1
  • 2
    • 0029099616 scopus 로고
    • Chemoattractant signaling and leukocyte activation
    • Bokoch, G. M. 1995. Chemoattractant signaling and leukocyte activation. Blood 86:1649.
    • (1995) Blood , vol.86 , pp. 1649
    • Bokoch, G.M.1
  • 4
    • 0023807326 scopus 로고
    • Protein phosphorylation and the respiratory burst
    • Babior, B. M. 1988. Protein phosphorylation and the respiratory burst. Arch. Biochem. Biophys. 264:361.
    • (1988) Arch. Biochem. Biophys. , vol.264 , pp. 361
    • Babior, B.M.1
  • 5
    • 0024465665 scopus 로고
    • Protein phosphorylation associated with synergistic stimulation of neutrophils
    • Heyworth, P. G., M. L. Karnovsky, and J. A. Badwey. 1989. Protein phosphorylation associated with synergistic stimulation of neutrophils. J. Biol. Chem. 264: 14935.
    • (1989) J. Biol. Chem. , vol.264 , pp. 14935
    • Heyworth, P.G.1    Karnovsky, M.L.2    Badwey, J.A.3
  • 7
    • 0025166886 scopus 로고
    • Utility of staurosporine in uncovering differences in the signal transduction pathways for superoxide production in neutrophils
    • Robinson, J. M., P. G. Heyworth, and J. A. Badwey. 1990. Utility of staurosporine in uncovering differences in the signal transduction pathways for superoxide production in neutrophils. Biochim. Biophys. Acta 1055:55.
    • (1990) Biochim. Biophys. Acta , vol.1055 , pp. 55
    • Robinson, J.M.1    Heyworth, P.G.2    Badwey, J.A.3
  • 8
    • 0027526348 scopus 로고
    • Protein kinase C isotypes and signal-transduction in human neutrophils: Selective substrate specificity of calcium-dependent β-PKC and novel calcium-independent PKC
    • Majumdar, S., L. H. Kane, M. W. Rossi, B. D. Volpp, W. M. Nauseef, and H. M. Korchak. 1993. Protein kinase C isotypes and signal-transduction in human neutrophils: selective substrate specificity of calcium-dependent β-PKC and novel calcium-independent PKC. Biochim. Biophys. Acta 1176:276.
    • (1993) Biochim. Biophys. Acta , vol.1176 , pp. 276
    • Majumdar, S.1    Kane, L.H.2    Rossi, M.W.3    Volpp, B.D.4    Nauseef, W.M.5    Korchak, H.M.6
  • 9
    • 0028321912 scopus 로고
    • Reciprocal interactions between protein kinase C and components of the NADPH oxidase complex may regulate superoxide production by neutrophils stimulated with a phorbol ester
    • Curnutte, J. T., R. W. Erickson, J. Ding, and J. A. Badwey. 1994. Reciprocal interactions between protein kinase C and components of the NADPH oxidase complex may regulate superoxide production by neutrophils stimulated with a phorbol ester. J. Biol. Chem. 269:10813.
    • (1994) J. Biol. Chem. , vol.269 , pp. 10813
    • Curnutte, J.T.1    Erickson, R.W.2    Ding, J.3    Badwey, J.A.4
  • 12
    • 0031571746 scopus 로고    scopus 로고
    • Opsonized zymosan stimulates the redistribution of protein kinase C isoforms in human neutrophils
    • Sergeant, S., and L. C. McPhail. 1997. Opsonized zymosan stimulates the redistribution of protein kinase C isoforms in human neutrophils. J. Immunol. 159: 2877.
    • (1997) J. Immunol. , vol.159 , pp. 2877
    • Sergeant, S.1    McPhail, L.C.2
  • 13
    • 0030897084 scopus 로고    scopus 로고
    • Kinase-dependcnt activation of the leukocyte NADPH oxidase in a cell-free system
    • Park, J.-W., C. R. Hoyal, J. El Benna, and B. M. Babior. 1997. Kinase-dependcnt activation of the leukocyte NADPH oxidase in a cell-free system. J. Biol. Chem. 272:11035.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11035
    • Park, J.-W.1    Hoyal, C.R.2    El Benna, J.3    Babior, B.M.4
  • 14
    • 0028198653 scopus 로고
    • Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins
    • Bokoch, G. M. 1994. Regulation of the human neutrophil NADPH oxidase by the Rac GTP-binding proteins. Curr. Opinion Cell Biol. 6:212.
