메뉴 건너뛰기




Volumn 177, Issue , 2000, Pages 150-174

Chemokines, chemokine receptors and hematopoiesis

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CHEMOKINE; BETA CHEMOKINE; CHEMOKINE; CHEMOKINE RECEPTOR; GROWTH FACTOR;

EID: 0033668778     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-065X.2000.17701.x     Document Type: Review
Times cited : (113)

References (344)
  • 2
    • 0343754068 scopus 로고    scopus 로고
    • Phenotypic and proliferative characteristics of cord blood hematopoietic stem and progenitor cells and gene transfer
    • Broxmeyer HE, ed. Cellular characteristics of cord blood and cord blood transplantation
    • (1997) American Association Blood Banking , pp. 11-44
    • Broxmeyer, H.E.1
  • 3
    • 0027967350 scopus 로고
    • What defines a pluripotent hematopoietic stem cell (PHSC): Will the real PHSC please stand up
    • (1994) Blood , vol.84 , pp. 3991-3994
    • Orlic, D.1    Bodine, D.M.2
  • 6
    • 0029999842 scopus 로고    scopus 로고
    • Is interleukin-17, an inducible cytokine that stimulates production of other cytokines, merely a redundant player in a sea of other biomolecules?
    • (1996) J Exp Med , vol.183 , pp. 2411-2415
    • Broxmeyer, H.E.1
  • 8
    • 0001513212 scopus 로고    scopus 로고
    • Measurement of interleukin-3 and other hematopoietic growth factors, such as GM-CSF, G-CSF, M-CSF, erythropoietin and the potent co-stimulating cytokines Steel factor and Flt-3 ligand
    • Coligan JE, Kruisbeek AM, Margulies DH, Shevach EM, Strober W, Coico R, eds. New York: John Wiley and Sons, Inc
    • (1996) Current protocols in immunology. Supplement 18 , pp. 641-6412
    • Cooper, S.1    Broxmeyer, H.E.2
  • 9
    • 0025160956 scopus 로고
    • Candidate ligand for the c-kit transmembrane kinase receptor: KL, a fibroblast derived growth factor stimulates mast cells and erythroid progenitors
    • (1990) EMBO J , vol.9 , pp. 3287-3294
    • Nocka, K.1    Buck, J.2    Levi, E.3    Besmer, P.4
  • 10
    • 0025077796 scopus 로고
    • The hematopoietic growth factor KL is encoded by the S1 locus and is the ligand of the c-kit receptor, the gene product of the W locus
    • (1990) Cell , vol.63 , pp. 225-233
    • Huang, E.1
  • 11
    • 0025013548 scopus 로고
    • Identification of a ligand for the c-kit proto-oncogene
    • (1990) Cell , vol.63 , pp. 167-174
    • Williams, D.E.1
  • 12
    • 0025001892 scopus 로고
    • Identification, purification and biological characterization of hematopoietic stem cell factor from buffalo rat liver-conditioned medium
    • (1990) Cell , vol.63 , pp. 195-201
    • Zsebo, K.M.1
  • 13
    • 0025011056 scopus 로고
    • The kit ligand: A cell surface molecule altered in Steel mutant fibroblasts
    • (1990) Cell , vol.63 , pp. 185-194
    • Flanagan, J.G.1    Leder, P.2
  • 14
    • 0026320943 scopus 로고
    • The Kit receptor and its ligand, Steel factor, as regulators of hemopoiesis
    • (1991) Cancer Cells , vol.3 , pp. 480-487
    • Broxmeyer, H.E.1
  • 15
    • 0030846533 scopus 로고    scopus 로고
    • Stem cell factor and hematopoiesisis
    • (1997) Blood , vol.90 , pp. 1345-1364
    • Broudy, V.1
  • 16
    • 0032519768 scopus 로고    scopus 로고
    • C-kit ligand and Flt3 ligand: Stem/progenitor cell factors with overlapping but distinct activities
    • (1998) Blood , vol.91 , pp. 1101-1134
    • Lyman, S.D.1    Jacobsen, S.E.W.2
  • 17
    • 0025938925 scopus 로고
    • Comparative analysis of signaling pathways between mast cell growth factor (c-kit ligand) and granulocyte-macrophage colony stimulating factor in a human factor-dependent myeloid cell line involves phosphorylation of Raf-1, GTPase-activating protein and mitogen-activated protein kinase
    • (1991) Exp Hematol , vol.19 , pp. 1110-1123
    • Miyazawa, K.1    Hendrie, P.C.2    Mantel, C.3    Wood, K.4    Ashman, L.K.5    Broxmeyer, H.E.6
  • 18
    • 0027395767 scopus 로고
    • Involvement of immediate-early gene expression in the synergistic effects of Steel factor in combination with granulocyte-macrophage colony stimulating factor or interleukin-3 on proliferation of a human factor-dependent cell line
    • (1993) J Biol Chem , vol.268 , pp. 968-973
    • Horie, M.1    Broxmeyer, H.E.2
  • 22
    • 0028362418 scopus 로고
    • SH2-containing phosphotyrosine phosphatase Syp is a target of p210bcr-abl tyrosine kinase
    • (1994) J Biol Chem , vol.269 , pp. 15381-15387
    • Tauchi, T.1
  • 24
    • 0028847937 scopus 로고
    • The combination of Steel factor and granulocyte-macrophage colony-stimulating factor blocks apoptosis induced by retinoic acid and upregulates AP-1 in a human growth factor-dependent cell line
