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Volumn 164, Issue 1, 2000, Pages 404-411

fMet-Leu-Phe stimulates proinflammatory cytokine gene expression in human peripheral blood monocytes: The role of phosphatidylinositol 3-kinase

Author keywords

[No Author keywords available]

Indexed keywords

2 MORPHOLINO 8 PHENYLCHROMONE; CYTOKINE; IMMUNOGLOBULIN ENHANCER BINDING PROTEIN; INTERLEUKIN 1; LEUCINE; METHIONINE; PHENYLALANINE; PHOSPHATIDYLINOSITOL 3 KINASE; WORTMANNIN;

EID: 0033975860     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: 10.4049/jimmunol.164.1.404     Document Type: Article
Times cited : (60)

References (49)
  • 1
    • 0011079304 scopus 로고
    • Cellular and molecular mechanisms of inflammation
    • C. G. Cochrane and J. A. Gimbrone, eds. Academic Press, New York
    • Allen, R. A., A. J. Jekaitis, and C. G. Cochrane. 1990. Cellular and molecular mechanisms of inflammation. In Cellular and Molecular Mechanisms of Inflammation. C. G. Cochrane and J. A. Gimbrone, eds. Academic Press, New York, p. 83.
    • (1990) Cellular and Molecular Mechanisms of Inflammation , pp. 83
    • Allen, R.A.1    Jekaitis, A.J.2    Cochrane, C.G.3
  • 2
    • 0011115337 scopus 로고
    • Inflammation: Basic principles and clinical correlates
    • J. I. Gallin, I. M. Goldstein, and R. Snyderman, eds. Raven Press, New York
    • Snyderman, R., and R. J. Uhing. 1988. Inflammation: basic principles and clinical correlates. In Inflammation: Basic Principles and Clinical Correlates. J. I. Gallin, I. M. Goldstein, and R. Snyderman, eds. Raven Press, New York, p. 309.
    • (1988) Inflammation: Basic Principles and Clinical Correlates , pp. 309
    • Snyderman, R.1    Uhing, R.J.2
  • 3
    • 0030175987 scopus 로고    scopus 로고
    • N-formyl-methionyl-leucyl-phenyl-alanine (fMLP), a bacterial derivative, induces and modulates IL-1β and IL-6 in human PBMC
    • Arbour, N., P. Tremblay, and D. Oth. 1996 N-formyl-methionyl-leucyl-phenyl-alanine (fMLP), a bacterial derivative, induces and modulates IL-1β and IL-6 in human PBMC. Cytokine 8:468.
    • (1996) Cytokine , vol.8 , pp. 468
    • Arbour, N.1    Tremblay, P.2    Oth, D.3
  • 4
    • 0023968859 scopus 로고
    • Calcium influx stimulates a second pathway for sustained diacylglycerol production in leukocytes activated by chemoattractants
    • Truett, A.P., III, M. W. Verghese, S. B. Dillon, R. Snyderman. 1988 Calcium influx stimulates a second pathway for sustained diacylglycerol production in leukocytes activated by chemoattractants. Proc. Natl. Acad. Sci. USA 85:1549.
    • (1988) Proc. Natl. Acad. Sci. USA , vol.85 , pp. 1549
    • Truett A.P. III1    Verghese, M.W.2    Dillon, S.B.3    Snyderman, R.4
  • 5
    • 0025615835 scopus 로고
    • The human N-formylpeptide receptor: Characterization of two cDNA isolates and evidence for a new subfamily of G-protein-coupled receptors
    • Boulay, F., M. Tardif, L. Brouchon, and P. Vignais. 1990 The human N-formylpeptide receptor: characterization of two cDNA isolates and evidence for a new subfamily of G-protein-coupled receptors. Biochemistry 29:11123.
    • (1990) Biochemistry , vol.29 , pp. 11123
    • Boulay, F.1    Tardif, M.2    Brouchon, L.3    Vignais, P.4
  • 6
    • 0028245263 scopus 로고
    • Thrombin and thrombin receptor agonist peptide induce early events of T cell activation and synergize with TCR cross-linking for CD69 expression and interleukin 2 production
    • Mari, B., V. Imbert, N. Belhacene, D. Far, J.-F. Peyron, J. Pouyssegur, E. Van Obberghen-Schilling, B. Rossi, and P. Auberger. 1994 Thrombin and thrombin receptor agonist peptide induce early events of T cell activation and synergize with TCR cross-linking for CD69 expression and interleukin 2 production. J. Biol. Chem. 269:8517.
