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Volumn 163, Issue 11, 1999, Pages 5954-5963

The CXC chemokine stromal cell-derived factor activates a G(i)-coupled phosphoinositide 3-kinase in T lymphocytes

Author keywords

[No Author keywords available]

Indexed keywords

2 (2 AMINO 3 METHOXYPHENYL)CHROMONE; 2 MORPHOLINO 8 PHENYLCHROMONE; ALPHA CHEMOKINE; CHEMOKINE RECEPTOR CXCR4; INHIBITORY GUANINE NUCLEOTIDE BINDING PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PERTUSSIS TOXIN; PHOSPHATIDYLINOSITOL 3 KINASE; POLYPHOSPHOINOSITIDE; PROTEIN KINASE B; WORTMANNIN;

EID: 0033486065     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (210)

References (85)
  • 1
    • 0032127167 scopus 로고    scopus 로고
    • Chemokines and T lymphocytes: More than an attraction
    • Ward, S. G., K. B. Bacon, and J. Westwick. 1998. Chemokines and T lymphocytes: more than an attraction. Immunity 9:1.
    • (1998) Immunity , vol.9 , pp. 1
    • Ward, S.G.1    Bacon, K.B.2    Westwick, J.3
  • 2
    • 0028052968 scopus 로고
    • Interleukin-8 and related chemotactic cytokine: CXC and CC chemokines
    • Baggiolini, M., B. Dewald, and B. Moser. 1994. Interleukin-8 and related chemotactic cytokine: CXC and CC chemokines. Adv. Immunol. 55:97.
    • (1994) Adv. Immunol. , vol.55 , pp. 97
    • Baggiolini, M.1    Dewald, B.2    Moser, B.3
  • 4
    • 0029805203 scopus 로고    scopus 로고
    • Host factors and the pathogenesis of HIV-induced disease
    • Fauci, A. S. 1996. Host factors and the pathogenesis of HIV-induced disease. Nature 384:529.
    • (1996) Nature , vol.384 , pp. 529
    • Fauci, A.S.1
  • 5
    • 0030793861 scopus 로고    scopus 로고
    • Co-receptors for HIV-1 entry
    • Moore, J. P. 1997. Co-receptors for HIV-1 entry. Curr. Opin. Immunol. 8:551.
    • (1997) Curr. Opin. Immunol. , vol.8 , pp. 551
    • Moore, J.P.1
  • 6
    • 0032143524 scopus 로고    scopus 로고
    • Chemokines: Understanding their role in T-lymphocyte biology
    • Ward, S. G., and J. Westwick. 1998. Chemokines: understanding their role in T-lymphocyte biology. Biochem. J. 333:457.
    • (1998) Biochem. J. , vol.333 , pp. 457
    • Ward, S.G.1    Westwick, J.2
  • 7
    • 0028324454 scopus 로고
    • Molecular cloning and structure of a pre-B cell growth-stimulating factor. Proc
    • Nagasawa, T., H. Kikutani, and T. Kishimoto. 1994. Molecular cloning and structure of a pre-B cell growth-stimulating factor. Proc. Natl. Acad. Sci. USA 91: 2305.
    • (1994) Natl. Acad. Sci. USA , vol.91 , pp. 2305
    • Nagasawa, T.1    Kikutani, H.2    Kishimoto, T.3
  • 8
    • 0029099521 scopus 로고
    • Structure and chromosomal localization of the human stromal cell-derived factor-1 gene
    • Shirozu, M., T. Nakano, J. Inazawa, K. Tashiro, H. Tada, T. Shinohara, and T. Honjo. 1995. Structure and chromosomal localization of the human stromal cell-derived factor-1 gene. Genomics 28:495.
    • (1995) Genomics , vol.28 , pp. 495
    • Shirozu, M.1    Nakano, T.2    Inazawa, J.3    Tashiro, K.4    Tada, H.5    Shinohara, T.6    Honjo, T.7
  • 9
  • 12
    • 0030002637 scopus 로고    scopus 로고
    • HIV-1 entry cofactor: Functional cDNa cloning of a seven transmembrane G protein-coupled receptor
    • Feng, Y., C. C. Broder, P. E. Kennedy, and E. A. Berger. 1996. HIV-1 entry cofactor: functional cDNA cloning of a seven transmembrane G protein-coupled receptor. Science 272:872.