    • (1995) Exp Hematol , vol.23 , pp. 168-173
    • Horie, M.1    Broxmeyer, H.E.2
  • 25
    • 0028148266 scopus 로고
    • The ubiquitously expressed Syp phosphatase interacts with c-kit and Grb2 in hematopoietic cells
    • (1994) J Biol Chem , vol.269 , pp. 25206-25211
    • Tauchi, T.1
  • 26
    • 0029101751 scopus 로고
    • Interferon-inducible protein 10 and macrophage inflammatory protein-1α inhibit growth factor stimulation of Raf-1 kinase activity and protein synthesis in a human growth factor-dependent hematopoietic cell line
    • (1995) J Biol Chem , vol.270 , pp. 21998-22007
    • Aronica, S.M.1
  • 27
    • 0029122028 scopus 로고
    • Synergistic induction of phospholipid metabolism by granulocyte-macrophage colony stimulating factor and Steel factor in human growth factor-dependent cell line, M07 e
    • (1995) Lipids , vol.30 , pp. 641-647
    • Mantel, C.1    Luo, Z.2    Broxmeyer, H.E.3
  • 31
    • 0030977401 scopus 로고    scopus 로고
    • Macrophage inflammatory protein-1α and interferon-inducible protein 1α inhibit synergistically-induced growth factor stimulation of MAP kinase activity, and suppress phosphorylation of eukaryotic initiation factor-4E binding protein 1 (4E-BP1)
    • (1997) Blood , vol.89 , pp. 3582-3595
    • Aronica, S.M.1    Gingras, A.C.2    Sonenberg, N.3    Broxmeyer, H.E.4
  • 34
    • 0030918253 scopus 로고    scopus 로고
    • C-kit receptor signaling through its phosphatidylinositide-3'-kinase binding site and protein kinase C: Role in mast cell enhancement of degranulation, adhesion and membrane ruffling
    • (1997) Mol Biol Cell , vol.8 , pp. 909-922
    • Vosseller, K.1    Stella, G.2    Besmer, P.3
  • 35
    • 0027955112 scopus 로고
    • + human bone marrow cells and is involved in the proliferation of early progenitor/stem cells
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 459-463
    • Small, D.1
  • 36
    • 0027494860 scopus 로고
    • Mitogenic signaling and substrate specificity of the flk 2/flt 3 receptor tyrosine kinase in fibroblasts and interleukin-3-dependent hematopoietic cells
    • (1993) Mol Cell Biol , vol.13 , pp. 6572-6585
    • Dosil, M.1    Wang, S.2    Lemischka, I.R.3
  • 37
    • 0027146421 scopus 로고
    • Molecular cloning of a ligand for the flt 3/flk-2 tyrosine kinase receptor: A proliferative factor for primitive hematopoietic cells
    • (1993) Cell , vol.75 , pp. 1157-1167
    • Lyman, S.D.1
  • 41
    • 0027494860 scopus 로고
    • Mitogenic signaling and substrate specificity of the Flk2/Flt3 receptor tyrosine kinase in fibroblasts and interleukin 3-dependent hematopoietic cells
    • (1993) Mol Cell Biol , vol.13 , pp. 6572-6585
    • Dosil, M.1    Wang, S.2    Lemischka, I.R.3
  • 42
    • 0027461751 scopus 로고
    • Biochemical characterization and analysis of the transforming potential of the Flt3/Flk2 receptor tyrosine kinase
    • (1993) Oncogene , vol.8 , pp. 909-918
    • Maroc, N.1
  • 43
    • 0028357497 scopus 로고
    • Substrate specificities and identification of a putative binding site for PI3K in the carboxy tail of the murine Flt3 receptor tyrosine kinase
    • (1994) Oncogene , vol.9 , pp. 1755-1765
    • Rottapel, R.1
  • 45
    • 0029810842 scopus 로고    scopus 로고
    • Phosphatidylinositol-3' kinase is not required for mitogenesis or internalization of the Flt3/Flk2 recaptor tyrosine kinase
    • (1996) J Biol Chem , vol.271 , pp. 20075-20081
    • Beslu, N.1
  • 48
    • 0033020705 scopus 로고    scopus 로고
    • Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells
    • (1999) J Leukoc Biol , vol.65 , pp. 372-380
    • Zhang, S.1    Broxmeyer, H.E.2
  • 49
    • 0033582304 scopus 로고    scopus 로고
    • P85 subunit of PI3 kinase does not bind to human Flt3 receptor, but associates with SHP2, SHIP and a tyrosine phosphorylated 100 kDa protein in Flt3 ligand-stimulated hematopoietic cells
    • (1999) Biochem Biophys Res Comm , vol.154 , pp. 440-445
    • Zhang, S.1    Broxmeyer, H.E.2
  • 50
    • 0023199623 scopus 로고
    • The in vivo effects of purified recombinant IL-3 and purified natural CSF-1 on murine high proliferative potential colony forming cells: Demonstration of in vivo synergism
    • (1987) Blood , vol.70 , pp. 401-403
    • Williams, D.E.1
  • 51
    • 0023204443 scopus 로고
    • Synergistic myelopoietic action in vivo of combinations of purified natural murine colony stimulating factor-1, recombinant murine interleukin-3, and recombinant routine granulocyte-macrophage colony stimulating factor administered to mice
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 3871-3875