    • (1994) Curr. Opinion Cell Biol. , vol.6 , pp. 212
    • Bokoch, G.M.1
  • 15
    • 0029148040 scopus 로고
    • Low-molecular-weight GTP-binding proteins and leukocyte signal transduction
    • Quinn, M. T. 1995. Low-molecular-weight GTP-binding proteins and leukocyte signal transduction. J. Leukocyte Biol. 58:263.
    • (1995) J. Leukocyte Biol. , vol.58 , pp. 263
    • Quinn, M.T.1
  • 16
    • 0025944684 scopus 로고
    • Activation of the NADPH oxidase involves the small GTP-binding protein p21 rac1
    • Abo, A., E. Pick, A. Hall, N. Totty, C. G. Teahan, and A. Segal. 1991. Activation of the NADPH oxidase involves the small GTP-binding protein p21 rac1. Nature 353:668.
    • (1991) Nature , vol.353 , pp. 668
    • Abo, A.1    Pick, E.2    Hall, A.3    Totty, N.4    Teahan, C.G.5    Segal, A.6
  • 17
    • 0026335622 scopus 로고
    • Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac2
    • Knaus, U. G., P. G. Heyworth, T. Evans, J. T. Curnutte, and G. M. Bokoch. 1991. Regulation of phagocyte oxygen radical production by the GTP-binding protein Rac2. Science 254:1512.
    • (1991) Science , vol.254 , pp. 1512
    • Knaus, U.G.1    Heyworth, P.G.2    Evans, T.3    Curnutte, J.T.4    Bokoch, G.M.5
  • 18
    • 0028299331 scopus 로고
    • Activation of NADPH oxidase involves the dissociation of p21rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane
    • Abo, A., M. R. Webb, A. Grogan, and A. W. Segal. 1994. Activation of NADPH oxidase involves the dissociation of p21rac from its inhibitory GDP/GTP exchange protein (rhoGDI) followed by its translocation to the plasma membrane. Biochem. J. 298:585.
    • (1994) Biochem. J. , vol.298 , pp. 585
    • Abo, A.1    Webb, M.R.2    Grogan, A.3    Segal, A.W.4
  • 20
    • 0026795613 scopus 로고
    • Reconstitution of neutrophil NADPH oxidase activity in the cell-free system by four components: P67-phox, p47-phox, p21rac1, and cytochrome b-245
    • Abo, A., A. Boyhan, I. West, A. J. Thrasher, and A. Segal. 1992. Reconstitution of neutrophil NADPH oxidase activity in the cell-free system by four components: p67-phox, p47-phox, p21rac1, and cytochrome b-245. J. Biol. Chem. 267: 16767.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16767
    • Abo, A.1    Boyhan, A.2    West, I.3    Thrasher, A.J.4    Segal, A.5
  • 21
    • 0029731739 scopus 로고    scopus 로고
    • Membrane association of Rac is required for high activity of the respiratory burst oxidase
    • Kreck, M. L., J. L. Freeman, A. Abo, and J. D. Lambeth. 1996. Membrane association of Rac is required for high activity of the respiratory burst oxidase. Biochemistry 35:15683.
    • (1996) Biochemistry , vol.35 , pp. 15683
    • Kreck, M.L.1    Freeman, J.L.2    Abo, A.3    Lambeth, J.D.4
  • 22
    • 0026662445 scopus 로고
    • Inhibition of superoxide production in B lymphocytes by Rac antisense oligonucleotides
    • Dorseuil, O., A. Vazquez, P. Lang, J. Bertoglio, G. Gacon, and G. Leca. 1992. Inhibition of superoxide production in B lymphocytes by Rac antisense oligonucleotides. J. Biol. Chem. 267:20540.
    • (1992) J. Biol. Chem. , vol.267 , pp. 20540
    • Dorseuil, O.1    Vazquez, A.2    Lang, P.3    Bertoglio, J.4    Gacon, G.5    Leca, G.6
  • 23
    • 0028906471 scopus 로고
    • Function of wild-type or mutant Rac2 and Rap1a GTPases in differentiated cell NADPH oxidase activation
    • Gabig, T., C. D. Crean, P. L. Mantel, and R. Rosli. 1995. Function of wild-type or mutant Rac2 and Rap1a GTPases in differentiated cell NADPH oxidase activation. Blood 85:804.