    • (1996) Science , vol.272 , pp. 872
    • Feng, Y.1    Broder, C.C.2    Kennedy, P.E.3    Berger, E.A.4
  • 13
    • 0028012561 scopus 로고
    • Cloning of a human seven-transmembrane domain receptor, LESTR, that is highly expressed in leukocytes
    • Loetscher, M., T. Geiser, T. O'Reilly, R. Zwahlen. M. Baggiolini, and B. Moser. 1994. Cloning of a human seven-transmembrane domain receptor, LESTR, that is highly expressed in leukocytes. J. Biol. Chem. 269:232.
    • (1994) J. Biol. Chem. , vol.269 , pp. 232
    • Loetscher, M.1    Geiser, T.2    O'Reilly, T.3    Zwahlen, R.4    Baggiolini, M.5    Moser, B.6
  • 16
    • 0031569539 scopus 로고    scopus 로고
    • Alternate splicing of mouse fusin/CXC chemokine receptor-4: SDF-1α is a ligand for both CXC chemokine receptor-4 isoforms
    • Heesen, M., M. A. Berman, U. E. Hopken, N. P. Gerard, and M. E. Dorf. 1997. Alternate splicing of mouse fusin/CXC chemokine receptor-4: SDF-1α is a ligand for both CXC chemokine receptor-4 isoforms. J. Immunol. 158:3561.
    • (1997) J. Immunol. , vol.158 , pp. 3561
    • Heesen, M.1    Berman, M.A.2    Hopken, U.E.3    Gerard, N.P.4    Dorf, M.E.5
  • 17
    • 0032536869 scopus 로고    scopus 로고
    • Flexible programs of chemokine receptor expression on human polarized T helper 1 and 2 lymphocytes
    • Sallusto, F., D. Lenig, C. R. Mackay, and A. Lanzavecchia. 1998. Flexible programs of chemokine receptor expression on human polarized T helper 1 and 2 lymphocytes. J. Exp. Med. 187:875.
    • (1998) J. Exp. Med. , vol.187 , pp. 875
    • Sallusto, F.1    Lenig, D.2    Mackay, C.R.3    Lanzavecchia, A.4
  • 18
    • 0031985684 scopus 로고    scopus 로고
    • CXCR-4 is expressed by primary macrophages and supports CCR5-independent infection by dual-tropic but not T-tropic isolates of human immunodeficiency virus type 1
    • Yi, Y. J., S. Rana, J. D. Turner, N. Gaddis, and R. G. Collman. 1998. CXCR-4 is expressed by primary macrophages and supports CCR5-independent infection by dual-tropic but not T-tropic isolates of human immunodeficiency virus type 1. J. Virol. 72:772.
    • (1998) J. Virol. , vol.72 , pp. 772
    • Yi, Y.J.1    Rana, S.2    Turner, J.D.3    Gaddis, N.4    Collman, R.G.5
  • 19
    • 0031975540 scopus 로고    scopus 로고
    • Identification and characterization of the CXCR4 chemokine receptor in human T cell lines: Ligand binding, biological activity, and HIV-1 infectivity
    • Hesselgesser, J., M. Liang, J. Hoxie, M. Greenberg, L. F. Brass, M. J. Orsini, D. Taub, and R. Horuk. 1998. Identification and characterization of the CXCR4 chemokine receptor in human T cell lines: ligand binding, biological activity, and HIV-1 infectivity. J. Immunol. 160:877.
    • (1998) J. Immunol. , vol.160 , pp. 877
    • Hesselgesser, J.1    Liang, M.2    Hoxie, J.3    Greenberg, M.4    Brass, L.F.5    Orsini, M.J.6    Taub, D.7    Horuk, R.8
  • 20
    • 0038117657 scopus 로고    scopus 로고
    • Intracellular and surface expression of the HIV-1 coreceptor CXCR4/fusin on various leukocyte subsets: Rapid internalization and recycling upon activation
    • Forster, R., E. Kremmer, A. Schubel, D. Breitfeld, A. Kleinschmidt, C. Nerl, G. Bernhardt, and M. Lipp. 1998. Intracellular and surface expression of the HIV-1 coreceptor CXCR4/fusin on various leukocyte subsets: rapid internalization and recycling upon activation. J. Immunol. 160:1522.