    • Broxmeyer, H.E.1
  • 55
    • 0033020968 scopus 로고    scopus 로고
    • Regulation of hematopoiesis in a sea of chemokine family members with a plethora of redundant activities
    • (1999) Exp Hematol , vol.17 , pp. 1113-1123
    • Broxmeyer, H.E.1    Kim, C.H.2
  • 60
    • 0025355270 scopus 로고
    • Identification and characterization of an inhibitor of haemopoietic stem cell proliferation
    • (1990) Nature , vol.344 , pp. 442-444
    • Graham, G.J.1
  • 61
    • 0025195391 scopus 로고
    • Enhancing and suppressing effects of recombinant murine macrophage inflammatory proteins on colony formation in vitro by bone marrow myeloid progenitor cells
    • (1990) Blood , vol.76 , pp. 1110-1116
    • Broxmeyer, H.E.1
  • 62
    • 0025947125 scopus 로고
    • Macrophage inflammatory protein (MIP)-1β abrogates the capacity of MIP-1α to suppress myeloid progenitor cell growth
    • (1991) J Immunol , vol.147 , pp. 2586-2594
    • Broxmeyer, H.E.1
  • 63
    • 0026467558 scopus 로고
    • Biological and structural properties of MIP-1α expressed in yeast
    • (1992) Cytokine , vol.4 , pp. 76-82
    • Clements, J.M.1
  • 66
    • 0026656723 scopus 로고
    • Demonstration of stem cell inhibition and myeloprotective effects of SCI/rhuMIP-1α in vivo
    • (1992) Blood , vol.79 , pp. 2221-2225
    • Dunlop, D.J.1
  • 68
    • 0027300330 scopus 로고
    • Comparative analysis of the suppressive effects of the human macrophage inflammatory protein family of cytokines (chemokines) on proliferation of human myeloid progenitor cells
    • (1993) J Immunol , vol.150 , pp. 3448-3458
    • Broxmeyer, H.E.1
  • 69
    • 0027893238 scopus 로고
    • +++ stem/progenitor cells from human bone marrow and umbilical cord blood plated with and without serum
    • (1993) Exp Hematol , vol.21 , pp. 1442-1446
    • Lu, L.1
  • 71
    • 0029586149 scopus 로고
    • Human chemokines: Enhancement of specific activity and effects in vitro on normal and leukemic progenitors and a factor dependent cell line and in vivo in mice
    • (1995) Ann Hematol , vol.71 , pp. 235-246
    • Broxmeyer, H.E.1
  • 72
    • 0028806172 scopus 로고
    • BB10010: An active variant of human macrophage inflammatory protein-1α with improved pharmaceutical properties
    • (1995) Blood , vol.86 , pp. 4400-4408
    • Hunter, M.G.1
  • 74
    • 0024853541 scopus 로고
    • Myelopoietic enhancing effects of murine macrophage inflammatory proteins 1 and 2 in vitro on colony formation by murine and human bone marrow granulocyte-macrophage progenitor cells
    • (1989) J Exp Med , vol.170 , pp. 1583-1594
    • Broxmeyer, H.E.1
  • 77
    • 0030809822 scopus 로고    scopus 로고
    • Impaired monocyte migration and reduced Type 1 (Th1) cytokine responses in CCR2 knockout mice
    • (1997) J Clin Invest , vol.100 , pp. 2552-2561
    • Boring, L.1
  • 78
    • 0033105728 scopus 로고    scopus 로고
    • Enhanced myeloid progenitor cell cycling and apoptosis in mice lacking the chemokine receptor, CCR2
    • (1999) Blood , vol.93 , pp. 1524-1533
    • Reid, S.1
  • 79
    • 0030913175 scopus 로고    scopus 로고
    • Impaired host defense, hematopoiesis, granulomatous inflammation and type 1/type 2 cytokine balance in mice lacking cc chemokine receptor 1
    • (1997) J Exp Med , vol.185 , pp. 1959-1968
    • Gao, J.L.1
  • 83
    • 0028941483 scopus 로고
    • Correlation of terminal cell cycle arrest of skeletal muscle with induction of p21 by MyoD
    • (1995) Science , vol.267 , pp. 1018-1020
    • Halevy, O.1
  • 84
    • 0028986639 scopus 로고
    • P53-independent expression of p21 (cip1) in muscle and other terminally differentiating cells
    • (1995) Science , vol.267 , pp. 1024-1027
    • Parker, S.B.1
  • 87
    • 0027359827 scopus 로고
    • WAF1, a potential indicator of p53 tumor suppression
    • (1993) Cell , vol.75 , pp. 817-825
    • El-Diery, W.S.1
  • 88
    • 0029808466 scopus 로고    scopus 로고
    • Cell cycle checkpoints: Preventing an identity crisis
    • (1996) Science , vol.274 , pp. 1664-1672
    • Elledge, S.J.1
  • 89
    • 0028913739 scopus 로고
    • A p53-dependent mouse spindle checkpoint
    • (1995) Science , vol.267 , pp. 1353-1356
    • Cross, S.M.1
  • 90
    • 0032005132 scopus 로고    scopus 로고
    • p53 And Rb prevent rereplication in response to microtubule inhibitors by mediating a reversible G1 arrest
    • (1998) Cancer Res , vol.58 , pp. 396-401
    • Khan, S.H.1    Wahl, G.M.2
  • 91
  • 92
    • 0033557572 scopus 로고    scopus 로고
    • P21(waf-1/cip1) deficiency causes deformed nuclear architecture, centriole overduplication, polyploidy, and relaxed microtubule damage checkpoints in human hematopoietic cells
