메뉴 건너뛰기




Volumn 89, Issue 9, 1997, Pages 3434-3442

Focal adhesion kinase upregulated by granulocyte-macrophage colony- stimulating factor but not by interleukin-3 in differentiating myeloid cells

Author keywords

[No Author keywords available]

Indexed keywords

FOCAL ADHESION KINASE; GRANULOCYTE MACROPHAGE COLONY STIMULATING FACTOR; INTERLEUKIN 3;

EID: 0030968133     PISSN: 00064971     EISSN: None     Source Type: Journal    
DOI: 10.1182/blood.v89.9.3434     Document Type: Article
Times cited : (23)

References (43)
  • 1
    • 0025376378 scopus 로고
    • Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases
    • Kanner SB, Reynolds AB, Vines RR, Parsons JT: Monoclonal antibodies to individual tyrosine-phosphorylated protein substrates of oncogene-encoded tyrosine kinases. Proc Natl Acad Sci USA 87:3328, 1990
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 3328
    • Kanner, S.B.1    Reynolds, A.B.2    Vines, R.R.3    Parsons, J.T.4
  • 3
    • 0026674919 scopus 로고
    • Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin
    • Hanks SK, Calalb MB, Harper MC, Patel SK: Focal adhesion protein-tyrosine kinase phosphorylated in response to cell attachment to fibronectin. Proc Natl Acad Sci USA 89:8487, 1992
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 8487
    • Hanks, S.K.1    Calalb, M.B.2    Harper, M.C.3    Patel, S.K.4
  • 4
    • 0026249489 scopus 로고
    • Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein
    • Guan JL, Trevithick JE, Hynes RO: Fibronectin/integrin interaction induces tyrosine phosphorylation of a 120-kDa protein. Cell Regul 2:951, 1991
    • (1991) Cell Regul , vol.2 , pp. 951
    • Guan, J.L.1    Trevithick, J.E.2    Hynes, R.O.3
  • 5
    • 0027055575 scopus 로고
    • Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase
    • Kornberg L, Earp HS, Parsons JT, Schaller M, Juliano RL: Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J Biol Chem 267:23439, 1992
    • (1992) J Biol Chem , vol.267 , pp. 23439
    • Kornberg, L.1    Earp, H.S.2    Parsons, J.T.3    Schaller, M.4    Juliano, R.L.5
  • 6
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer DD, Hanks SK, Hunter T, van der Geer P: Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 372:786, 1994
    • (1994) Nature , vol.372 , pp. 786
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    Van Der Geer, P.4
  • 7
    • 0026700191 scopus 로고
    • Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells
    • Zachary I, Sinnett-Smith J, Rozengurt E: Bombesin, vasopressin, and endothelin stimulation of tyrosine phosphorylation in Swiss 3T3 cells. J Biol Chem 267:19031, 1992
    • (1992) J Biol Chem , vol.267 , pp. 19031
    • Zachary, I.1    Sinnett-Smith, J.2    Rozengurt, E.3
  • 8
    • 0029068160 scopus 로고
    • Differential effects of platelet-derived growth factor BB on p 125 focal adhesion kinase and paxillin tyrosine phosphorylation and on cell migration in rabbit aortic vascular smooth muscle cells and Swiss 3T3 fibroblasts
    • Abedi H, Dawes KE, Zachary I: Differential effects of platelet-derived growth factor BB on p 125 focal adhesion kinase and paxillin tyrosine phosphorylation and on cell migration in rabbit aortic vascular smooth muscle cells and Swiss 3T3 fibroblasts. J Biol Chem 270:11367, 1995
    • (1995) J Biol Chem , vol.270 , pp. 11367
    • Abedi, H.1    Dawes, K.E.2    Zachary, I.3
  • 10
    • 0026759309 scopus 로고
    • Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation
    • Guan JL, Shalloway D: Regulation of focal adhesion-associated protein tyrosine kinase by both cellular adhesion and oncogenic transformation. Nature 358:690, 1992
    • (1992) Nature , vol.358 , pp. 690
    • Guan, J.L.1    Shalloway, D.2
  • 11
    • 0026476697 scopus 로고
    • FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes
    • FAK): A point of convergence in the action of neuropeptides, integrins, and oncogenes. Cell 71:891, 1992
    • (1992) Cell , vol.71 , pp. 891
    • Zachary, I.1    Rozengurt, E.2
  • 13
    • 0027242121 scopus 로고
    • Tyrosine phosphorylation and cytoskeletal reorganization in platelets are triggered by interaction of integrin receptors with their immobilized ligands