    • (1998) J. Immunol. , vol.160 , pp. 1522
    • Forster, R.1    Kremmer, E.2    Schubel, A.3    Breitfeld, D.4    Kleinschmidt, A.5    Nerl, C.6    Bernhardt, G.7    Lipp, M.8
  • 21
    • 0031042433 scopus 로고    scopus 로고
    • The HIV coreceptors CXCR4 and CCR5 are differentially expressed and regulated on human T lympocytes
    • Bleul, C. C., L. Wu, J. A. Hoxie, T. A. Springer, and C. R. MacKay. 1997. The HIV coreceptors CXCR4 and CCR5 are differentially expressed and regulated on human T lympocytes. Proc. Natl. Acad. Sci. USA 94:1925.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 1925
    • Bleul, C.C.1    Wu, L.2    Hoxie, J.A.3    Springer, T.A.4    MacKay, C.R.5
  • 22
    • 0030759182 scopus 로고    scopus 로고
    • Chemically synthesized SDF-1α analogue, N33A, is a potent chemotactic agent for CXCR4/fusin/LESTR-expressing human leukocytes
    • Ueda, H., M. A. Siani, W. H. Gong, D. A. Thompson, G. G. Brown, and J. M. Wang. 1997. Chemically synthesized SDF-1α analogue, N33A, is a potent chemotactic agent for CXCR4/fusin/LESTR-expressing human leukocytes. J. Biol. Chem. 272:24966.
    • (1997) J. Biol. Chem. , vol.272 , pp. 24966
    • Ueda, H.1    Siani, M.A.2    Gong, W.H.3    Thompson, D.A.4    Brown, G.G.5    Wang, J.M.6
  • 27
    • 0032507962 scopus 로고    scopus 로고
    • Function of the chemokine receptor CXCR4 in haematopoiesis and in cerebellar development
    • Zou, Y. R., A. H. Kottmann, M. Kuroda, I. Taniuchi, and D. R. Littman. 1998. Function of the chemokine receptor CXCR4 in haematopoiesis and in cerebellar development. Nature 393:595.
    • (1998) Nature , vol.393 , pp. 595
    • Zou, Y.R.1    Kottmann, A.H.2    Kuroda, M.3    Taniuchi, I.4    Littman, D.R.5
  • 28
    • 0031927822 scopus 로고    scopus 로고
    • Binding of human immunodeficiency virus type 1 to CD4 and CXCR4 receptors differentially regulates expression of inflammatory genes and activates the MEK/ERK signaling pathway
    • Popik, W., J. E. Hesselgesser, and P. M. Pitha. 1998. Binding of human immunodeficiency virus type 1 to CD4 and CXCR4 receptors differentially regulates expression of inflammatory genes and activates the MEK/ERK signaling pathway. J. Virol. 72:6406.
    • (1998) J. Virol. , vol.72 , pp. 6406
    • Popik, W.1    Hesselgesser, J.E.2    Pitha, P.M.3
  • 31
    • 0032483419 scopus 로고    scopus 로고
    • The α-chemokine, stromal cell-derived factor-1α, binds to the transmembrane G-protein-coupled CXCR-4 receptor and activates multiple signal transduction pathways
    • Ganju, R. K., S. A. Brubaker, J. Meyer, P. Dutt, Y. M. Yang, S. X. Qin, W. Newman, and J. E. Groopman. 1998. The α-chemokine, stromal cell-derived factor-1α, binds to the transmembrane G-protein-coupled CXCR-4 receptor and activates multiple signal transduction pathways. J. Biol. Chem. 273:23169.
    • (1998) J. Biol. Chem. , vol.273 , pp. 23169
    • Ganju, R.K.1    Brubaker, S.A.2    Meyer, J.3    Dutt, P.4    Yang, Y.M.5    Qin, S.X.6    Newman, W.7    Groopman, J.E.8
  • 34
    • 0028334738 scopus 로고
    • A novel phosphoinositide 3 kinase activity in myeloid cells is activated by G protein βγ subunits
    • Stephens, L. R., A. S. Smrcka, F. T. Cooke, T. R. Jackson, P. C. Sternweiss, and P. T. Hawkins. 1994. A novel phosphoinositide 3 kinase activity in myeloid cells is activated by G protein βγ subunits. Cell 77:83.