    • (1995) Blood , vol.85 , pp. 804
    • Gabig, T.1    Crean, C.D.2    Mantel, P.L.3    Rosli, R.4
  • 24
    • 0027520431 scopus 로고
    • Translocation of Rac correlates with NADPH oxidase activation. Evidence for equimolar translocation of oxidase components
    • Quinn, M. T., T. Evans, L. R. Loetterle, A. J. Jesaitis, and G. M. Bokoch. 1993. Translocation of Rac correlates with NADPH oxidase activation. Evidence for equimolar translocation of oxidase components. J. Biol. Chem. 268:20983.
    • (1993) J. Biol. Chem. , vol.268 , pp. 20983
    • Quinn, M.T.1    Evans, T.2    Loetterle, L.R.3    Jesaitis, A.J.4    Bokoch, G.M.5
  • 25
    • 0029002363 scopus 로고
    • phox is required for the translocation of Rac1 but not of Rac2 from cytosol to the membranes
    • phox is required for the translocation of Rac1 but not of Rac2 from cytosol to the membranes. Biochem. J. 308:991.
    • (1995) Biochem. J. , vol.308 , pp. 991
    • Dusi, S.1    Donini, M.2    Rossi, F.3
  • 26
    • 0028990158 scopus 로고
    • rac2 from cytosol to plasma membrane is neither necessary nor sufficient for neutrophil NADPH oxidase activity
    • rac2 from cytosol to plasma membrane is neither necessary nor sufficient for neutrophil NADPH oxidase activity. J. Biol. Chem. 270:11514.
    • (1995) J. Biol. Chem. , vol.270 , pp. 11514
    • Philips, M.R.1    Feokstistov, A.2    Pillinger, M.H.3    Abramson, S.B.4
  • 27
    • 0024436756 scopus 로고
    • Transient increase in phosphatidylinositol 3,4 biphosphate and phosphatidyl inositol trisphosphate during activation of human neutrophils
    • Traynor-Kaplan, A. E., B. L. Thompson, A. L. Harris, P. Taylor, G. M. Omann, and L. A. Sklar. 1989. Transient increase in phosphatidylinositol 3,4 biphosphate and phosphatidyl inositol trisphosphate during activation of human neutrophils. J. Biol. Chem. 264:15668.
    • (1989) J. Biol. Chem. , vol.264 , pp. 15668
    • Traynor-Kaplan, A.E.1    Thompson, B.L.2    Harris, A.L.3    Taylor, P.4    Omann, G.M.5    Sklar, L.A.6
  • 28
    • 0027285860 scopus 로고
    • Receptor stimulated accumulation of phosphatidylinositol (3,4,5)-trisphosphate by G-protein mediated pathways in human myeloid derived cells
    • Stephens, L., A. Eguinoa, S. Corey, T. Jackson, and P. T. Hawkins. 1993. Receptor stimulated accumulation of phosphatidylinositol (3,4,5)-trisphosphate by G-protein mediated pathways in human myeloid derived cells. EMBO J. 12:2265.
    • (1993) EMBO J. , vol.12 , pp. 2265
    • Stephens, L.1    Eguinoa, A.2    Corey, S.3    Jackson, T.4    Hawkins, P.T.5
  • 29
    • 0026667731 scopus 로고
    • Chemoattractant-induced tyrosine phosphorylation and activation of microtubule-associated protein kinase in human neutrophils
    • Grinstein, S., and W. Furuya. 1992. Chemoattractant-induced tyrosine phosphorylation and activation of microtubule-associated protein kinase in human neutrophils. J. Biol. Chem. 267:18122.
    • (1992) J. Biol. Chem. , vol.267 , pp. 18122
    • Grinstein, S.1    Furuya, W.2
  • 30
    • 0027462356 scopus 로고
    • The chemotactic factor N-formylmethionyl-leucyl-phenylalanine activates microtubule-associated protein 2 (MAP) kinase and MAP kinase kinase in polymorphonuclear leucocytes
    • Thompson, H. L., M. Shiroo, and J. Saklatvala. 1993. The chemotactic factor N-formylmethionyl-leucyl-phenylalanine activates microtubule-associated protein 2 (MAP) kinase and MAP kinase kinase in polymorphonuclear leucocytes. Biochem. J. 290:483.
