메뉴 건너뛰기




Volumn 83, Issue 1, 1996, Pages 13-21

Upmodulation of αvβ1 integrin on human tumor cells by leukemia inhibitory factor (LIF) and oncostatin M (OSM);MODULATION DE L'EXPRESSION DE L'INTEGRINE αVβ1 A LA SURFACE DES CELLULES CANCEREUSES HUMAINES PAR LE LEUKEMIA INHIBITORY FACTOR (LIF) ET L'ONCOSTATINE M (OSM)

Author keywords

integrins; LIF; oncostatin M; tumor cells

Indexed keywords

INTEGRIN; LEUKEMIA INHIBITORY FACTOR; MONOCLONAL ANTIBODY; ONCOSTATIN M; TUMOR NECROSIS FACTOR ALPHA;

EID: 0030052905     PISSN: 00074551     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (7)

References (41)
  • 1
    • 0023612884 scopus 로고
    • Biosynthesis and acquisition of biological activity of the fibronectin receptor
    • Akiyama SK, Yamada KM. Biosynthesis and acquisition of biological activity of the fibronectin receptor. J Biol Chem 1987;262:17536-42
    • (1987) J Biol Chem , vol.262 , pp. 17536-17542
    • Akiyama, S.K.1    Yamada, K.M.2
  • 2
    • 0027395858 scopus 로고
    • Biology of disease. Role of integrins and other cell adhesion molecules in tumor progression and metastasis
    • Albelda SM. Biology of disease. Role of integrins and other cell adhesion molecules in tumor progression and metastasis. Lab Invest 1993;68:4-17
    • (1993) Lab Invest , vol.68 , pp. 4-17
    • Albelda, S.M.1
  • 3
    • 0024400598 scopus 로고
    • Hepatocyte stimulating factor II shares structural and functional identity with leukemia inhibitory factor
    • Baumann H, Wong GG. Hepatocyte stimulating factor II shares structural and functional identity with leukemia inhibitory factor. J Immunol 1989;143:1163-7
    • (1989) J Immunol , vol.143 , pp. 1163-1167
    • Baumann, H.1    Wong, G.G.2
  • 4
    • 0027469531 scopus 로고
    • Reconstitution of the response to leukemia inhibitory factor, oncostatin M, ciliary neurotrophic factor in hepatoma cells
    • Baumann H, Ziegler SF, Mosley B, Morella KK, Pajovic S, Gearing DP. Reconstitution of the response to leukemia inhibitory factor, oncostatin M, ciliary neurotrophic factor in hepatoma cells. J Biol Chem 1993;268:8414-7
    • (1993) J Biol Chem , vol.268 , pp. 8414-8417
    • Baumann, H.1    Ziegler, S.F.2    Mosley, B.3    Morella, K.K.4    Pajovic, S.5    Gearing, D.P.6
  • 5
    • 0026322355 scopus 로고
    • Shedding of ICAM-1 from human melanoma cell lines induced by interferon-γ and tumor necrosis factor-α. Functional consequences on cell-mediated cytotoxicity
    • Becker JC, Dummer R, Hartmann AA, Burg G, Schmidt RE. Shedding of ICAM-1 from human melanoma cell lines induced by interferon-γ and tumor necrosis factor-α. Functional consequences on cell-mediated cytotoxicity. J Immunol 1991;147:4398-401
    • (1991) J Immunol , vol.147 , pp. 4398-4401
    • Becker, J.C.1    Dummer, R.2    Hartmann, A.A.3    Burg, G.4    Schmidt, R.E.5
  • 6
    • 0024323254 scopus 로고
    • Synthesis and expression of the fibroblast fibronectin receptor in human monocytes
    • Brown DL, Phillips DR, Damsky CH, Charo IF. Synthesis and expression of the fibroblast fibronectin receptor in human monocytes. J Clin Invest 1989;84:366-70
    • (1989) J Clin Invest , vol.84 , pp. 366-370
    • Brown, D.L.1    Phillips, D.R.2    Damsky, C.H.3    Charo, I.F.4
  • 7
    • 0023463846 scopus 로고
    • Cell surface receptors for extracellular matrix molecules
    • Buck CA, Howitz AF. Cell surface receptors for extracellular matrix molecules. Annu Rev Cell Biol 1987;13:179-205
    • (1987) Annu Rev Cell Biol , vol.13 , pp. 179-205
    • Buck, C.A.1    Howitz, A.F.2