    • (1994) Cell , vol.77 , pp. 83
    • Stephens, L.R.1    Smrcka, A.S.2    Cooke, F.T.3    Jackson, T.R.4    Sternweiss, P.C.5    Hawkins, P.T.6
  • 35
    • 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
  • 36
    • 0030869757 scopus 로고    scopus 로고
    • Heterodimeric phosphoinositide 3-kinase consisting of p85 and p110β is synergistically activated by the βγ subunits of G proteins and phosphotyrosyl peptide
    • Kurosu, H., T. Maehama, T. Okada, T. Yamamoto, S. Hoshino, Y. Fukui, M. Ui, O. Hazeki, and T. Katada. 1996. Heterodimeric phosphoinositide 3-kinase consisting of p85 and p110β is synergistically activated by the βγ subunits of G proteins and phosphotyrosyl peptide. J. Biol. Chem. 272:24252.
    • (1996) J. Biol. Chem. , vol.272 , pp. 24252
    • Kurosu, H.1    Maehama, T.2    Okada, T.3    Yamamoto, T.4    Hoshino, S.5    Fukui, Y.6    Ui, M.7    Hazeki, O.8    Katada, T.9
  • 38
    • 0030992837 scopus 로고    scopus 로고
    • Signalling through the lipid products of phosphoinositide-3-OH kinase
    • Toker, A., and L. C. Cantley. 1997. Signalling through the lipid products of phosphoinositide-3-OH kinase. Nature 387:673.
    • (1997) Nature , vol.387 , pp. 673
    • Toker, A.1    Cantley, L.C.2
  • 41
    • 0032143284 scopus 로고    scopus 로고
    • Phosphoinositide 3-kinase: The key switch mechanism in insulin signaling
    • Shepherd, P. R., D. J. Withers, and K. Siddle. 1998. Phosphoinositide 3-kinase: the key switch mechanism in insulin signaling. Biochem. J. 333:471.
    • (1998) Biochem. J. , vol.333 , pp. 471
    • Shepherd, P.R.1    Withers, D.J.2    Siddle, K.3
  • 43
    • 0027432424 scopus 로고
    • Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: The role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses
    • Arcaro, A., and M. P. Wymann. 1993. Wortmannin is a potent phosphatidylinositol 3-kinase inhibitor: the role of phosphatidylinositol 3,4,5-trisphosphate in neutrophil responses. Biochem. J. 296:297.
    • (1993) Biochem. J. , vol.296 , pp. 297
    • Arcaro, A.1    Wymann, M.P.2
  • 44
    • 0029160069 scopus 로고
    • Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction
    • Burgering, B. T., and P. J. Coffer. 1995. Protein kinase B (c-Akt) in phosphatidylinositol-3-OH kinase signal transduction. Nature 376:599.
    • (1995) Nature , vol.376 , pp. 599
    • Burgering, B.T.1    Coffer, P.J.2
  • 45
    • 0028178928 scopus 로고
    • PDGF-dependent and insulin-dependent pp70(S6K) activation mediated by phosphatidylinositol-3-OH kinase
    • Chung, J. K., T. C. Grammer, K. P. Lemon, A. Kazlauskas, and J. Blenis. 1994. PDGF-dependent and insulin-dependent pp70(S6K) activation mediated by phosphatidylinositol-3-OH kinase. Nature 370:71.
    • (1994) Nature , vol.370 , pp. 71
    • Chung, J.K.1    Grammer, T.C.2    Lemon, K.P.3    Kazlauskas, A.4    Blenis, J.5
  • 47
    • 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., G. S. Worthen, and G. L. Johnson. 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.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 3052
    • Knall, C.1    Worthen, G.S.2    Johnson, G.L.3
  • 48
    • 0029126042 scopus 로고
    • RANTES-activated human T lymphocytes: A role for phosphoinositide 3-kinase
    • Turner, L., S. G. Ward, and J. Westwick. 1995. RANTES-activated human T lymphocytes: a role for phosphoinositide 3-kinase. J. Immunol. 155:2437.
    • (1995) J. Immunol. , vol.155 , pp. 2437
    • Turner, L.1    Ward, S.G.2    Westwick, J.3
  • 49
    • 0032476036 scopus 로고    scopus 로고
    • The CC chemokine monocyte chemotactic peptide-1 activates both the class I p85/p110 phosphatidylinositol 3-kinase and the class II P13K-C2α
    • Turner, S. J., J. Domin, M. D. Waterfield, S. G. Ward, and J. Westwick. 1998. The CC chemokine monocyte chemotactic peptide-1 activates both the class I p85/p110 phosphatidylinositol 3-kinase and the class II P13K-C2α. J. Biol. Chem. 273:25987.