    • (1993) Biochem. J. , vol.290 , pp. 483
    • Thompson, H.L.1    Shiroo, M.2    Saklatvala, J.3
  • 31
    • 0027238929 scopus 로고
    • Stimulation of human neutrophils with formyl-methionyl-leucyl-phenylalanine induces tyrosine phosphorylation and activation of distinct mitogen-activated protein-kinases
    • Torres, M., F. L. Hall, and K. O'Neill. 1993. Stimulation of human neutrophils with formyl-methionyl-leucyl-phenylalanine induces tyrosine phosphorylation and activation of distinct mitogen-activated protein-kinases. J. Immunol. 150: 1563.
    • (1993) J. Immunol. , vol.150 , pp. 1563
    • Torres, M.1    Hall, F.L.2    O'Neill, K.3
  • 32
    • 0023714546 scopus 로고
    • Two transduction sequences are necessary for neutrophil activation by receptor agonists
    • Dewald, B., M. Thelen, and M. Baggiolini. 1988. Two transduction sequences are necessary for neutrophil activation by receptor agonists. J. Biol. Chem. 263: 16179.
    • (1988) J. Biol. Chem. , vol.263 , pp. 16179
    • Dewald, B.1    Thelen, M.2    Baggiolini, M.3
  • 33
    • 0027432424 scopus 로고
    • Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: The role of phosphatidylinositol 3,4,5-trisphosphate in neutrophils responses
    • Arcaro, A., and M. Wymann. 1993. Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophils responses. Biochem. J. 296:297.
    • (1993) Biochem. J. , vol.296 , pp. 297
    • Arcaro, A.1    Wymann, M.2
  • 34
    • 0028228654 scopus 로고
    • Wortmannin and 1-butanol block activation of a novel family of protein kinases in neutrophils
    • Ding, J., and J. A. Badwey. 1994. Wortmannin and 1-butanol block activation of a novel family of protein kinases in neutrophils. FEBS Lett. 348:149.
    • (1994) FEBS Lett. , vol.348 , pp. 149
    • Ding, J.1    Badwey, J.A.2
  • 35
    • 0028146616 scopus 로고
    • Blockage of chemotactic peptide-induced stimulation of neutrophils by wortmannin as a result of selective inhibition of phosphatidyl 3-kinase
    • Okada, T., L. Sakuma, Y. Fukui, O. Hazeki, and M. Ui. 1994. Blockage of chemotactic peptide-induced stimulation of neutrophils by wortmannin as a result of selective inhibition of phosphatidyl 3-kinase. J. Biol. Chem. 269:3563.
    • (1994) J. Biol. Chem. , vol.269 , pp. 3563
    • Okada, T.1    Sakuma, L.2    Fukui, Y.3    Hazeki, O.4    Ui, M.5
  • 36
    • 0028321727 scopus 로고
    • Wortmannin binds specifically to 1-phosphatidylinositol 3-kinase while inhibiting guanine nucleotide-binding protein-coupled receptor signaling in neutrophil leukocytes
    • Thelen, M., M. P. Wymann, and H. Langen. 1994. Wortmannin binds specifically to 1-phosphatidylinositol 3-kinase while inhibiting guanine nucleotide-binding protein-coupled receptor signaling in neutrophil leukocytes. Proc. Natl. Acad. Sci. USA 91:4960.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 4960
    • Thelen, M.1    Wymann, M.P.2    Langen, H.3
  • 40
    • 0030821702 scopus 로고    scopus 로고
    • Cytosolic phospholipase A2 and its mode of activation in human neutrophils by opsonized zymosan
    • Hazan, I., R. Dana, Y. Granot, and R. Levy. 1997. Cytosolic phospholipase A2 and its mode of activation in human neutrophils by opsonized zymosan. Biochem. J. 326:867.
    • (1997) Biochem. J. , vol.326 , pp. 867
    • Hazan, I.1    Dana, R.2    Granot, Y.3    Levy, R.4
  • 41
    • 0031573210 scopus 로고    scopus 로고
    • Formyl peptide receptor are coupled to multiple mitogen-activated protein kinase cascades by distinct signal transduction pathways
    • Rane, M. J., S. L. Carrithers, J. M. Arthur, J. B. Klein, and K. R. McLeish. 1997. Formyl peptide receptor are coupled to multiple mitogen-activated protein kinase cascades by distinct signal transduction pathways. J. Immunol. 159:5070.
