메뉴 건너뛰기




Volumn 339, Issue 1, 2004, Pages 131-144

Regulation of LIP level and ROS formation through interaction of H-ferritin with G-CSF receptor

Author keywords

6 diamidino 2 , phenylindole; A2D, ataxin 2 domain; CA fluorescence, calcein AM fluorescence; CAT, chloramphenicol acetyltransferase; DAPI, 4 ; granulocyte colony stimulating factor; interaction; labile iron pool; reactive oxygen species; receptor

Indexed keywords

CELL SURFACE RECEPTOR; FERRITIN HEAVY CHAIN; GLUTATHIONE TRANSFERASE; GRANULOCYTE COLONY STIMULATING FACTOR RECEPTOR; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; HEMOPOIETIC GROWTH FACTOR; INTERLEUKIN 3; IRON CHELATING AGENT; IRON COMPLEX; ISOPROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; PHOSPHOPROTEIN PHOSPHATASE; PROTEIN KINASE C; PROTEIN SUBUNIT; REACTIVE OXYGEN METABOLITE; STAT3 PROTEIN; THROMBOPOIETIN; UNCLASSIFIED DRUG;

EID: 2342462210     PISSN: 00222836     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.jmb.2004.03.027     Document Type: Article
Times cited : (47)

References (30)
  • 1
    • 0029780711 scopus 로고    scopus 로고
    • Molecular analysis of the granulocyte colony-stimulating factor receptor
    • Avalos B.R. Molecular analysis of the granulocyte colony-stimulating factor receptor. Blood. 88:1996;761-777
    • (1996) Blood , vol.88 , pp. 761-777
    • Avalos, B.R.1
  • 2
    • 0033591347 scopus 로고    scopus 로고
    • Multiple signals mediate proliferation, differentiation, and survival from the granulocyte colony-stimulating factor receptor in myeloid 32D cells
    • Ward A.C., Smith L., Koning J.P., Aesch Y., Touw I.P. Multiple signals mediate proliferation, differentiation, and survival from the granulocyte colony-stimulating factor receptor in myeloid 32D cells. J. Biol. Chem. 274:1999;14956-14962
    • (1999) J. Biol. Chem. , vol.274 , pp. 14956-14962
    • Ward, A.C.1    Smith, L.2    Koning, J.P.3    Aesch, Y.4    Touw, I.P.5
  • 3
    • 0033555439 scopus 로고    scopus 로고
    • Defective internalization and sustained activation of truncated granulocyte colony-stimulating factor receptor found in severe congenital neutropenia/acute myeloid leukemia
    • Ward A.C., van Aesch Y.M., Schelen A.M., Touw I.P. Defective internalization and sustained activation of truncated granulocyte colony-stimulating factor receptor found in severe congenital neutropenia/acute myeloid leukemia. Blood. 93:1999;447-458
    • (1999) Blood , vol.93 , pp. 447-458
    • Ward, A.C.1    Van Aesch, Y.M.2    Schelen, A.M.3    Touw, I.P.4
  • 4
    • 0034161391 scopus 로고    scopus 로고
    • Activation of Akt kinase by granulocyte colony-stimulating factor (G-CSF): Evidence for the role of a tyrosine kinase activity distinct from the Janus kinases
    • Dong F., Larner A.C. Activation of Akt kinase by granulocyte colony-stimulating factor (G-CSF): evidence for the role of a tyrosine kinase activity distinct from the Janus kinases. Blood. 95:2000;1656-1662
    • (2000) Blood , vol.95 , pp. 1656-1662
    • Dong, F.1    Larner, A.C.2
  • 5
    • 0036156281 scopus 로고    scopus 로고
    • Distinct region of the granulocyte colony-stimulating factor receptor mediates proliferative signaling through activation of Janus kinase 2 and p44/42 mitogen-activated protein kinase
    • Koay D.C., Nguyen T., Sartorelli A.C. Distinct region of the granulocyte colony-stimulating factor receptor mediates proliferative signaling through activation of Janus kinase 2 and p44/42 mitogen-activated protein kinase. Cell. Signal. 14:2002;239-247
    • (2002) Cell. Signal. , vol.14 , pp. 239-247
    • Koay, D.C.1    Nguyen, T.2    Sartorelli, A.C.3
  • 6
    • 0038819107 scopus 로고    scopus 로고
    • The carboxy-terminal region of the granulocyte colony-stimulating factor receptor transduces a phagocytic signal
    • Santini V., Scappini B., Indik Z.K., Gozzini A., Ferrini P.R., Schreiber A.D. The carboxy-terminal region of the granulocyte colony-stimulating factor receptor transduces a phagocytic signal. Blood. 101:2003;4615-4621