    • (1998) J. Biol. Chem. , vol.273 , pp. 25987
    • Turner, S.J.1    Domin, J.2    Waterfield, M.D.3    Ward, S.G.4    Westwick, J.5
  • 51
    • 0027373348 scopus 로고
    • B7/CD28 but not LFA-3/CD2 interactions can provide "third party" costimulation for human T cell activation
    • Sansom, D. M., A. Wilson, M. Boshell, J. Lewis, and N. D. Hall. 1993. B7/CD28 but not LFA-3/CD2 interactions can provide "third party" costimulation for human T cell activation. Immunology 80:242.
    • (1993) Immunology , vol.80 , pp. 242
    • Sansom, D.M.1    Wilson, A.2    Boshell, M.3    Lewis, J.4    Hall, N.D.5
  • 52
    • 0025217753 scopus 로고
    • Heterogeneity of the regulation of phospholipase C by phorbol esters in T lymphocytes
    • Ward, S. G., and D. A. Cantrell. 1990. Heterogeneity of the regulation of phospholipase C by phorbol esters in T lymphocytes. J. Immunol. 144:3523.
    • (1990) J. Immunol. , vol.144 , pp. 3523
    • Ward, S.G.1    Cantrell, D.A.2
  • 53
    • 0026674617 scopus 로고
    • Receptor specificity of growth factor-stimulated synthesis of 3-phosphorylated inositol lipids in Swiss 3T3 cells
    • Jackson, T. R., L. R. Stephens, and P. T. Hawkins. 1992. Receptor specificity of growth factor-stimulated synthesis of 3-phosphorylated inositol lipids in Swiss 3T3 cells. J. Biol. Chem. 267:16627.
    • (1992) J. Biol. Chem. , vol.267 , pp. 16627
    • Jackson, T.R.1    Stephens, L.R.2    Hawkins, P.T.3
  • 54
    • 0027429761 scopus 로고
    • Ligation of CD28 receptor by B7 induces the formation of D-3 phosphoinositides in T lymphocytes independently of T cell receptor/CD3 activation
    • Ward, S. G., W. J. N. Hall, J. Westwick, and D. M. Sansom. 1993. Ligation of CD28 receptor by B7 induces the formation of D-3 phosphoinositides in T lymphocytes independently of T cell receptor/CD3 activation. Eur. J. Immunol. 23: 2572.
    • (1993) Eur. J. Immunol. , vol.23 , pp. 2572
    • Ward, S.G.1    Hall, W.J.N.2    Westwick, J.3    Sansom, D.M.4
  • 55
    • 0028940428 scopus 로고
    • Inhibition of CD28-mediated T cell costimulation by the phosphoinositide 3-kinase inhibitor wortmannin
    • Ward, S. G., A. Wilson, L. Turner, J. Westwick, and D. M. Sansom. 1995. Inhibition of CD28-mediated T cell costimulation by the phosphoinositide 3-kinase inhibitor wortmannin. Eur. J. Immunol. 25:526.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 526
    • Ward, S.G.1    Wilson, A.2    Turner, L.3    Westwick, J.4    Sansom, D.M.5
  • 56
    • 0032575620 scopus 로고    scopus 로고
    • N-terminal peptides of stromal-cell derived factor-1 with CXC chemokine receptor 4 agonist and antagonist activities
    • Loetscher, P., J. H. Gong, B. Dewald, M. Baggiolini, and I. Clark-Lewis. 1998. N-terminal peptides of stromal-cell derived factor-1 with CXC chemokine receptor 4 agonist and antagonist activities. J. Biol. Chem. 273:22279.
    • (1998) J. Biol. Chem. , vol.273 , pp. 22279
    • Loetscher, P.1    Gong, J.H.2    Dewald, B.3    Baggiolini, M.4    Clark-Lewis, I.5
  • 57
    • 0032055484 scopus 로고    scopus 로고
    • Phosphatidylinositol 3,4,5-trisphosphate/Tec kinase-dependent calcium signalling pathway: A target for SHIP-mediated inhibitory signals
    • Scharenberg, A. M., O. El-Hillal, D. A. Fruman, L. O. Beitz, Z. Li, S. Lin, I. Gout, L. C. Cantley, D. J. Rawlings, and J. P. Kinet. 1998. Phosphatidylinositol 3,4,5-trisphosphate/Tec kinase-dependent calcium signalling pathway: a target for SHIP-mediated inhibitory signals. EMBO J. 17:1961.