    • (1997) J. Immunol. , vol.159 , pp. 5070
    • Rane, M.J.1    Carrithers, S.L.2    Arthur, J.M.3    Klein, J.B.4    McLeish, K.R.5
  • 43
    • 0029016789 scopus 로고
    • Dissociation of mitogen-activated protein kinase activation from the oxidative burst in differentiated HL-60 cells and human neutrophils
    • Yu, H. 1995. Dissociation of mitogen-activated protein kinase activation from the oxidative burst in differentiated HL-60 cells and human neutrophils. J. Biol. Chem. 270:15719.
    • (1995) J. Biol. Chem. , vol.270 , pp. 15719
    • Yu, H.1
  • 44
    • 0038903189 scopus 로고    scopus 로고
    • Differential effects of tyrosine kinase inhibitors and an inhibitor of the mitogen-activated protein kinase cascade on degranulation and superoxide production of human neutrophil granulocytes
    • Mócsai, A., B. Bánfi, A. Kapus, G. Farkas, M. Geiszt, L. Buday, A. Faragó, and E. Ligeti. 1997. Differential effects of tyrosine kinase inhibitors and an inhibitor of the mitogen-activated protein kinase cascade on degranulation and superoxide production of human neutrophil granulocytes. Biochem. Pharmacol. 54:781.
    • (1997) Biochem. Pharmacol. , vol.54 , pp. 781
    • Mócsai, A.1    Bánfi, B.2    Kapus, A.3    Farkas, G.4    Geiszt, M.5    Buday, L.6    Faragó, A.7    Ligeti, E.8
  • 45
    • 0030831333 scopus 로고    scopus 로고
    • Inhibition of neutrophil oxidative burst and granule secretion by wortmannin: Potential role of MAP kinase and renaturable kinases
    • Sue-A-Quan, A. K., L. Fialkow, C. J. Vlahos, J. A. Schelm, S. Grinstein, J. Butler, and G. P. Downey. 1997. Inhibition of neutrophil oxidative burst and granule secretion by wortmannin: potential role of MAP kinase and renaturable kinases. J. Cell. Physiol. 172:94.
    • (1997) J. Cell. Physiol. , vol.172 , pp. 94
    • Sue-A-Quan, A.K.1    Fialkow, L.2    Vlahos, C.J.3    Schelm, J.A.4    Grinstein, S.5    Butler, J.6    Downey, G.P.7
  • 46
    • 0031973151 scopus 로고    scopus 로고
    • Comparison of the roles of mitogen-activated protein kinase kinase and phosphatidylinositol 3-kinase signal transduction in neutrophil effector function
    • J. L. J.-W
    • Coffer, P. J., N. Geijsen, L. M'Rabet, R. C. Schweizer, T. Maikoe, J. A. M. Raaijmakers, J. L. J.-W, and L. Koenderman. 1998. Comparison of the roles of mitogen-activated protein kinase kinase and phosphatidylinositol 3-kinase signal transduction in neutrophil effector function. Biochem. J. 329:121.
    • (1998) Biochem. J. , vol.329 , pp. 121
    • Coffer, P.J.1    Geijsen, N.2    M'Rabet, L.3    Schweizer, R.C.4    Maikoe, T.5    Raaijmakers, J.A.M.6    Koenderman, L.7
  • 47
    • 0029967151 scopus 로고    scopus 로고
    • Activation of a p38 mitogen-activated protein kinase in human neutrophils by lipopolysaccharide
    • Nick, J. A., N. J. Avdi, P. Gerwins, G. L. Johnson, and G. Scott Worthen. 1996. Activation of a p38 mitogen-activated protein kinase in human neutrophils by lipopolysaccharide. J. Immunol. 156:4867.
    • (1996) J. Immunol. , vol.156 , pp. 4867
    • Nick, J.A.1    Avdi, N.J.2    Gerwins, P.3    Johnson, G.L.4    Scott Worthen, G.5
  • 48
    • 0030937347 scopus 로고    scopus 로고
    • Common and distinct intracellular signaling pathways in human neutrophils utilized by platelet activating factor and FMLP
    • W. G. S.