    • (1994) J. Biol. Chem. , vol.269 , pp. 8517
    • Mari, B.1    Imbert, V.2    Belhacene, N.3    Far, D.4    Peyron, J.-F.5    Pouyssegur, J.6    Van Obberghen-Schilling, E.7    Rossi, B.8    Auberger, P.9
  • 8
    • 0029031505 scopus 로고
    • Platelet-activating factor induces NF-κB activation through a G protein-coupled pathway
    • Kravchenko, V. V., Z. K. Pan, J. Han, R. J. Ulevitch, and R. D. Ye. 1995 Platelet-activating factor induces NF-κB activation through a G protein-coupled pathway. J. Biol. Chem. 270:14928.
    • (1995) J. Biol. Chem. , vol.270 , pp. 14928
    • Kravchenko, V.V.1    Pan, Z.K.2    Han, J.3    Ulevitch, R.J.4    Ye, R.D.5
  • 9
    • 0028967112 scopus 로고
    • Platelet-activating factor stimulates transcription of the heparin-binding EGF-like growth factor in monocytes: Correlation with an increased κB binding activity
    • Pan, Z. K., V. V. Kravchenko, and R. D. Ye. 1995 Platelet-activating factor stimulates transcription of the heparin-binding EGF-like growth factor in monocytes: correlation with an increased κB binding activity. J. Biol. Chem. 270:7787.
    • (1995) J. Biol. Chem. , vol.270 , pp. 7787
    • Pan, Z.K.1    Kravchenko, V.V.2    Ye, R.D.3
  • 10
    • 0029909907 scopus 로고    scopus 로고
    • Bradykinin stimulates NF-κB activation and IL-1β gene expression in cultured human fibroblast
    • Pan, Z. K., B. L. Zuraw, C. C. Lung. E. R. Prossnitz, D. D. Browning, and R. D. Ye. 1996 Bradykinin stimulates NF-κB activation and IL-1β gene expression in cultured human fibroblast. J. Clin. Invest. 98:2042.
    • (1996) J. Clin. Invest. , vol.98 , pp. 2042
    • Pan, Z.K.1    Zuraw, B.L.2    Lung, C.C.3    Prossnitz, E.R.4    Browning, D.D.5    Ye, R.D.6
  • 11
    • 0026612229 scopus 로고
    • Leukotriene B4 transcriptionally activates interleukin-6 expression involving NF-κB and NF-IL6
    • Brach, M. A., S. de Vos, C. Arnold, H.-J. Gruss, R. Mertelsmann, and F. Herrmann. 1992 Leukotriene B4 transcriptionally activates interleukin-6 expression involving NF-κB and NF-IL6. Eur. J. Immunol. 22:2705.
    • (1992) Eur. J. Immunol. , vol.22 , pp. 2705
    • Brach, M.A.1    De Vos, S.2    Arnold, C.3    Gruss, H.-J.4    Mertelsmann, R.5    Herrmann, F.6
  • 12
    • 0028913968 scopus 로고
    • Monocyte tethering by P-selectin regulates monocyte chemotactic protein-1 and tumor necrosis factor-α secretion
    • Weyrich, A. S., T. M. MeIntyre, R. P. McEver, S. M. Prescott, and G. A. Zimmerman. 1995 Monocyte tethering by P-selectin regulates monocyte chemotactic protein-1 and tumor necrosis factor-α secretion. J. Clin. Invest. 95: 2297.
    • (1995) J. Clin. Invest. , vol.95 , pp. 2297
    • Weyrich, A.S.1    Meintyre, T.M.2    McEver, R.P.3    Prescott, S.M.4    Zimmerman, G.A.5
  • 13
    • 0030938211 scopus 로고    scopus 로고
    • Cell type- and developmental stage-specific activation of NF-κB by fMet-Leu-Phe in myeloid cells
    • Browning, D. D., Z. K. Pan, Prossnitz, E. R., and R. D. Ye. 1997 Cell type- and developmental stage-specific activation of NF-κB by fMet-Leu-Phe in myeloid cells. J. Biol. Chem. 272:7995.