    • (1999) Blood , vol.93 , pp. 1390-1398
    • Mantel, C.1
  • 93
    • 0028172867 scopus 로고
    • Interleukin-2-mediated elimination of the p27(kip-1) cyclin-dependent kinase inhibitor prevented by rapamycin
    • (1994) Nature , vol.372 , pp. 570-573
    • Nourse, J.1
  • 97
    • 0032081244 scopus 로고    scopus 로고
    • A positive effect of p21(cip1/waf1) in the proliferation of murine myeloid progenitor cells as assessed by retroviral mediated gene transfer
    • (1998) Blood Cells Mol Dis , vol.24 , pp. 138-148
    • Braun, S.E.1
  • 98
    • 0030973878 scopus 로고    scopus 로고
    • New functional activities for the p21 family of CDK inhibitors
    • (1997) Genes Dev , vol.11 , pp. 847-862
    • LaBaer, J.1
  • 100
    • 0033559264 scopus 로고    scopus 로고
    • The p21(cip1) and p27(kip1) cdk inhibitors are essential activators of cyclin D-dependent kinases in murine fibroblasts
    • (1999) EMBO J , vol.18 , pp. 1571-1583
    • Cheng, M.1
  • 103
    • 0028141496 scopus 로고
    • Transformation of mammalian cells by constitutively active MAP kinase kinase
    • (1994) Science , vol.265 , pp. 966-970
    • Mansour, S.J.1
  • 105
    • 0028907351 scopus 로고
    • Requirement of MAP kinase for the differentiation of fibroblasts to adiopocytes, for insulin activation of p90 S6 kinase and for insulin or serum stimulation of DNA synthesis
    • (1995) EMBO J , vol.14 , pp. 674-684
    • Sale, E.M.1    Atkinson, P.G.2    Sale, G.J.3
  • 106
    • 0030765077 scopus 로고    scopus 로고
    • Stress-activated protein kinases: Activation, regulation and function
    • (1997) Cell Signal , vol.9 , pp. 403-410
    • Paul, A.1
  • 111
    • 0027197067 scopus 로고
    • Mutations at the murine motheaten locus are within the hematopoietic cell protein-tyrosine phosphatase (Hcph) gene
    • (1993) Cell , vol.73 , pp. 1445-1454
    • Shultz, L.D.1
  • 119
    • 0032570586 scopus 로고    scopus 로고
    • The Shp-2 tyrosine phosphatase has opposite effects in mediating the activation of extracellular signal-regulated and c-Jun NH2-terminal mitogen-activated protein kinases
    • (1998) J Biol Chem , vol.273 , pp. 4904-4908
    • Shi, Z.Q.1    Lu, W.2    Feng, G.S.3
  • 120
  • 123
    • 0030113662 scopus 로고    scopus 로고
    • Multiple forms of an inositol polyphosphatase 5-phosphatase form signaling complexes with Shc and Grb2
    • (1996) Curr Biol , vol.6 , pp. 438-445
    • Kavanaugh, W.M.1
  • 130
    • 2642684541 scopus 로고    scopus 로고
    • Targeted disruption of SHIP leads to hemopoietic perturbations, lung pathology, and a shortened life span
    • (1998) Genes Dev , vol.12 , pp. 1610-1620
    • Helgason, C.D.1
  • 132
    • 0032934156 scopus 로고    scopus 로고
    • Functional roles of Stat family proteins: Lessons from knockout mice
    • (1999) Stem Cells , vol.17 , pp. 138-146
    • Akira, S.1
  • 133
    • 85068954603 scopus 로고    scopus 로고
    • Jaks, Stats, cytokine signal transduction and immunoregulation: Are we there yet?
    • (1997) Immunity , vol.7 , pp. 1-11
    • O'Shea, J.J.1
  • 134
    • 0033105768 scopus 로고    scopus 로고
    • Resolving conflicting signals: Cross inhibition of cytokine signaling pathways
    • (1999) Blood , vol.93 , pp. 1443-1447
    • Begley, C.G.1    Nicola, N.A.2
  • 139
    • 0000943469 scopus 로고    scopus 로고
    • Stat5a and Stat5b proteins have essential and nonessential, or redundant, roles in cytokine responses
    • (1998) Cell , vol.93 , pp. 841-850
    • Teglund, S.1
  • 140
    • 0030930196 scopus 로고    scopus 로고
    • Stat5a-deficient mice demonstrate a defect in granulocyte-macrophage colony-stimulating factor-induced proliferation and gene expression
    • (1997) Blood , vol.90 , pp. 1768-1776
    • Feldman, G.M.I.1
  • 142
    • 0032076542 scopus 로고    scopus 로고
    • Jak2 is essential for signaling through a variety of cytokine receptors
    • (1998) Cell , vol.93 , pp. 385-395
    • Parganas, E.1
  • 144
    • 0032076183 scopus 로고    scopus 로고
    • Disruption of the Jak1 gene demonstrates obligatory and nonredundant roles of the Jaks in cytokine-induced biologic responses
    • (1998) Cell , vol.93 , pp. 373-383
    • Rodig, S.J.1
  • 147
    • 0033387959 scopus 로고    scopus 로고
    • Altered responsiveness to chemokines due to targeted disruption of SHIP
    • (1999) J Clin Invest , vol.104 , pp. 1751-1759
    • Kim, C.H.1
  • 148
    • 85085225785 scopus 로고    scopus 로고
    • Stat 4, BCL-6, P21(cip1/waf1), SHP-1, SHIP, and NF1 are implicated as common mediators of myelosuppression by CC, CXC, and C chemokines through use of mice functionally deleted in these intracellular molecules