    • Nick, J. A., N. J. Avdi, S. K. Young, C. Knall, P. Gerwins, G. L. Johnson, and W. G. S. 1997. Common and distinct intracellular signaling pathways in human neutrophils utilized by platelet activating factor and FMLP. J. Clin. Invest. 99: 975.
    • (1997) J. Clin. Invest. , vol.99 , pp. 975
    • Nick, J.A.1    Avdi, N.J.2    Young, S.K.3    Knall, C.4    Gerwins, P.5    Johnson, G.L.6
  • 49
    • 0029890991 scopus 로고    scopus 로고
    • Activation of MAP kinase-activated protein kinase 2 in human neutrophils after phorbol ester or fMLP peptide stimulation
    • Zu, Y.-L., Y. Ai, A. Gilchrist, M. E. Labadia, R. I. Sha'afi, and C.-K. Huang. 1996. Activation of MAP kinase-activated protein kinase 2 in human neutrophils after phorbol ester or fMLP peptide stimulation. Blood 87:5287.
    • (1996) Blood , vol.87 , pp. 5287
    • Zu, Y.-L.1    Ai, Y.2    Gilchrist, A.3    Labadia, M.E.4    Sha'afi, R.I.5    Huang, C.-K.6
  • 50
    • 0031012781 scopus 로고    scopus 로고
    • Chemotactic peptide N-formyl-Met-Leu-Phe activation of p38 mitogen-activated protein kinase (MAPK) and MAPK-activated protein kinase-2 in human neutrophils
    • Krump, E., J. S. Sanghera, S. L. Pelech, W. Furuya, and S. Grinstein. 1997. Chemotactic peptide N-formyl-Met-Leu-Phe activation of p38 mitogen-activated protein kinase (MAPK) and MAPK-activated protein kinase-2 in human neutrophils. J. Biol. Chem. 272:937.
    • (1997) J. Biol. Chem. , vol.272 , pp. 937
    • Krump, E.1    Sanghera, J.S.2    Pelech, S.L.3    Furuya, W.4    Grinstein, S.5
  • 51
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K., and M. Favre. 1973. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
    • (1973) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1    Favre, M.2
  • 52
    • 0027231533 scopus 로고
    • Agonist-dependent phosphorylation of N-formyl peptide and activation peptide from the fifth component of C (C5a) chemoattractant receptors in differentiated HL60 cells
    • Tardif, M., L. Mery, L. Brouchon, and F. Boulay. 1993. Agonist-dependent phosphorylation of N-formyl peptide and activation peptide from the fifth component of C (C5a) chemoattractant receptors in differentiated HL60 cells. J. Immunol. 150:3534.
    • (1993) J. Immunol. , vol.150 , pp. 3534
    • Tardif, M.1    Mery, L.2    Brouchon, L.3    Boulay, F.4
  • 54
    • 0028168429 scopus 로고
    • Protein kinase C-β is required for macrophage differentiation of human HL-60 leukemia cells
    • Tonetti, D. A., C. Henning-Chubb, D. T. Yamanishi, and E. Huberman. 1994. Protein kinase C-β is required for macrophage differentiation of human HL-60 leukemia cells. J. Biol. Chem. 269:23230.
    • (1994) J. Biol. Chem. , vol.269 , pp. 23230
    • Tonetti, D.A.1    Henning-Chubb, C.2    Yamanishi, D.T.3    Huberman, E.4
  • 56
    • 0027322679 scopus 로고
    • Protein kinase C isoenzymes: Divergence in signal transduction?
    • Hug, H., and T. F. Sarre. 1993. Protein kinase C isoenzymes: divergence in signal transduction? Biochem. J. 291:329.
    • (1993) Biochem. J. , vol.291 , pp. 329
    • Hug, H.1    Sarre, T.F.2
  • 57
    • 0031578232 scopus 로고    scopus 로고
    • Translocation of protein kinase C isoforms in rat neutrophils
    • Tsao, L.-T., and J.-P. Wang. 1997. Translocation of protein kinase C isoforms in rat neutrophils. Biochem. Biophys. Res. Commun. 234:412.