  • 8
    • 0025301327 scopus 로고
    • Isolation of a novel integrin receptor mediating arg-gly-asp directed cell adhesion to fibronectin and type I collagen from human neuroblastoma cells. Association of a novel β1 related subunit with αv
    • Dedhar S, Gray V. Isolation of a novel integrin receptor mediating arg-gly-asp directed cell adhesion to fibronectin and type I collagen from human neuroblastoma cells. Association of a novel β1 related subunit with αv. J Cell Biol 1990;110:2185-93
    • (1990) J Cell Biol , vol.110 , pp. 2185-2193
    • Dedhar, S.1    Gray, V.2
  • 9
    • 0025138216 scopus 로고
    • Alterations in integrin receptor expression on chemical transformed human cells: Specific enhancement of laminin and collagen receptors
    • Dedhar S, Saulnier R. Alterations in integrin receptor expression on chemical transformed human cells: specific enhancement of laminin and collagen receptors. J Cell Biol 1990;110:481-9
    • (1990) J Cell Biol , vol.110 , pp. 481-489
    • Dedhar, S.1    Saulnier, R.2
  • 10
    • 0022574146 scopus 로고
    • Induction by IL-1 and interferon-γ. tissue distribution, biochemistry and function of a natural adherence molecule (ICAM-1)
    • Dustin ML, Rothlein R, Bhan AK, Dinarello CA, Springer TA. Induction by IL-1 and interferon-γ. tissue distribution, biochemistry and function of a natural adherence molecule (ICAM-1). J Immunol 1986;137:245-54
    • (1986) J Immunol , vol.137 , pp. 245-254
    • Dustin, M.L.1    Rothlein, R.2    Bhan, A.K.3    Dinarello, C.A.4    Springer, T.A.5
  • 11
    • 0026020583 scopus 로고
    • Receptors functions for the integrin VLA-3: Fibronectin, collagen and laminin binding are differentially influenced by RGD peptide and divalent cations
    • Elices MJ, Urry LA, Hemler ME. Receptors functions for the integrin VLA-3: fibronectin, collagen and laminin binding are differentially influenced by RGD peptide and divalent cations. J Cell Biol 1991;112:169-81
    • (1991) J Cell Biol , vol.112 , pp. 169-181
    • Elices, M.J.1    Urry, L.A.2    Hemler, M.E.3
  • 12
    • 0026519068 scopus 로고
    • Oncostatin M binds the high-affinity leukemia inhibitory factor receptor
    • Gearing DP, Bruce. Oncostatin M binds the high-affinity leukemia inhibitory factor receptor. New Biol 1992;4:61-5
    • (1992) New Biol , vol.4 , pp. 61-65
    • Gearing, D.P.1    Bruce2
  • 13
    • 0026506566 scopus 로고
    • The IL-6 signal transducer, gp130: An oncostatin M receptor and affinity converter for the LIF receptor
    • Gearing DP, Comeau MR, Friend DJ et al. The IL-6 signal transducer, gp130: an oncostatin M receptor and affinity converter for the LIF receptor. Science 1992;255:1434-7
    • (1992) Science , vol.255 , pp. 1434-1437
    • Gearing, D.P.1    Comeau, M.R.2    Friend, D.J.3
  • 14
    • 0027958212 scopus 로고
    • Proliferative response and binding properties of hematopoietic cells transfected with low-affinity receptors for leukemia inhibitory factor, oncostatin M and ciliary neurotrophic factor
    • Gearing DP, Ziegler SF, Comeau MR et al. Proliferative response and binding properties of hematopoietic cells transfected with low-affinity receptors for leukemia inhibitory factor, oncostatin M and ciliary neurotrophic factor. Proc Natl Acad Sci USA 1994;91:1119-23
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 1119-1123
    • Gearing, D.P.1    Ziegler, S.F.2    Comeau, M.R.3
  • 15
    • 0025214421 scopus 로고
    • Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells
    • Giancotti FG, Ruoslahti E. Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells. Cell 1990;60:849-54
    • (1990) Cell , vol.60 , pp. 849-854
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 16
    • 0026688515 scopus 로고
    • High and low affinity receptors for human interleukin for DA cells/leukemia inhibitory factor on human cells: Molecular characterization and cellular distribution
    • Godard A, Heymann D, Raher S et al. High and low affinity receptors for human interleukin for DA cells/leukemia inhibitory factor on human cells: molecular characterization and cellular distribution. J Biol Chem 1992;267: 3214-22
    • (1992) J Biol Chem , vol.267 , pp. 3214-3222
    • Godard, A.1    Heymann, D.2    Raher, S.3
  • 17
    • 0024788078 scopus 로고
    • Transforming growth factor-β switches the pattern of integrins expressed in MG-63 human osteosarcoma cells and causes a selective lost of cell adhesion to laminin
    • Heino J, Massagué J. Transforming growth factor-β switches the pattern of integrins expressed in MG-63 human osteosarcoma cells and causes a selective lost of cell adhesion to laminin. J Biol Chem 1989;264:21806-11
    • (1989) J Biol Chem , vol.264 , pp. 21806-21811
    • Heino, J.1    Massagué, J.2
  • 18
    • 0024534130 scopus 로고
    • Regulation of cell adhesion receptors by transforming growth factor-β
    • Heino J, Ignotz RA, Hemler ME, Crouse C, Massagué J. Regulation of cell adhesion receptors by transforming growth factor-β. J Biol Chem 1989;264:380-8
    • (1989) J Biol Chem , vol.264 , pp. 380-388
    • Heino, J.1    Ignotz, R.A.2    Hemler, M.E.3    Crouse, C.4    Massagué, J.5
  • 19
    • 0021267104 scopus 로고
    • Glycoproteins of 210,000 and 130,000 MW on activated T cells: Cell distribution and antigenic relation to components on resting cells and T cell lines
    • Hemler ME, Sanchez-Madrid F, Flotte TJ et al. Glycoproteins of 210,000 and 130,000 MW on activated T cells: Cell distribution and antigenic relation to components on resting cells and T cell lines. J Immunol 1984;132:3011-8
    • (1984) J Immunol , vol.132 , pp. 3011-3018
    • Hemler, M.E.1    Sanchez-Madrid, F.2    Flotte, T.J.3
  • 20
    • 0028921009 scopus 로고
    • Human interleukin for DA cells/leukemia inhibitory factor and oncostatin M enhance membrane expression of intercellular adhesion molecule-1 on melanoma cells but not the shedding of its soluble form
    • Heymann D, Godard A, Raher S et al. Human interleukin for DA cells/leukemia inhibitory factor and oncostatin M enhance membrane expression of intercellular adhesion molecule-1 on melanoma cells but not the shedding of its soluble form. Cytokine 1995;7:111-7
    • (1995) Cytokine , vol.7 , pp. 111-117
    • Heymann, D.1    Godard, A.2    Raher, S.3
  • 21
    • 0024495948 scopus 로고
    • Regulation of cell adhesion receptors by transforming growth factor-β
    • Ignotz RA, Heino J, Massagué J. Regulation of cell adhesion receptors by transforming growth factor-β. J Biol Chem 1989;264:389-92
    • (1989) J Biol Chem , vol.264 , pp. 389-392
    • Ignotz, R.A.1    Heino, J.2    Massagué, J.3
  • 22
    • 0023583855 scopus 로고
    • Membrane receptors for extracellular matrix macromolecules: Relationship to cell adhesion and tumor metastasis
    • Juliano R. Membrane receptors for extracellular matrix macromolecules: relationship to cell adhesion and tumor metastasis. Biochem Biophys Acta 1987;907:261-78
    • (1987) Biochem Biophys Acta , vol.907 , pp. 261-278
    • Juliano, R.1
  • 23
    • 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 1970; 227:680-5