    • (1997) J. Biol. Chem. , vol.272 , pp. 7995
    • Browning, D.D.1    Pan, Z.K.2    Prossnitz, E.R.3    Ye, R.D.4
  • 14
    • 0022481133 scopus 로고
    • Multiple nuclear factors interact with the immunoglobulin enhancer sequences
    • Sen, R., and D. Baltimore. 1986 Multiple nuclear factors interact with the immunoglobulin enhancer sequences. Cell 46:705.
    • (1986) Cell , vol.46 , pp. 705
    • Sen, R.1    Baltimore, D.2
  • 15
    • 0028174061 scopus 로고
    • Function and activation of NF-κb in the immune system
    • Baeuerle, P. A., and T. Henkel. 1994 Function and activation of NF-κB in the immune system. Annu. Rev. Immunol. 32:141.
    • (1994) Annu. Rev. Immunol. , vol.32 , pp. 141
    • Baeuerle, P.A.1    Henkel, T.2
  • 16
    • 0023951485 scopus 로고
    • The kinetics of interleukin 1 secretion from activated monocytes: Differences between interleukin 1β
    • Hazuda, D. J., J. C. Lee, and P. R. Young. 1988 The kinetics of interleukin 1 secretion from activated monocytes: differences between interleukin 1β. J. Biol. Chem. 263:8473.
    • (1988) J. Biol. Chem. , vol.263 , pp. 8473
    • Hazuda, D.J.1    Lee, J.C.2    Young, P.R.3
  • 17
    • 0022508713 scopus 로고
    • Control of cachectin (tumor necrosis factor) synthesis: Mechanisms of endotoxin resistance
    • Beutler, B., N. Krochin, I. W. Milsark, C. Luedke, and A. Cerami. 1986 Control of cachectin (tumor necrosis factor) synthesis: mechanisms of endotoxin resistance. Science 232:977.
    • (1986) Science , vol.232 , pp. 977
    • Beutler, B.1    Krochin, N.2    Milsark, I.W.3    Luedke, C.4    Cerami, A.5
  • 18
    • 0023724778 scopus 로고
    • IκB: A specific inhibitor of the NF-κB transcription factor
    • Baeuerle, P. A., and D. Baltimore. 1988 IκB: a specific inhibitor of the NF-κB transcription factor. Science 242:540.
    • (1988) Science , vol.242 , pp. 540
    • Baeuerle, P.A.1    Baltimore, D.2
  • 19
    • 0027618650 scopus 로고
    • Regulation of the NF-κB/rel transcription factor and 1κB inhibitor system
    • Liou, H. C., and D. Baltimore. 1993 Regulation of the NF-κB/rel transcription factor and 1κB inhibitor system. Curr. Opin. Cell Biol. 5:477.
    • (1993) Curr. Opin. Cell Biol. , vol.5 , pp. 477
    • Liou, H.C.1    Baltimore, D.2
  • 20
    • 0028986193 scopus 로고
    • NF-κB: A lesson in family value
    • Thanos, D., and T. Maniatis. 1995 NF-κB: a lesson in family value. Cell 80:529.
    • (1995) Cell , vol.80 , pp. 529
    • Thanos, D.1    Maniatis, T.2
  • 21
    • 0030610362 scopus 로고    scopus 로고
    • A cytokine-responsive 1κB kinase that activates the transcription factor NF-κB
    • DiDonato, J. A., M. Hayakawa, D. M. Rothwarf, E. Zandi, and M. Karin. 1997 A cytokine-responsive 1κB kinase that activates the transcription factor NF-κB. Nature 388:548.
    • (1997) Nature , vol.388 , pp. 548
    • DiDonato, J.A.1    Hayakawa, M.2    Rothwarf, D.M.3    Zandi, E.4    Karin, M.5
  • 22
    • 0031586174 scopus 로고    scopus 로고
    • Identification and characterization of an 1κB kinase
    • Regnier, C. H., H. Y. Song, D. V. Goeddel, Z. Cao, and M. Rothe. 1997 Identification and characterization of an 1κB kinase. Cell 90:373.
    • (1997) Cell , vol.90 , pp. 373
    • Regnier, C.H.1    Song, H.Y.2    Goeddel, D.V.3    Cao, Z.4    Rothe, M.5
  • 23
    • 0030611595 scopus 로고    scopus 로고
    • 1κB kinase-β: NF-κB activation and complex formation with 1κ-α and NIK
    • Woronicz, J. D., X. Gao, Z. Cao, M. Rothe, and D. V. Goeddel. 1997 1κB kinase-β: NF-κB activation and complex formation with 1κ-α and NIK. Science 278:866.