    • (1997) Biochem. Biophys. Res. Commun. , vol.234 , pp. 412
    • Tsao, L.-T.1    Wang, J.-P.2
  • 58
    • 0027281298 scopus 로고
    • Heterogeneity of protein kinase C isoform expression in chemically induced HL60 cells
    • Seibenhener, M. L., and M. W. Wooten. 1993. Heterogeneity of protein kinase C isoform expression in chemically induced HL60 cells. Exp. Cell Res. 207:183.
    • (1993) Exp. Cell Res. , vol.207 , pp. 183
    • Seibenhener, M.L.1    Wooten, M.W.2
  • 59
    • 0030423479 scopus 로고    scopus 로고
    • Differential expression of protein kinase C isozymes and small GTP-binding proteins during HL60 cell differentiation by retinoic acid and cyclic AMP: Relation with phospholipase D (PLD) activation
    • Nakashima, S., Y. Iwasaki, T. Mizutani, K. Ohguchi, K. Nagata, Y. Kitajima, and Y. Nozawa. 1996. Differential expression of protein kinase C isozymes and small GTP-binding proteins during HL60 cell differentiation by retinoic acid and cyclic AMP: relation with phospholipase D (PLD) activation. Immunobiology 196:588.
    • (1996) Immunobiology , vol.196 , pp. 588
    • Nakashima, S.1    Iwasaki, Y.2    Mizutani, T.3    Ohguchi, K.4    Nagata, K.5    Kitajima, Y.6    Nozawa, Y.7
  • 60
    • 0027986577 scopus 로고
    • Wortmannin inhibits mitogen-activated protein kinase activation induced by platelet-activating factor in guinea pig neutrophils
    • Ferby, I. M., I. Waga, C. Sakanaka, K. Kume, and T. Shimizu. 1994. Wortmannin inhibits mitogen-activated protein kinase activation induced by platelet-activating factor in guinea pig neutrophils. J. Biol. Chem. 269:30485.
    • (1994) J. Biol. Chem. , vol.269 , pp. 30485
    • Ferby, I.M.1    Waga, I.2    Sakanaka, C.3    Kume, K.4    Shimizu, T.5
  • 62
    • 0030718609 scopus 로고    scopus 로고
    • Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells
    • Takaishi, K., T. Sasaki, H. Kotani, H. Nishioka, and Y. Takai. 1997. Regulation of cell-cell adhesion by Rac and Rho small G proteins in MDCK cells. J. Cell Biol. 139:1047.
    • (1997) J. Cell Biol. , vol.139 , pp. 1047
    • Takaishi, K.1    Sasaki, T.2    Kotani, H.3    Nishioka, H.4    Takai, Y.5
  • 64
    • 0028157617 scopus 로고
    • The requirement of p47 phosphorylation for activation of NADPH oxidase by opsonized zymosan in human neutrophils
    • Levy, R., R. Dana, T. L. Leto, and H. L. Malech. 1994. The requirement of p47 phosphorylation for activation of NADPH oxidase by opsonized zymosan in human neutrophils. Biochim. Biophys. Acta 1220:253.
    • (1994) Biochim. Biophys. Acta , vol.1220 , pp. 253
    • Levy, R.1    Dana, R.2    Leto, T.L.3    Malech, H.L.4
  • 65
    • 0030892639 scopus 로고    scopus 로고
    • Protein kinase C-ζ mediates angiotensin II activation of ERK1/2 in vascular smooth muscle cells
    • Liao, D.-F., B. Monia, N. Dean, and B. C. Berk. 1997. Protein kinase C-ζ mediates angiotensin II activation of ERK1/2 in vascular smooth muscle cells. J. Biol. Chem. 272:6146.
    • (1997) J. Biol. Chem. , vol.272 , pp. 6146
    • Liao, D.-F.1    Monia, B.2    Dean, N.3    Berk, B.C.4
  • 67
    • 0039791449 scopus 로고    scopus 로고
    • Activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by conventional, novel, and atypical protein kinase C isotypes
    • Schönwasser, D. C., R. M. Marais, C. J. Marshall, and P. J. Parker. 1998. Activation of the mitogen-activated protein kinase/extracellular signal-regulated kinase pathway by conventional, novel, and atypical protein kinase C isotypes. Mol. Cell. Biol. 18:790.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 790
    • Schönwasser, D.C.1    Marais, R.M.2    Marshall, C.J.3    Parker, P.J.4
  • 68
    • 0030048490 scopus 로고    scopus 로고
    • Interleukin-8 regulation of the Ras/Raf/mitogen-activated protein kinase pathway in human neutrophils
    • Knall, C., S. Young, J. A. Nick, A. M. Buhl, G. S. Worthen, and G. L. Johnson. 1996. Interleukin-8 regulation of the Ras/Raf/mitogen-activated protein kinase pathway in human neutrophils. J. Biol. Chem. 271:2832.