    • Haimovich B, Lipfert L, Brugge JS, Shattil SJ: Tyrosine phosphorylation and cytoskeletal reorganization in platelets are triggered by interaction of integrin receptors with their immobilized ligands. J Biol Chem 268:15868, 1993
    • (1993) J Biol Chem , vol.268 , pp. 15868
    • Haimovich, B.1    Lipfert, L.2    Brugge, J.S.3    Shattil, S.J.4
  • 15
    • 0027996890 scopus 로고
    • Lymphocyte antigen receptor activation of a focal adhesion kinase-related tyrosine kinase-substrate
    • Kanner SB, Aruffo A, Chan PY: Lymphocyte antigen receptor activation of a focal adhesion kinase-related tyrosine kinase-substrate. Proc Natl Acad Sci USA 91:10484, 1994
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10484
    • Kanner, S.B.1    Aruffo, A.2    Chan, P.Y.3
  • 16
    • 0028839191 scopus 로고
    • Integrin stimulation decreases tyrosine phosphorylation and activity of focal adhesion kinase in thymocytes
    • Kanazawa S, Ilic D, Noumura T, Yamamoto T, Aizawa S: Integrin stimulation decreases tyrosine phosphorylation and activity of focal adhesion kinase in thymocytes. Biochem Biophys Res Commun 215:438, 1995
    • (1995) Biochem Biophys Res Commun , vol.215 , pp. 438
    • Kanazawa, S.1    Ilic, D.2    Noumura, T.3    Yamamoto, T.4    Aizawa, S.5
  • 18
    • 0027340002 scopus 로고
    • FAK by the aggregation of high affinity immunoglobulin e receptors requires cell adherence
    • FAK by the aggregation of high affinity immunoglobulin E receptors requires cell adherence. J Biol Chem 268:6851, 1993
    • (1993) J Biol Chem , vol.268 , pp. 6851
    • Hamawy, M.M.1    Mergenhagen, S.E.2    Siraganian, R.P.3
  • 19
    • 0028079740 scopus 로고
    • The aggregation of the high affinity IgE receptor induces tyrosine phosphorylation of paxillin, a focal adhesion protein
    • Hamawy MM, Swaim WD, Minoguchi K, de Feijter AW, Mergenhagen SE, Siraganian RP: The aggregation of the high affinity IgE receptor induces tyrosine phosphorylation of paxillin, a focal adhesion protein. J Immunol 153:4655, 1994
    • (1994) J Immunol , vol.153 , pp. 4655
    • Hamawy, M.M.1    Swaim, W.D.2    Minoguchi, K.3    De Feijter, A.W.4    Mergenhagen, S.E.5    Siraganian, R.P.6
  • 21
    • 0027273886 scopus 로고
    • Expression of a gene encoding a unique protein-tyrosine kinase within specific fetal- and adult-derived hematopoietic lineages
    • Choi K, Kennedy M, Keller G: Expression of a gene encoding a unique protein-tyrosine kinase within specific fetal- and adult-derived hematopoietic lineages. Proc Natl Acad Sci USA 90:5747, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 5747
    • Choi, K.1    Kennedy, M.2    Keller, G.3
  • 22
    • 0025772979 scopus 로고
    • In utero manipulation of coat color formation by a monoclonal anti-c-kit antibody: Two distinct waves of c-kit-dependency during melanocyte development
    • Nishikawa S, Kusakabe M, Yoshinaga K, Ogawa M, Hayashi S, Kunisada T, Era T, Sakakura T, Nishikawa S: In utero manipulation of coat color formation by a monoclonal anti-c-kit antibody: Two distinct waves of c-kit-dependency during melanocyte development. EMBO J 10:2111, 1991
    • (1991) EMBO J , vol.10 , pp. 2111
    • Nishikawa, S.1    Kusakabe, M.2    Yoshinaga, K.3    Ogawa, M.4    Hayashi, S.5    Kunisada, T.6    Era, T.7    Sakakura, T.8    Nishikawa, S.9
  • 24
    • 0023277545 scopus 로고
    • Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction
    • Chomczynski P, Sacchi N: Single-step method of RNA isolation by acid guanidium thiocyanate-phenol-chloroform extraction. Anal Biochem 162:156, 1987
    • (1987) Anal Biochem , vol.162 , pp. 156
    • Chomczynski, P.1    Sacchi, N.2
  • 25
    • 0023905495 scopus 로고
    • Transcription of the dystrophin gene in human muscle and non-muscle tissue
    • Chelly J, Kaplan JC, Maire P, Gautron S, Kahn A: Transcription of the dystrophin gene in human muscle and non-muscle tissue. Nature 333:858, 1988
    • (1988) Nature , vol.333 , pp. 858
    • Chelly, J.1    Kaplan, J.C.2    Maire, P.3    Gautron, S.4    Kahn, A.5
  • 26
  • 27
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680, 1970
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 28
    • 0009482260 scopus 로고
    • Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications
    • Towbin H, Staehelin T, Gordon J: Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: Procedure and some applications. Proc Natl Acad Sci USA 76:4350, 1979
    • (1979) Proc Natl Acad Sci USA , vol.76 , pp. 4350
    • Towbin, H.1    Staehelin, T.2    Gordon, J.3
  • 30
    • 0018885287 scopus 로고
    • A 48-well micro chemotaxis assembly for rapid and accurate measurement of leukocyte migration
    • Falk W, Goodwin RH, Leonard EJ: A 48-well micro chemotaxis assembly for rapid and accurate measurement of leukocyte migration. J Immunol Method 33:239, 1980
    • (1980) J Immunol Method , vol.33 , pp. 239
    • Falk, W.1    Goodwin, R.H.2    Leonard, E.J.3
  • 31
    • 0019422743 scopus 로고
    • Monocyte responsiveness to chemotactic stimuli is a property of a subpopulation of cells that can respond to multiple chemoattractants
    • Cianciolo GJ, Snyderman R: Monocyte responsiveness to chemotactic stimuli is a property of a subpopulation of cells that can respond to multiple chemoattractants. J Clin Invest 67:60, 1981
    • (1981) J Clin Invest , vol.67 , pp. 60
    • Cianciolo, G.J.1    Snyderman, R.2
  • 33
    • 0029096541 scopus 로고
    • Cloning and characterization of cell adhesion kinase β, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily
    • Sasaki H, Nagura K, Ishino M, Tobioka H, Kotani K, Sasaki T: Cloning and characterization of cell adhesion kinase β, a novel protein-tyrosine kinase of the focal adhesion kinase subfamily. J Biol Chem 270:21206, 1995
    • (1995) J Biol Chem , vol.270 , pp. 21206
    • Sasaki, H.1    Nagura, K.2    Ishino, M.3    Tobioka, H.4    Kotani, K.5    Sasaki, T.6
  • 35
  • 36
    • 0027489710 scopus 로고
    • Receptors for granulocyte-macrophage colony-stimulating factor, interleukin-3, and interleukin-5
    • Miyajima A, Mui ALF, Ogorochi T, Sakamaki K: Receptors for granulocyte-macrophage colony-stimulating factor, interleukin-3, and interleukin-5. Blood 82:1960, 1993
    • (1993) Blood , vol.82 , pp. 1960
    • Miyajima, A.1    Mui, A.L.F.2    Ogorochi, T.3    Sakamaki, K.4
  • 37
    • 0028845212 scopus 로고
    • Cytokine receptor signaling
    • Ihle JN: Cytokine receptor signaling. Nature 377:591, 1995
    • (1995) Nature , vol.377 , pp. 591
    • Ihle, J.N.1
  • 39
    • 0029073476 scopus 로고
    • Evidence for a signaling role for the α chains of a granulocyte-macrophage colony-stimulating factor (GM-CSF), interleukin-3 (IL-3), and IL-5 receptors: Divergent signaling pathways between GM-CSF/IL-3 and IL-5
    • Mire-Sluis A, Page LA, Wadhwa M, Thorpe R: Evidence for a signaling role for the α chains of a granulocyte-macrophage colony-stimulating factor (GM-CSF), interleukin-3 (IL-3), and IL-5 receptors: Divergent signaling pathways between GM-CSF/IL-3 and IL-5. Blood 86:2679, 1995
    • (1995) Blood , vol.86 , pp. 2679
    • Mire-Sluis, A.1    Page, L.A.2    Wadhwa, M.3    Thorpe, R.4
  • 41
    • 0028241389 scopus 로고
    • Hyaluronan and the hyaluronan receptor RHAMM promote focal adhesion turnover and transient tyrosine kinase activity
    • Hall CL, Wang C, Lange LA, Turley EA: Hyaluronan and the hyaluronan receptor RHAMM promote focal adhesion turnover and transient tyrosine kinase activity. J Cell Biol 126:575, 1994
    • (1994) J Cell Biol , vol.126 , pp. 575
    • Hall, C.L.1    Wang, C.2    Lange, L.A.3    Turley, E.A.4
  • 42
    • 0028783271 scopus 로고
    • Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK
    • Furuta Y, Ilic D, Kanazawa S, Takeda N, Yamamoto T, Aizawa S: Mesodermal defect in late phase of gastrulation by a targeted mutation of focal adhesion kinase, FAK. Oncogene 11:1989, 1995
    • (1995) Oncogene , vol.11 , pp. 1989
    • Furuta, Y.1    Ilic, D.2    Kanazawa, S.3    Takeda, N.4    Yamamoto, T.5    Aizawa, S.6
  • 43
    • 0028048369 scopus 로고
    • Generation of lymphohematopoietic cells from embryonic stem cells in culture
    • Nakano T, Kodama H, Honjo T: Generation of lymphohematopoietic cells from embryonic stem cells in culture. Science 265:1098, 1994
    • (1994) Science , vol.265 , pp. 1098
    • Nakano, T.1    Kodama, H.2    Honjo, T.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.