    • (1998) EMBO J. , vol.17 , pp. 1961
    • Scharenberg, A.M.1    El-Hillal, O.2    Fruman, D.A.3    Beitz, L.O.4    Li, Z.5    Lin, S.6    Gout, I.7    Cantley, L.C.8    Rawlings, D.J.9    Kinet, J.P.10
  • 58
    • 0029965452 scopus 로고    scopus 로고
    • Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction
    • Wymann, M. P., G. Bulgarelli-Leva, M. J. Zvelebil, L. Pirola, B. Vanhaesebroeck, M. D. Waterfield, and G. Panayotou. 1996. Wortmannin inactivates phosphoinositide 3-kinase by covalent modification of Lys-802, a residue involved in the phosphate transfer reaction. Mol. Cell. Biol. 16:1722.
    • (1996) Mol. Cell. Biol. , vol.16 , pp. 1722
    • Wymann, M.P.1    Bulgarelli-Leva, G.2    Zvelebil, M.J.3    Pirola, L.4    Vanhaesebroeck, B.5    Waterfield, M.D.6    Panayotou, G.7
  • 59
    • 0021227906 scopus 로고
    • Chemotactic peptide modulation of actin assembly and locomotion in neutrophils
    • Howard, T. H., and W. H. Meyer. 1984. Chemotactic peptide modulation of actin assembly and locomotion in neutrophils. J. Cell Biol. 98:1265.
    • (1984) J. Cell Biol. , vol.98 , pp. 1265
    • Howard, T.H.1    Meyer, W.H.2
  • 60
    • 0031037296 scopus 로고    scopus 로고
    • Linkage of the G-protein coupled receptors to the MAPK signalling pathway through PI 3-kinase-γ
    • Lopez-Ilasaca, M., P. Crespo, P. G. Pellici, J. S. Gutkind, and R. Wetzker. 1997. Linkage of the G-protein coupled receptors to the MAPK signalling pathway through PI 3-kinase-γ. Science 275:394.
    • (1997) Science , vol.275 , pp. 394
    • Lopez-Ilasaca, M.1    Crespo, P.2    Pellici, P.G.3    Gutkind, J.S.4    Wetzker, R.5
  • 63
    • 0025754159 scopus 로고
    • Bombesin, vasopressin, and endothelin rapidly stimulate tyrosine phosphorylation in intact Swiss 3T3 cells
    • Zachary, I., J. Gil, W. Lehmann, J. Sinnett-Smith, and E. Rozengurt. 1991. Bombesin, vasopressin, and endothelin rapidly stimulate tyrosine phosphorylation in intact Swiss 3T3 cells. Proc. Natl. Acad. Sci. USA 88:4577.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 4577
    • Zachary, I.1    Gil, J.2    Lehmann, W.3    Sinnett-Smith, J.4    Rozengurt, E.5
  • 64
    • 0030035099 scopus 로고    scopus 로고
    • Synergistic activation of phosphoinositide 3-kinase by tyrosine-phosphorylated peptide and βγ subunits of GTP binding proteins
    • Okada, T., O. Hazeki, and T. Katada. 1996. Synergistic activation of phosphoinositide 3-kinase by tyrosine-phosphorylated peptide and βγ subunits of GTP binding proteins. Biochem. J. 317:475.
    • (1996) Biochem. J. , vol.317 , pp. 475
    • Okada, T.1    Hazeki, O.2    Katada, T.3
  • 65
    • 0030995012 scopus 로고    scopus 로고
    • Regulation of phosphoinositide-specific phospholipase C isozymes
    • Rhee, S. G., and Y. S. Bae. 1997. Regulation of phosphoinositide-specific phospholipase C isozymes. J. Biol. Chem. 272:15045.
    • (1997) J. Biol. Chem. , vol.272 , pp. 15045
    • Rhee, S.G.1    Bae, Y.S.2
  • 66
    • 0032933558 scopus 로고    scopus 로고
    • TCR activation inhibits chemotaxis toward stromal cell-derived factor-1: Evidence for the reciprocal regulation between CXCR4 and the TCR
    • Peacock, J. W., and F. R. Jirick. 1998. TCR activation inhibits chemotaxis toward stromal cell-derived factor-1: evidence for the reciprocal regulation between CXCR4 and the TCR. J. Immunol. 162:215.