    • (1996) J. Biol. Chem. , vol.271 , pp. 2832
    • Knall, C.1    Young, S.2    Nick, J.A.3    Buhl, A.M.4    Worthen, G.S.5    Johnson, G.L.6
  • 69
    • 0030823258 scopus 로고    scopus 로고
    • The phosphatidylinositol 3-kinase inhibitor wortmannin markedly reduces chemotactic peptide-induced locomotion and increases in cytoskeletal actin in human neutrophils
    • Niggli, V., and H. Keller. 1997. The phosphatidylinositol 3-kinase inhibitor wortmannin markedly reduces chemotactic peptide-induced locomotion and increases in cytoskeletal actin in human neutrophils. Eur. J. Pharmacol. 355:43.
    • (1997) Eur. J. Pharmacol. , vol.355 , pp. 43
    • Niggli, V.1    Keller, H.2
  • 70
    • 0028875683 scopus 로고
    • Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation
    • Bagrodia, S., B. Dérijard, R. J. Davis, and R. A. Cerione. 1995. Cdc42 and PAK-mediated signaling leads to Jun kinase and p38 mitogen-activated protein kinase activation. J. Biol. Chem. 270:27995.
    • (1995) J. Biol. Chem. , vol.270 , pp. 27995
    • Bagrodia, S.1    Dérijard, B.2    Davis, R.J.3    Cerione, R.A.4
  • 71
    • 0029070887 scopus 로고
    • Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs
    • Minden, A., A. Lin, F.-X. Claret, A. Abo, and M. Karin. 1995. Selective activation of the JNK signaling cascade and c-Jun transcriptional activity by the small GTPases Rac and Cdc42Hs. Cell 81:1147.
    • (1995) Cell , vol.81 , pp. 1147
    • Minden, A.1    Lin, A.2    Claret, F.-X.3    Abo, A.4    Karin, M.5
  • 72
    • 0028820587 scopus 로고
    • Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1
    • Zhang, S., J. Han, M. A. Sells, J. Chernoff, U. G. Knaus, R. J. Ulevitch, and G. M. Bokoch. 1995. Rho family GTPases regulate p38 mitogen-activated protein kinase through the downstream mediator Pak1. J. Biol. Chem. 270:23934.
    • (1995) J. Biol. Chem. , vol.270 , pp. 23934
    • Zhang, S.1    Han, J.2    Sells, M.A.3    Chernoff, J.4    Knaus, U.G.5    Ulevitch, R.J.6    Bokoch, G.M.7
  • 73
    • 0028998794 scopus 로고
    • Regulation of human leukocytes p21-activated kinases through G protein-coupled receptors
    • Knaus, U. G., S. Morris, H.-J. Dong, J. Chernoff, and G. M. Bokoch. 1995. Regulation of human leukocytes p21-activated kinases through G protein-coupled receptors. Science 269:221.
    • (1995) Science , vol.269 , pp. 221
    • Knaus, U.G.1    Morris, S.2    Dong, H.-J.3    Chernoff, J.4    Bokoch, G.M.5
  • 74
    • 0028961293 scopus 로고
    • Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C. D., and A. Hall. 1995. Rho, Rac, and Cdc42 GTPases regulate the assembly of multimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell 81:53.
    • (1995) Cell , vol.81 , pp. 53
    • Nobes, C.D.1    Hall, A.2
  • 75
    • 0031974716 scopus 로고    scopus 로고
    • The small GTP-binding protein Rac promotes the dissociation of gelsolin from actin filaments in neutrophils
    • Arcaro, A. 1998. The small GTP-binding protein Rac promotes the dissociation of gelsolin from actin filaments in neutrophils. J. Biol. Chem. 273:805.
    • (1998) J. Biol. Chem. , vol.273 , pp. 805
    • Arcaro, A.1


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