    • (1997) Science , vol.278 , pp. 866
    • Woronicz, J.D.1    Gao, X.2    Cao, Z.3    Rothe, M.4    Goeddel, D.V.5
  • 24
    • 0033537850 scopus 로고    scopus 로고
    • Requirement of phosphatidylinositol 3-kinase activity for bradykinin stimulation of NF-κB activation in cultured human epithelial cells
    • Pan, Z. K., S. C. Christiansen, A. Ptasznik, and B. L. Zuraw. 1999 Requirement of phosphatidylinositol 3-kinase activity for bradykinin stimulation of NF-κB activation in cultured human epithelial cells. J. Biol. Chem. 274:9918.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9918
    • Pan, Z.K.1    Christiansen, S.C.2    Ptasznik, A.3    Zuraw, B.L.4
  • 26
    • 0028883178 scopus 로고
    • Phospholipid signaling
    • Divecha, N., and R. F. Irvine. 1995 Phospholipid signaling. Cell 80:269.
    • (1995) Cell , vol.80 , pp. 269
    • Divecha, N.1    Irvine, R.F.2
  • 27
    • 0028095620 scopus 로고
    • Structure, regulation and function of phosphoinositide 3-kinase
    • Fry, M. J. 1994 Structure, regulation and function of phosphoinositide 3-kinase. Biochim. Biophys. Acta 1226:237.
    • (1994) Biochim. Biophys. Acta , vol.1226 , pp. 237
    • Fry, M.J.1
  • 28
    • 0025727594 scopus 로고
    • cDNA cloning of a novel 85 kd protein that has SH2 domains and regulates binding of Pi3-kinase to the PDGF β-receptor
    • Escobedo, J. A., S. Navankasattusas, W. M. Kavanaugh, D. Milfay, V. A. Fried, and L. T. Williams. 1991 cDNA cloning of a novel 85 kd protein that has SH2 domains and regulates binding of PI3-kinase to the PDGF β-receptor. Cell 65:75.
    • (1991) Cell , vol.65 , pp. 75
    • Escobedo, J.A.1    Navankasattusas, S.2    Kavanaugh, W.M.3    Milfay, D.4    Fried, V.A.5    Williams, L.T.6
  • 29
    • 0025755422 scopus 로고
    • Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase
    • Otsu, M., I. Hiles, I. Gout, M. J. Fry, F. Ruiz-Larrea, G. Panayotou, A. Thompson, R. Dhand, J. Hsuan, and N. Totty. 1991 Characterization of two 85 kd proteins that associate with receptor tyrosine kinases, middle-T/pp60c-src complexes, and PI3-kinase. Cell 65:91.
    • (1991) Cell , vol.65 , pp. 91
    • Otsu, M.1    Hiles, I.2    Gout, I.3    Fry, M.J.4    Ruiz-Larrea, F.5    Panayotou, G.6    Thompson, A.7    Dhand, R.8    Hsuan, J.9    Totty, N.10
  • 30
    • 0028334738 scopus 로고
    • A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein β-γ subunits
    • Stephens, L., A. Smrcka, F. T. Cooke, T. R. Jackson, P. C. Sternweis, and P. T. Hawkins. 1994 A novel phosphoinositide 3 kinase activity in myeloid-derived cells is activated by G protein β-γ subunits. Cell 77:83.
    • (1994) Cell , vol.77 , pp. 83
    • Stephens, L.1    Smrcka, A.2    Cooke, F.T.3    Jackson, T.R.4    Sternweis, P.C.5    Hawkins, P.T.6
  • 32
    • 0023810588 scopus 로고
    • An inositol tetrakisphosphate-containing phospholipid in activated neutrophils
    • Traynor-Kaplan, A. E., A. L. Harris, B. L. Thompson, P. Taylor, and L. A. Sklar. 1988 An inositol tetrakisphosphate-containing phospholipid in activated neutrophils. Nature 334:353.