    • (1998) J. Immunol. , vol.162 , pp. 215
    • Peacock, J.W.1    Jirick, F.R.2
  • 67
    • 0031148668 scopus 로고    scopus 로고
    • A negative role for phosphoinositide 3-kinase in T cell antigen receptor signalling
    • Reif, K., S. Lucas, and D. A. Cantrell. 1997. A negative role for phosphoinositide 3-kinase in T cell antigen receptor signalling. Curr. Biol. 7:285.
    • (1997) Curr. Biol. , vol.7 , pp. 285
    • Reif, K.1    Lucas, S.2    Cantrell, D.A.3
  • 68
    • 0032500730 scopus 로고    scopus 로고
    • Bifurcation of lipid and protein kinase signals of PI 3-kinase-γ to the protein kinases PKB and MAPK
    • Bondeva, T., L. Pirola, G. Bulgarelli-Leva, I. Rubio, R. Wetzker, and M. P. Wymann. 1998. Bifurcation of lipid and protein kinase signals of PI 3-kinase-γ to the protein kinases PKB and MAPK. Science 282:293.
    • (1998) Science , vol.282 , pp. 293
    • Bondeva, T.1    Pirola, L.2    Bulgarelli-Leva, G.3    Rubio, I.4    Wetzker, R.5    Wymann, M.P.6
  • 69
    • 0032563295 scopus 로고    scopus 로고
    • Activation of Akt/PKB by G protein-coupled receptors: A role for α and βγ subunits of heterotrimeric G proteins acting through PI 3-kinase
    • Murga, C., L. Laguinge, R. Wetzker, A. Cuadrado, and J. S. Gutkind. 1998. Activation of Akt/PKB by G protein-coupled receptors: a role for α and βγ subunits of heterotrimeric G proteins acting through PI 3-kinase. J. Biol. Chem. 273:19080.
    • (1998) J. Biol. Chem. , vol.273 , pp. 19080
    • Murga, C.1    Laguinge, L.2    Wetzker, R.3    Cuadrado, A.4    Gutkind, J.S.5
  • 70
    • 0030737427 scopus 로고    scopus 로고
    • G protein-coupled receptors and Fcγy-receptors mediate activation of Akt/ protein kinase B in human phagocytes
    • Tilton, B., M. Andjelkovic, S. Didichenko, B. A. Hemmings, and M. Thelen. 1997. G protein-coupled receptors and Fcγy-receptors mediate activation of Akt/ protein kinase B in human phagocytes. J. Biol. Chem. 272:28096.
    • (1997) J. Biol. Chem. , vol.272 , pp. 28096
    • Tilton, B.1    Andjelkovic, M.2    Didichenko, S.3    Hemmings, B.A.4    Thelen, M.5
  • 71
    • 0031034574 scopus 로고    scopus 로고
    • Anti-apoptotic signalling by the insulin-like growth factor 1 receptor, PI 3-kinase and Akt
    • Kulik, G., A. Klippel, and M. J. Weber. 1997. Anti-apoptotic signalling by the insulin-like growth factor 1 receptor, PI 3-kinase and Akt. Mol. Cell. Biol. 17: 1595.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 1595
    • Kulik, G.1    Klippel, A.2    Weber, M.J.3
  • 74
    • 0032492918 scopus 로고    scopus 로고
    • Neuronal apoptosis induced by HIV-1 gp120 and the chemokine SDF-1α is mediated by the chemokine receptor CXCR4
    • Hesselgesser, J., D. Taub, P. Baskar, M. Greenberg, J. Hoxie, D. L. Kolson, and R. Horuk. 1998. Neuronal apoptosis induced by HIV-1 gp120 and the chemokine SDF-1α is mediated by the chemokine receptor CXCR4. Curr. Biol. 8:595.
    • (1998) Curr. Biol. , vol.8 , pp. 595
    • Hesselgesser, J.1    Taub, D.2    Baskar, P.3    Greenberg, M.4    Hoxie, J.5    Kolson, D.L.6    Horuk, R.7
  • 77
    • 0031951334 scopus 로고    scopus 로고
    • MAP kinase function in amoeboid chemotaxis
    • Wang, Y. W., J. Liu, and J. E. Segall. 1998. MAP kinase function in amoeboid chemotaxis. J. Cell Sci. 111:373.