    • (1999) Blood , vol.94 , Issue.SUPPL. 1
    • Broxmeyer, H.E.1
  • 149
    • 0032101030 scopus 로고    scopus 로고
    • Multiple inhibitory cytokines induce deregulated progenitor growth and apoptosis in hematopoietic cells from Fac(-/-) mice
    • (1998) Blood , vol.91 , pp. 4092-4098
    • Haneline, L.1
  • 151
    • 0026690842 scopus 로고
    • Signal transduction through small GTPases-a tale of two GAPs
    • (1992) Cell , vol.69 , pp. 389-391
    • Hall, A.1
  • 152
    • 0032577581 scopus 로고    scopus 로고
    • Chemokine receptors: Keys to AIDS pathogenesis
    • (1998) Cell , vol.93 , pp. 677-680
    • Littman, D.R.1
  • 160
    • 0032874677 scopus 로고    scopus 로고
    • Signal transduction, cell regulatory, and anti-apoptotic pathways regulated by IL-3 in hematopoietic cells: Possible sites for intervention with antineoplastic drugs
    • (1999) Leukemia , vol.13 , pp. 1109-1166
    • Blalock, W.L.1
  • 161
    • 0032859258 scopus 로고    scopus 로고
    • Suppression of P53-mediated growth factor withdrawal induced apoptosis in the myeloid compartment by hematopoietic cytokines: An overview of hematopoiesis and apoptosis with a presentation of thrombopoietin and the M07 e cell line as a model
    • (1999) Crit Rev Oncol Hematol , vol.31 , pp. 169-191
    • Ritchie, A.1    Broxmeyer, H.E.2
  • 164
  • 167
    • 0028800947 scopus 로고
    • Early distribution of plasma membrane phosphatidylserine is a general feature of apoptosis regardless of the initiating stimulus: Inhibition by overexpression of Bcl-2 and Abl
    • (1995) J Exp Med , vol.182 , pp. 1545-1556
    • Martin, S.J.1
  • 170
    • 0028943734 scopus 로고
    • Apoptosis in the pathogenesis and treatment of disease
    • (1995) Science , vol.267 , pp. 1456-1462
    • Thompson, C.B.1
  • 171
    • 0029050456 scopus 로고
    • Cell death: Current difficulties in discriminating apoptosis from necrosis in the content of pathological processes in vivo
    • (1995) J Cell Biochem , vol.58 , pp. 181-190
    • Columbano, A.1
  • 175
    • 0029096427 scopus 로고
    • + cells and their granulocytic descendents
    • (1995) Blood , vol.86 , pp. 917-923
    • Anzai, N.1
  • 176
    • 0030881653 scopus 로고    scopus 로고
    • Activation of caspase-2 in apoptosis
    • (1997) J Biol Chem , vol.272 , pp. 21010-21017
    • Li, H.1
  • 179
    • 0029068871 scopus 로고
    • Identification and inhibition of the ICE/CED-3 protease necessary for mammalian apoptosis
    • (1995) Nature , vol.376 , pp. 37-43
    • Nicholson, D.W.1
  • 180
  • 182
    • 0028963084 scopus 로고
    • Requirement for phosphatidylinositol-3 kinase in the prevention of apoptosis by nerve growth factor
    • (1995) Science , vol.267 , pp. 2003-2006
    • Yao, R.1    Cooper, G.M.2
  • 183
  • 185
    • 0032475861 scopus 로고    scopus 로고
    • Negative regulation of PKB/Akt-dependent cell survival by the tumor suppressor PTEN
    • (1998) Cell , vol.95 , pp. 29-39
    • Stambolic, V.1
  • 186
    • 13144249184 scopus 로고    scopus 로고
    • High cancer susceptibility and embryonic lethality associated with mutation of the PTEN tumor suppressor gene in mice
    • (1998) Curr Biol , vol.8 , pp. 1169-1178
    • Suzuki, A.1
  • 189
    • 0026006501 scopus 로고
    • Molecular cloning and characterization of a novel putative protein-serine kinase related to the cAMP-dependent and protein kinase C families
    • (1991) Eur J Biochem , vol.201 , pp. 475-481
    • Coffer, P.J.1    Woodgett, J.R.2
  • 190
    • 0031127305 scopus 로고    scopus 로고
    • Characterization of a 3-phosphoinositide-dependent protein kinase which phosphorylates and activates protein kinase Bα
    • (1997) Curr Biol , vol.7 , pp. 261-269
    • Alessi, D.R.1
  • 191
    • 0030799706 scopus 로고    scopus 로고
    • Dual role of phosphatidylinositol-3,4,5-triphosphate in the activation of protein kinase B
    • (1997) Science , vol.277 , pp. 567-570
    • Stokoe, D.1
  • 193
    • 0031470652 scopus 로고    scopus 로고
    • The structural basis for 14-3-3. Phosphopeptide binding specificity
    • (1997) Cell , vol.91 , pp. 961-971
    • Yaffe, M.B.1
  • 195
    • 0032515027 scopus 로고    scopus 로고
    • Regulation of cell death protease caspase-9 by phosphorylation
    • (1998) Science , vol.282 , pp. 1318-1321
    • Cardone, M.H.1
  • 198
    • 0033582929 scopus 로고    scopus 로고
    • Akt promotes cell survival by phosphorylation and inhibiting a Forkhead transcription factor
    • (1999) Cell , vol.96 , pp. 857-868
    • Brunet, A.1
  • 201
    • 0033517244 scopus 로고    scopus 로고