    • (2003) Blood , vol.101 , pp. 4615-4621
    • Santini, V.1    Scappini, B.2    Indik, Z.K.3    Gozzini, A.4    Ferrini, P.R.5    Schreiber, A.D.6
  • 8
    • 0031059585 scopus 로고    scopus 로고
    • Newly delivered transferrin iron and oxidative cell injury
    • Breuer W., Greenberg E., Cabantchik Z.I. Newly delivered transferrin iron and oxidative cell injury. FEBS Letters. 403:1997;213-219
    • (1997) FEBS Letters , vol.403 , pp. 213-219
    • Breuer, W.1    Greenberg, E.2    Cabantchik, Z.I.3
  • 9
    • 0028973482 scopus 로고
    • Requirement for generation of H2O2 for platelet-derived growth factor signal transduction
    • Sundaresan M., Yu Z.X., Ferrans V.J., Irani K., Finkel T. Requirement for generation of H2O2 for platelet-derived growth factor signal transduction. Science. 270:1995;296-299
    • (1995) Science , vol.270 , pp. 296-299
    • Sundaresan, M.1    Yu, Z.X.2    Ferrans, V.J.3    Irani, K.4    Finkel, T.5
  • 11
    • 0001515988 scopus 로고    scopus 로고
    • Involvement of tyrosine phosphorylation and protein kinase C in the activation of phospholipase D by H2O2 in Swiss 3T3 fibroblasts
    • Min D.S., Kim E.G., Exton J.H. Involvement of tyrosine phosphorylation and protein kinase C in the activation of phospholipase D by H2O2 in Swiss 3T3 fibroblasts. J. Biol. Chem. 273:1998;29986-29994
    • (1998) J. Biol. Chem. , vol.273 , pp. 29986-29994
    • Min, D.S.1    Kim, E.G.2    Exton, J.H.3
  • 12
    • 0001952829 scopus 로고    scopus 로고
    • Redox signaling: Hydrogen peroxide as intracellular messenger
    • Rhee S.G. Redox signaling: hydrogen peroxide as intracellular messenger. Expt. Mol. Med. 31:1999;53-59
    • (1999) Expt. Mol. Med. , vol.31 , pp. 53-59
    • Rhee, S.G.1
  • 13
    • 0034733807 scopus 로고    scopus 로고
    • Redox-dependent signal transduction
    • Finkel T. Redox-dependent signal transduction. FEBS Letters. 476:2000;52-54
    • (2000) FEBS Letters , vol.476 , pp. 52-54
    • Finkel, T.1
  • 14
    • 0037430971 scopus 로고    scopus 로고
    • Oxidative stress in cell culture: An under-appreciated problem?
    • Halliwell B. Oxidative stress in cell culture: an under-appreciated problem? FEBS Letters. 540:2003;3-6
    • (2003) FEBS Letters , vol.540 , pp. 3-6
    • Halliwell, B.1
  • 15
    • 0142043984 scopus 로고    scopus 로고
    • Redox signaling and the MAP kinase pathways
    • Torres M., Forman H.J. Redox signaling and the MAP kinase pathways. Biofactors. 17:2003;287-296
    • (2003) Biofactors , vol.17 , pp. 287-296
    • Torres, M.1    Forman, H.J.2
  • 17
    • 0029790979 scopus 로고    scopus 로고
    • Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents
    • Knebel A., Rahmsdorf H.J., Ullrich A., Herrlich P. Dephosphorylation of receptor tyrosine kinases as target of regulation by radiation, oxidants or alkylating agents. EMBO J. 15:1996;5314-5325
    • (1996) EMBO J. , vol.15 , pp. 5314-5325
    • Knebel, A.1    Rahmsdorf, H.J.2    Ullrich, A.3    Herrlich, P.4
  • 18
    • 0037268178 scopus 로고    scopus 로고
    • Platelet-drived growth factor activates production of reactive oxygen species by NADPH oxidase in smooth muscle cells through Gi1,2
    • Kreuzer J., Viedt C., Brandes R.P., Seeger F., Rosenkranz A.S., Sauer H., et al. Platelet-drived growth factor activates production of reactive oxygen species by NADPH oxidase in smooth muscle cells through Gi1, 2. FASEB J. 17:2003;38-40
    • (2003) FASEB J. , vol.17 , pp. 38-40
    • Kreuzer, J.1    Viedt, C.2    Brandes, R.P.3    Seeger, F.4    Rosenkranz, A.S.5    Sauer, H.6
  • 20
    • 0031919849 scopus 로고    scopus 로고
    • Jaks and STATs: Biological implications
    • Leonard W.J., Oshea J.J. Jaks and STATs: biological implications. Annu. Rev. Immunol. 16:1998;293-322
    • (1998) Annu. Rev. Immunol. , vol.16 , pp. 293-322
    • Leonard, W.J.1    Oshea, J.J.2
  • 21
    • 0031605490 scopus 로고    scopus 로고
    • Ferritin. Uptake, storage, and release of iron
    • Chasteen N.D. Ferritin. Uptake, storage, and release of iron. Met. Ions Biol. Syst. 35:1998;479-514