    • (1988) Nature , vol.334 , pp. 353
    • Traynor-Kaplan, A.E.1    Harris, A.L.2    Thompson, B.L.3    Taylor, P.4    Sklar, L.A.5
  • 33
    • 0024475227 scopus 로고
    • NF-κB: A pleiotropic mediator of inducible and tissue-specific gene control
    • Lenardo, M. J., and D. Baltimore. 1989 NF-κB: a pleiotropic mediator of inducible and tissue-specific gene control. Cell 58:227.
    • (1989) Cell , vol.58 , pp. 227
    • Lenardo, M.J.1    Baltimore, D.2
  • 35
    • 0021100690 scopus 로고
    • Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei
    • Dignam, J. D., R. M. Lebovitz, and R. G. Roeder. 1983 Accurate transcription initiation by RNA polymerase II in a soluble extract from isolated mammalian nuclei. Nucleic Acids Res. 11:1475.
    • (1983) Nucleic Acids Res. , vol.11 , pp. 1475
    • Dignam, J.D.1    Lebovitz, R.M.2    Roeder, R.G.3
  • 36
    • 0029148780 scopus 로고
    • G protein-coupled chemoattractant receptors regulate Lyn tyrosine kinase: She adapter protein signaling complexes
    • Plasznik, A., A. Traynor-Kaplan, and G. M. Bokoch. 1995 G protein-coupled chemoattractant receptors regulate Lyn tyrosine kinase: She adapter protein signaling complexes. J. Biol. Chem. 270:19969.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19969
    • Plasznik, A.1    Traynor-Kaplan, A.2    Bokoch, G.M.3
  • 37
    • 0028179929 scopus 로고
    • NF-κB regulates IL-1β transcription through a consensus NF-κB binding site and a nonconsensus CRE-like site
    • Cogswell, J. P., M. M. Godlevski, G. B. Wisely, W. C. Clay, L. M. Leesnitzer, J. P. Ways, and J. G. Gray. 1994 NF-κB regulates IL-1β transcription through a consensus NF-κB binding site and a nonconsensus CRE-like site. J. Immunol. 153:712.
    • (1994) J. Immunol. , vol.153 , pp. 712
    • Cogswell, J.P.1    Godlevski, M.M.2    Wisely, G.B.3    Clay, W.C.4    Leesnitzer, L.M.5    Ways, J.P.6    Gray, J.G.7
  • 38
    • 0020435972 scopus 로고
    • Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells
    • Gorman, C. M., L. F. Moffat, and B. H. Howard. 1982 Recombinant genomes which express chloramphenicol acetyltransferase in mammalian cells. Mol. Cell. Biol. 2:1044.
    • (1982) Mol. Cell. Biol. , vol.2 , pp. 1044
    • Gorman, C.M.1    Moffat, L.F.2    Howard, B.H.3
  • 39
    • 0026590541 scopus 로고
    • Dithiocarbamates as potent inhibitors of nuclear factor κB activation in intact cells
    • Schreck, R., B. Meier, D. N. Mannel, W. Droge, and P. A. Bacuerle. 1992 Dithiocarbamates as potent inhibitors of nuclear factor κB activation in intact cells. J. Exp. Med. 175:1181.
    • (1992) J. Exp. Med. , vol.175 , pp. 1181
    • Schreck, R.1    Meier, B.2    Mannel, D.N.3    Droge, W.4    Bacuerle, P.A.5
  • 40
    • 0028909206 scopus 로고
    • Regulation of phosphatidylinositol 3′-kinase by tyrosyl phosphoproteins: Full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit
    • Rordorf-Nikolic, T., D. J. Van Horn, D. Chen, M. F. White, and J. M. Backer. 1995 Regulation of phosphatidylinositol 3′-kinase by tyrosyl phosphoproteins: full activation requires occupancy of both SH2 domains in the 85-kDa regulatory subunit. J. Biol. Chem. 270:3662.
    • (1995) J. Biol. Chem. , vol.270 , pp. 3662
    • Rordorf-Nikolic, T.1    Van Horn, D.J.2    Chen, D.3    White, M.F.4    Backer, J.M.5
  • 41
    • 0029159785 scopus 로고
    • Novel functions of phosphatidylinositol 3-kinase in terminally differentiated cells
    • Nakanishi, S., H. Yano, and Y. Matsuda. 1995 Novel functions of phosphatidylinositol 3-kinase in terminally differentiated cells. Cell. Signalling 7:545.