    • Akt is more than just a Bad kinase
    • (1999) Nature , vol.401 , pp. 33-34
    • Khwaja, A.1
  • 209
    • 0033545604 scopus 로고    scopus 로고
    • A MAP kinase docking site is required for phosphorylation and activation of p90 (rsk)/MAPKAP kinase-1
    • (1999) Curr Biol , vol.9 , pp. 281-284
    • Gavin, A.C.1    Nebreda, A.R.2
  • 214
  • 215
    • 0033870417 scopus 로고    scopus 로고
    • Control of apoptosis during angiogenesis by survivin expression in endothelial cells
    • (2000) Am J Pathol , vol.156 , pp. 393-398
    • O'Conner, D.S.1
  • 216
    • 0032403126 scopus 로고    scopus 로고
    • IAP - Family protein survivin inhibits caspase activity and apoptosis induced by Fas (CD15), Bax, caspases, and anticancer drugs
    • (1998) Cancer Res , vol.58 , pp. 5315-5320
    • Tamm, I.1
  • 217
    • 0032506524 scopus 로고    scopus 로고
    • Control of apoptosis and mitotic spindle checkpoint by survivin
    • (1998) Nature , vol.396 , pp. 580-584
    • Li, F.1
  • 218
    • 0030714669 scopus 로고    scopus 로고
    • Thrombopoietin upregulates the promoter conformation of p53 in a proliferation independent manner coincident with a decreased expression of Bax: Potential mechanisms for survival enhancing effects
    • (1997) Blood , vol.90 , pp. 4394-4402
    • Ritchie, A.1    Gotoh, A.2    Gaddy, J.3    Braun, S.4    Broxmeyer, H.E.5
  • 219
    • 0033580225 scopus 로고    scopus 로고
    • Thrombopoietin-induced conformational change in p53 lies downstream of the p44/p42 mitogen activated protein kinase cascade in the human growth factor-dependent cell line M07 e
    • (1999) Oncogene , vol.18 , pp. 1465-1471
    • Ritchie, A.1    Braun, S.E.2    He, J.3    Broxmeyer, H.E.4
  • 223
    • 0033258543 scopus 로고    scopus 로고
    • Pleiotrophic cell-division defects and apoptosis induced by interference with survivin function
    • (1999) Nat Cell Biol , vol.1 , pp. 461-466
    • Li, F.1
  • 224
    • 0034594915 scopus 로고    scopus 로고
    • Survivin initiates procaspase 3/p21 complex formation as a result of interaction with cdK4 to resist Fas-mediated cell death
    • (2000) Oncogene , vol.19 , pp. 1346-1353
    • Suzubi, A.1
  • 225
    • 0001292222 scopus 로고    scopus 로고
    • Enhanced myelopoiesis in SDF-1 transgenic mice: SDF-1 modulates myelopoiesis by regulating progenitor cell survival and inhibitory effects of myelosuppressive chemokines
    • (1999) Blood , vol.94 , Issue.SUPPL. 1 PART 1
    • Broxmeyer, H.E.1    Hangoc, G.2    Cooper, S.3    Kim, C.H.4
  • 226
    • 0029758113 scopus 로고    scopus 로고
    • Defects of B lymphopoiesis and bone marrow myelopoiesis in mice lacking the CXC chemokine PBSF/SDF-1
    • (1996) Nature , vol.382 , pp. 635-638
    • Nagasawa, T.1
  • 227
    • 0032482926 scopus 로고    scopus 로고
    • Impaired B lymphopoiesis, myelopoiesis and derailed cerebellar neuron migration in CXCR4- and SDF-deficient mice
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 9448-9453
    • Ma, Q.1
  • 229
    • 0033000290 scopus 로고    scopus 로고
    • Survival of human leukemia B-cell precursors is supported by stromal cells and cytokines: Association with the expression of bcl-2 protein
    • (1999) Br J Haematol , vol.105 , pp. 701-710
    • Nishii, K.1
  • 230
    • 0034141444 scopus 로고    scopus 로고
    • + cell proliferation in synergy with cytokines: Possible role in progenitor survival
    • (2000) Blood , vol.95 , pp. 756-768
    • Lataillade, J.J.1
  • 234
    • 0029099521 scopus 로고
    • Structure and chromosomal localization of the human stromal cell-derived factor 1 (SDF1) gene
    • (1995) Genomics , vol.28 , pp. 495-500
    • Shirozu, M.1
  • 237
    • 0032483419 scopus 로고    scopus 로고
    • The α-chemokine, stromal cell derived factor-1α binds to the transmembrane G-protein-coupled CXCR4 receptor and activates multiple signal transduction pathways
    • (1998) J Biol Chem , vol.273 , pp. 23169-23175
    • Ganju, R.K.1
  • 238
    • 0032193739 scopus 로고    scopus 로고
    • Stromal cell-derived factor 1α and stem cell factor/kit ligand share signaling pathways in hematopoietic progenitors: A potential mechanism for cooperative induction of chemotaxis
    • (1998) J Immunol , vol.161 , pp. 3652-3658
    • Dutt, P.1    Wang, J.-F.2    Groopman, J.E.3
  • 239
    • 0033215149 scopus 로고    scopus 로고
    • Involvement of phosphatidylinositol 3-kinase in stromal cell-derived factor-1α-induced lymphocyte polarization and chemotaxis
    • (1999) J Immunol , vol.163 , pp. 4001-4012
    • Vincente-Mannzannares, M.1
  • 243
    • 0026506022 scopus 로고