    • (1998) Met. Ions Biol. Syst. , vol.35 , pp. 479-514
    • Chasteen, N.D.1
  • 22
    • 0037108199 scopus 로고    scopus 로고
    • The labile iron pool: Characterization, measurement, and participation in cellular processes
    • Kakhlon O., Cabantchik Z.I. The labile iron pool: characterization, measurement, and participation in cellular processes. Free Radic. Biol. Med. 33:2002;1037-1046
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 1037-1046
    • Kakhlon, O.1    Cabantchik, Z.I.2
  • 23
    • 0036884413 scopus 로고    scopus 로고
    • Macrophage-colony-stimulating factor-induced activation of extracellular-regulated kinase involves phosphatidylinositol 3-kinase and reactive oxygen species in human monocytes
    • Bhatt N.Y., Kelley T.W., Khramtsov V.V., Wang Y., Lam G.K., Clanton T.L., Marsh C.B. Macrophage-colony-stimulating factor-induced activation of extracellular-regulated kinase involves phosphatidylinositol 3-kinase and reactive oxygen species in human monocytes. J. Immunol. 169:2002;6427-6434
    • (2002) J. Immunol. , vol.169 , pp. 6427-6434
    • Bhatt, N.Y.1    Kelley, T.W.2    Khramtsov, V.V.3    Wang, Y.4    Lam, G.K.5    Clanton, T.L.6    Marsh, C.B.7
  • 24
    • 0027433327 scopus 로고
    • Growth and differentiation signals mediated by different regions in the cytoplasmic domain of granulocyte colony-stimulating factor receptor
    • Fukunaga R., Ishizaka-Ikeda E., Nagata S. Growth and differentiation signals mediated by different regions in the cytoplasmic domain of granulocyte colony-stimulating factor receptor. Cell. 74:1993;1079-1087
    • (1993) Cell , vol.74 , pp. 1079-1087
    • Fukunaga, R.1    Ishizaka-Ikeda, E.2    Nagata, S.3
  • 25
    • 0030013847 scopus 로고    scopus 로고
    • Bone sialoprotein stimulates in vitro bone resorption
    • Raynal C., Delmas P.D., Chenu C. Bone sialoprotein stimulates in vitro bone resorption. Endocrinology. 137:1996;2347-2354
    • (1996) Endocrinology , vol.137 , pp. 2347-2354
    • Raynal, C.1    Delmas, P.D.2    Chenu, C.3
  • 26
    • 0025940629 scopus 로고
    • The two-hybrid system: A method to identify and clone genes for proteins that interact with a protein of interest
    • Chien C.T., Bartel P.L., Sternglanz R., Fields S. The two-hybrid system: a method to identify and clone genes for proteins that interact with a protein of interest. Proc. Natl Acad. Sci. USA. 88:1991;9578-9582
    • (1991) Proc. Natl Acad. Sci. USA , vol.88 , pp. 9578-9582
    • Chien, C.T.1    Bartel, P.L.2    Sternglanz, R.3    Fields, S.4
  • 27
    • 0027251721 scopus 로고
    • The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit
    • Durfee T., Becherer K., Chen P.L., Yeh S.H., Yang Y., Kilburn A.E., et al. The retinoblastoma protein associates with the protein phosphatase type 1 catalytic subunit. Genes Dev. 7:1993;555-569
    • (1993) Genes Dev. , vol.7 , pp. 555-569
    • Durfee, T.1    Becherer, K.2    Chen, P.L.3    Yeh, S.H.4    Yang, Y.5    Kilburn, A.E.6
  • 28
    • 0028816076 scopus 로고
    • A non-isotopic, highly sensitive, fluorimetric, cell-cell adhesion microplate assay using calcein AM-labeled lymphocytes
    • Braut-Boucher F., Pichon J., Rat P., Adolphe M., Aubery M., Font J. A non-isotopic, highly sensitive, fluorimetric, cell-cell adhesion microplate assay using calcein AM-labeled lymphocytes. J. Immun. Methods. 178:1995;41-51
    • (1995) J. Immun. Methods , vol.178 , pp. 41-51
    • Braut-Boucher, F.1    Pichon, J.2    Rat, P.3    Adolphe, M.4    Aubery, M.5    Font, J.6
  • 30
    • 0027249757 scopus 로고
    • Evaluation of 2′,7′-dichlorofluorescin and dihydrorhodamine 123 as fluorescent probes for intracellular H2O2 in cultured endothelial cells
    • Royall J.A., Ischiropoulos H. Evaluation of 2′, 7′-dichlorofluorescin and dihydrorhodamine 123 as fluorescent probes for intracellular H2O2 in cultured endothelial cells. Arch. Biochem. Biophys. 302:1993;348-355
    • (1993) Arch. Biochem. Biophys. , vol.302 , pp. 348-355
    • Royall, J.A.1    Ischiropoulos, H.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.