    • (1995) Cell. Signalling , vol.7 , pp. 545
    • Nakanishi, S.1    Yano, H.2    Matsuda, Y.3
  • 42
    • 0028170210 scopus 로고
    • A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002)
    • Vlahos, C. J., W. F. Matter, K. Y. Hui, and R. F. Brown. 1994 A specific inhibitor of phosphatidylinositol 3-kinase, 2-(4-morpholinyl)-8-phenyl-4H-1-benzopyran-4-one (LY294002). J. Biol. Chem. 269:5241.
    • (1994) J. Biol. Chem. , vol.269 , pp. 5241
    • Vlahos, C.J.1    Matter, W.F.2    Hui, K.Y.3    Brown, R.F.4
  • 43
    • 0021320341 scopus 로고
    • Production of intra- and extracellular interleukin-1 (IL-1) by human monocytes
    • Lepe-Zuniga, J. L., and I. Gery. 1984 Production of intra- and extracellular interleukin-1 (IL-1) by human monocytes. Clin. Immunol. Immunopathol. 31:222.
    • (1984) Clin. Immunol. Immunopathol. , vol.31 , pp. 222
    • Lepe-Zuniga, J.L.1    Gery, I.2
  • 44
    • 0025731596 scopus 로고
    • Pathway of phosphatidylinositol (3,4,5)-trisphosphate synthesis in activated neutrophils
    • Stephens, L. R., K. T. Hughes, and R. F. Irvine. 1991 Pathway of phosphatidylinositol (3,4,5)-trisphosphate synthesis in activated neutrophils. Nature 351:33.
    • (1991) Nature , vol.351 , pp. 33
    • Stephens, L.R.1    Hughes, K.T.2    Irvine, R.F.3
  • 45
    • 0026340995 scopus 로고
    • Phosphoinositide 3-kinase: A new effector in signal transduction?
    • Downes, C. P., and A. N. Carter. 1991 Phosphoinositide 3-kinase: a new effector in signal transduction? Cell. Signalling 3:501.
    • (1991) Cell. Signalling , vol.3 , pp. 501
    • Downes, C.P.1    Carter, A.N.2
  • 46
    • 0026563923 scopus 로고
    • Phosphatidylinositol 3-kinase: A key enzyme in diverse signalling processes
    • Panayotou, G., and M. D. Waterfield. 1992 Phosphatidylinositol 3-kinase: a key enzyme in diverse signalling processes. Trends Cell Biol. 2:358.
    • (1992) Trends Cell Biol. , vol.2 , pp. 358
    • Panayotou, G.1    Waterfield, M.D.2
  • 47
    • 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
  • 48
    • 0029823946 scopus 로고    scopus 로고
    • A tyrosine kinase signaling pathway accounts for the majority of phosphatidylinositol 3,4,5-trisphosphate formation in chemoattractant-stimulated human neutrophils
    • Ptasznik, A., E. R. Prossnitz, D. Yoshikawa, A. Smrcka, A. E. Traynor-Kaplan, and G. M. Bokoch. 1996 A tyrosine kinase signaling pathway accounts for the majority of phosphatidylinositol 3,4,5-trisphosphate formation in chemoattractant-stimulated human neutrophils. J. Biol. Chem. 271:25204.
    • (1996) J. Biol. Chem. , vol.271 , pp. 25204
    • Ptasznik, A.1    Prossnitz, E.R.2    Yoshikawa, D.3    Smrcka, A.4    Traynor-Kaplan, A.E.5    Bokoch, G.M.6
  • 49
    • 0030853493 scopus 로고    scopus 로고
    • Co-operation of phosphatidylinositol transfer protein with phosphoinositide 3-kinase γ in the formylmethionyl-leucylphenylalanine-dependent production of phosphatidylinositol 3,4,5-trisphosphate in human neutrophils
    • Kular, G., M. Loubtchenkov, P. Swigart, J. Whatmore, A. Ball, S. Cockcroft, and R. Wetzker. 1997 Co-operation of phosphatidylinositol transfer protein with phosphoinositide 3-kinase γ in the formylmethionyl-leucylphenylalanine-dependent production of phosphatidylinositol 3,4,5-trisphosphate in human neutrophils. Biochem. J. 325:299.
    • (1997) Biochem. J. , vol.325 , pp. 299
    • Kular, G.1    Loubtchenkov, M.2    Swigart, P.3    Whatmore, J.4    Ball, A.5    Cockcroft, S.6    Wetzker, R.7


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