    • Growth characteristics and expansion of human umbilical cord blood and estimation of its potential for transplantation of adults
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4109-4113
    • Broxmeyer, H.E.1
  • 245
    • 0031985282 scopus 로고    scopus 로고
    • In vitro behavior of hematopoietic progenitor cells under the influence of chemoattractants: Stromal cell-derived factor-1, steel factor and the bone marrow environment
    • (1998) Blood , vol.91 , pp. 100-110
    • Kim, C.H.1    Broxmeyer, H.E.2
  • 247
    • 0032147012 scopus 로고    scopus 로고
    • The α-chemokine receptor CXCR4 is expressed on the megakaryocytic lineage from progenitor to platelets and modulates migration and adhesion
    • (1998) Blood , vol.92 , pp. 756-764
    • Wang, J.-F.1    Liu, X.-Y.2    Groopman, J.E.3
  • 249
    • 0344094088 scopus 로고    scopus 로고
    • CCR7 and CXCR3 ligand SLC/Exodus 2/6 Ckine induces chemotaxis of hematopoietic progenitor cells: Differential activity of ligands of CCR7, CXCR3, or CXCR4 in chemotaxis/actin polymerization vs suppression of progenitor proliferation
    • (1999) J Leukoc Biol , vol.66 , pp. 455-461
    • Kim, C.H.1    Broxmeyer, H.E.2
  • 254
    • 0034653894 scopus 로고    scopus 로고
    • Identification of a novel chemokine receptor that binds dendritic cell- and T cell-active chemokines including ELC, SLC, and TECK
    • (2000) J Immunol , vol.164 , pp. 2851-2856
    • Gosling, J.1
  • 255
    • 0034176108 scopus 로고    scopus 로고
    • The orphan chemokine receptor G protein-coupled receptor-2 (GPR-2,CCR10) binds the skin-associated chemokine CCL27 (CTACK/ALP/ILC)
    • (2000) J Immunol , vol.164 , pp. 3465-3470
    • Homey, B.1
  • 256
    • 0030938936 scopus 로고    scopus 로고
    • G-protein-coupled receptors: Molecular mechanisms involved in receptor activation and selectivity of G-protein recognition
    • (1997) FASEB J , vol.11 , pp. 346-354
    • Wess, J.1
  • 259
    • 0030946755 scopus 로고    scopus 로고
    • HIV-1 entry and macrophage inflammatory proetin-1β-mediated signaling are independent functions of the chemokine receptor CCR5
    • (1997) J Biol Chem , vol.272 , pp. 6854-6857
    • Farzan, M.1
  • 260
    • 0030846291 scopus 로고    scopus 로고
    • The amino-terminal domain of CCR2 is both necessary and sufficient for high affinity binding of monocyte chemoattractant protein 1
    • (1997) J Biol Chem , vol.272 , pp. 23186-23190
    • Monteclaro, F.S.1    Charo, I.F.2
  • 264
    • 0029761071 scopus 로고    scopus 로고
    • The amino-terminal extracellular domain of the MCP-1 receptor, but not the RANTES/MIP-1α receptor, confers chemokine selectivity. Evidence for a two-step mechanism for MCP-1 receptor activation
    • (1996) J Biol Chem , vol.9 , pp. 19084-19092
    • Monteclaro, F.S.1    Charo, I.F.2
  • 265
    • 0032493767 scopus 로고    scopus 로고
    • The N-terminal extracellular segments of the chemokine receptors CCR1 and CCR3 are determinants for MIP-1α and eotaxin binding, respectively, but a second domain is essential for efficient receptor activation
    • (1998) J Biol Chem , vol.273 , pp. 19972-19976
    • Pease, J.E.1    Wang, J.2    Ponath, P.D.3    Murphy, P.M.4
  • 266
    • 0030779808 scopus 로고    scopus 로고
    • Interaction of chemokine receptor CCR5 with its ligands: Multiple domains for HIV-1 gp120 binding and a single domain for chemokine binding
    • (1997) J Exp Med , vol.186 , pp. 1373-1381
    • Wu, L.1
  • 267
    • 0030447722 scopus 로고    scopus 로고
    • Multiple extracellular elements of CCR5 and HIV-1 entry: Dissociation from response to chemokines
    • (1996) Science , vol.274 , pp. 1924-1926
    • Atchison, R.E.1
  • 269
    • 0032568416 scopus 로고    scopus 로고
    • Rhodopsin-family receptors associated with small G proteins to activate phospholipase D
    • (1998) Nature , vol.392 , pp. 411-414
    • Mitchell, R.1
  • 271
    • 0032550337 scopus 로고    scopus 로고
    • Aminooxypentane-RANTES induces CCR5 internalization but inhibits recycling: A novel inhibitory mechanism of HIV infectivity
    • (1998) J Exp Med , vol.187 , pp. 1215-1224
    • Mack, M.1
  • 272
    • 0030754810 scopus 로고    scopus 로고
    • Dissociation of chemotaxis from agonist-induced receptor internalization in a lymphocyte cell line transfected with CCR2B. Evidence that directed migration does not require rapid modulation of signaling at the receptor level
    • (1997) J Biol Chem , vol.272 , pp. 25037-25042
    • Arai, H.1    Monteclaro, F.S.2    Tsou, C.L.3    Franci, C.4    Charo, I.F.5
  • 275
    • 0033523073 scopus 로고    scopus 로고
    • Beta-arrestins regulate interleukin-8-induced CXCR1 internalization