    • (1998) J. Cell Sci. , vol.111 , pp. 373
    • Wang, Y.W.1    Liu, J.2    Segall, J.E.3
  • 78
    • 0030723163 scopus 로고    scopus 로고
    • Platelet-derived growth factor and fibronectin-stimulated migration are differentially regulated by the Rac and extracellular signal-regulated kinase pathways
    • Anand-Apte, B., B. R. Zetter, A. Viswanathan, R. G. Qiu, J. Chen, R. Ruggieri, and M. Symons. 1997. Platelet-derived growth factor and fibronectin-stimulated migration are differentially regulated by the Rac and extracellular signal-regulated kinase pathways. J. Biol. Chem. 272:30688.
    • (1997) J. Biol. Chem. , vol.272 , pp. 30688
    • Anand-Apte, B.1    Zetter, B.R.2    Viswanathan, A.3    Qiu, R.G.4    Chen, J.5    Ruggieri, R.6    Symons, M.7
  • 80
    • 0029563238 scopus 로고
    • PI 3-kinase-dependent and independent chemotaxis of human neutrophil leukocytes
    • Thelen, M., M. Uguccioni, and J. Bosiger. 1995. PI 3-kinase-dependent and independent chemotaxis of human neutrophil leukocytes. Biochem. Biophys. Res. Commun. 217:1255.
    • (1995) Biochem. Biophys. Res. Commun. , vol.217 , pp. 1255
    • Thelen, M.1    Uguccioni, M.2    Bosiger, J.3
  • 82
    • 0031830195 scopus 로고    scopus 로고
    • Cytoskeletal reorganization by G protein-coupled receptors is dependent on PI 3-kinase-γ, a Rac guanosine exchange factor, and Rac
    • Ma, A., A. Metjian, S. Bagrodia, S. Taylor, and C. S. Abrams. 1998. Cytoskeletal reorganization by G protein-coupled receptors is dependent on PI 3-kinase-γ, a Rac guanosine exchange factor, and Rac. Mol. Cell. Biol. 18:4744.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 4744
    • Ma, A.1    Metjian, A.2    Bagrodia, S.3    Taylor, S.4    Abrams, C.S.5
  • 83
    • 0030745286 scopus 로고    scopus 로고
    • HIV coreceptor down-regulation as anti-viral principle: SDF-1α-dependent internalization of the chemokine receptor CXCR4 contributes to inhibition of HIV replication
    • Amara, A., S. Le Gall, O. Schwartz, J. Salamero, M. Montes, P. Loetscher, M. Baggiolini, J. L. Virelizier, and F. Arenzana-Seisdedos. 1997. HIV coreceptor down-regulation as anti-viral principle: SDF-1α-dependent internalization of the chemokine receptor CXCR4 contributes to inhibition of HIV replication. J. Exp. Med. 186:139.
    • (1997) J. Exp. Med. , vol.186 , pp. 139
    • Amara, A.1    Le Gall, S.2    Schwartz, O.3    Salamero, J.4    Montes, M.5    Loetscher, P.6    Baggiolini, M.7    Virelizier, J.L.8    Arenzana-Seisdedos, F.9
  • 84
    • 0033198102 scopus 로고    scopus 로고
    • CXCR4-Lo: Molecular cloning and functional expression of a novel human CXCR4 splice variant
    • Gupta, S. K., and K. Pillarisetti. 1999. CXCR4-Lo: molecular cloning and functional expression of a novel human CXCR4 splice variant. J. Immunol. 163:2368.
    • (1999) J. Immunol. , vol.163 , pp. 2368
    • Gupta, S.K.1    Pillarisetti, K.2
  • 85
    • 0031948845 scopus 로고    scopus 로고
    • PKB activation and lamellipodium formation are independent PI 3-kinase-mediated events differentially regulated by endogenous Ras
    • Van Weering, D. H., J. D. De Rooij, B. Marte, B. Downward, J. Bos, and B. M. T. Burgering 1998. PKB activation and lamellipodium formation are independent PI 3-kinase-mediated events differentially regulated by endogenous Ras. Mol. Cell. Biol. 18:1802.
    • (1998) Mol. Cell. Biol. , vol.18 , pp. 1802
    • Van Weering, D.H.1    De Rooij, J.D.2    Marte, B.3    Downward, B.4    Bos, J.5    Burgering, B.M.T.6


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