    • (1999) J Biol Chem , vol.274 , pp. 16287-16294
    • Barlic, J.1
  • 280
    • 0030745286 scopus 로고    scopus 로고
    • HIV coreceptor downregulation as antiviral principle: SDF-1α-dependent internalization of the chemokine receptor CXCR4 contributes to inhibition of HIV replication
    • (1997) J Exp Med , vol.186 , pp. 139-146
    • Amara, A.1
  • 281
    • 0029770657 scopus 로고    scopus 로고
    • Beta-arrestin acts as a clathrin adaptor in endocytosis of the β2-adrenergic receptor
    • (1996) Nature , vol.383 , pp. 447-450
    • Goodman O.B., Jr.1
  • 285
    • 0034161622 scopus 로고    scopus 로고
    • +- CXC chemokines and mechanisms regulating CXCR2 internalization and recycling
    • (2000) Blood , vol.95 , pp. 1551-1559
    • Feniger-Barish, R.1
  • 286
    • 0033613938 scopus 로고    scopus 로고
    • β-arrestin-dependent formation of β2 adrenergic receptor-Src protein kinase complexes
    • (1999) Science , vol.283 , pp. 655-661
    • Luttrell, L.M.1
  • 287
    • 0028011112 scopus 로고
    • G proteins: Critical control points for transmembrane signals
    • (1994) Protein Sci , vol.3 , pp. 3-14
    • Neer, E.J.1
  • 289
    • 0028860268 scopus 로고
    • Heterotrimeric G proteins: Organizers of transmembrane signals
    • (1995) Cell , vol.80 , pp. 249-257
    • Neer, E.J.1
  • 290
    • 0031461603 scopus 로고    scopus 로고
    • Chemotaxis in a lymphocyte cell line transfected with C-C chemokine receptor 2B: Evidence that directed migration is mediated by βγ dimers released by activation of Gαi-coupled receptors
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 14495-14499
    • Arai, H.1    Tsou, C.-L.2    Charo, I.F.3
  • 305
    • 0034651728 scopus 로고    scopus 로고
    • Regulator of G protein signaling 1 (RGS1) markedly impairs Giα signaling responses of B lymphocytes
    • (2000) J Immunol , vol.164 , pp. 1829-1838
    • Moratz, C.1
  • 314
    • 0034616165 scopus 로고    scopus 로고
    • av2 Is an activator of Cdc42, Rac1, and RhoA
    • (2000) J Biol Chem , vol.275 , pp. 10141-10149
    • Abe, K.1
  • 319
    • 0029090212 scopus 로고
    • Cloning and characterization of a G protein-activated human phosphoinositide-3 kinase
    • (1995) Science , vol.269 , pp. 690-693
    • Stoyanov, B.1
  • 320
    • 0030887632 scopus 로고    scopus 로고
    • The G βγ sensitivity of a PI3K is dependent upon a tightly associated adaptor, p101
    • (1997) Cell , vol.89 , pp. 105-114
    • Stephens, L.R.1
  • 323
    • 0034635264 scopus 로고    scopus 로고
    • Function of P13Kγ in thymocyte development, T cell activation, and neutrophil migration
    • (2000) Science , vol.287 , pp. 1040-1046
    • Sasaki, T.1
  • 325
    • 0034635452 scopus 로고    scopus 로고
    • Central role for G protein-coupled phosphoinositide 3-kinase γ in inflammation
    • (2000) Science , vol.287 , pp. 1049-1053
    • Hirsch, E.1
  • 327
    • 0030613627 scopus 로고    scopus 로고
    • MIP-1α and MCP-1 differentially regulate acute and relapsing autoimmune encephalomyelitis as well as Th1/Th2 lymphocyte differentiation
    • (1997) J Leukoc Biol , vol.62 , pp. 681-687
    • Karpus, W.J.1    Kennedy, K.J.2
  • 330
    • 0031053586 scopus 로고    scopus 로고
    • Regulation of neuronal survival by the serine-threonine protein kinase Akt
    • (1997) Science , vol.275 , pp. 661-665
    • Dudek, H.1
  • 332
    • 0034708482 scopus 로고    scopus 로고
    • Akt/protein kinase B is regulated by autophosphorylation at the hypothetical PDK-2 site
    • (2000) J Biol Chem , vol.275 , pp. 8271-8274
    • Toker, A.1    Newton, A.C.2
  • 340
    • 0029795488 scopus 로고    scopus 로고
    • Regulation mechanism of E/R/M (ezrin/radixin/moesin) protein/plasma membrane association: Possible involvement of phosphatidylinositol turnover and rho-dependent signaling pathway
    • (1996) J Cell Biol , vol.135 , pp. 37-51
    • Hirao, M.1
  • 341
    • 14444288533 scopus 로고    scopus 로고
    • Molecular dissection of the Rho-associated protein kinase (p160ROCK)-regulated neurite remodeling in neuroblastoma N1E-115 cells
    • (1998) J Cell Biol , vol.141 , pp. 1625-1636
    • Hirose, M.1
  • 342
    • 0031048791 scopus 로고    scopus 로고
    • Formation of actin stress fibers and focal adhesions enhanced by Rho-kinase
    • (1997) Science , vol.275 , pp. 1308-1311
    • Amano, M.1
  • 344
    • 2642641315 scopus 로고    scopus 로고
    • The chemokine monocyte chemotactic protein 1 triggers Janus kinase 2 activation and tyrosine phosphorylation of the CCR2B receptor
    • (1998) J Immunol , vol.161 , pp. 805-813
    • Mellado, M.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.