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 24
    • 0022656975 scopus 로고
    • Tumor invasion and metastases: Role of the extracellular matrix; Rhoads memorial award lecture
    • Liotta L. Tumor invasion and metastases: role of the extracellular matrix; Rhoads memorial award lecture. Cancer Res 1986;46:1-7
    • (1986) Cancer Res , vol.46 , pp. 1-7
    • Liotta, L.1
  • 25
    • 0025718892 scopus 로고
    • Integrin expression in human melanoma cell lines: Heterogeneity of vitronectin receptor composition and function
    • Marshall JF, Nesbitt SA, Helfrich MH, Horton MA, Polakova K, Hart IR. Integrin expression in human melanoma cell lines: heterogeneity of vitronectin receptor composition and function. Int J Cancer 1991;49:924-31
    • (1991) Int J Cancer , vol.49 , pp. 924-931
    • Marshall, J.F.1    Nesbitt, S.A.2    Helfrich, M.H.3    Horton, M.A.4    Polakova, K.5    Hart, I.R.6
  • 26
    • 0026062441 scopus 로고
    • Heterogeneity for integrin expression and cytokine-mediated VLA modulation can influence the adhesion of human melanoma cells to extracellular matrix proteins
    • Mortarini R, Anichini A, Parmiani G. Heterogeneity for integrin expression and cytokine-mediated VLA modulation can influence the adhesion of human melanoma cells to extracellular matrix proteins. Int J Cancer 1991;47:551-9
    • (1991) Int J Cancer , vol.47 , pp. 551-559
    • Mortarini, R.1    Anichini, A.2    Parmiani, G.3
  • 27
    • 0023095251 scopus 로고
    • Tumor cell instability, diversification and progression to the metastatic phenotypes: From oncogene to oncofetal expression
    • Nicolson GL. Tumor cell instability, diversification and progression to the metastatic phenotypes: from oncogene to oncofetal expression. Cancer Res 1987;47:1473-87
    • (1987) Cancer Res , vol.47 , pp. 1473-1487
    • Nicolson, G.L.1
  • 28
    • 9044246542 scopus 로고
    • Changes in integrin receptors on oncogenically transformed cells
    • Plantfaber LC, Hynes RO. Changes in integrin receptors on oncogenically transformed cells. Cell 1989;309:30-3
    • (1989) Cell , vol.309 , pp. 30-33
    • Plantfaber, L.C.1    Hynes, R.O.2
  • 29
    • 0026051784 scopus 로고
    • Oncostatin M is a member of a cytokine family which includes leukemia inhibitory factor, granulocyte colony stimulating factor and interleukin-6
    • Rose TM, Bruce AG. Oncostatin M is a member of a cytokine family which includes leukemia inhibitory factor, granulocyte colony stimulating factor and interleukin-6. Proc Natl Acad Sci USA 1991;88:8641-5
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 8641-8645
    • Rose, T.M.1    Bruce, A.G.2
  • 30
    • 0027365760 scopus 로고
    • Modulation of αvβ1, α2β1 and α3β1 integrin heterodimers during human neuroblastoma cell differentiation
    • Rozzo C, Ratti P, Ponzoni M, Corneglia-Ferraris. Modulation of αvβ1, α2β1 and α3β1 integrin heterodimers during human neuroblastoma cell differentiation. FEBS Lett 1993; 332:263-7
    • (1993) FEBS Lett , vol.332 , pp. 263-267
    • Rozzo, C.1    Ratti, P.2    Ponzoni, M.3    Corneglia-Ferraris4
  • 31
    • 0024150891 scopus 로고
    • Structure and biology of proteoglycans
    • Ruoslahti E. Structure and biology of proteoglycans. Annu Rev Cell Biol 1988;4:229-55
    • (1988) Annu Rev Cell Biol , vol.4 , pp. 229-255
    • Ruoslahti, E.1
  • 33
    • 0024957290 scopus 로고
    • Integrins and tumor cell dissemination
    • Ruoslahti E, Giancotti FG. Integrins and tumor cell dissemination. Cancer Cells 1989;1:119-26
    • (1989) Cancer Cells , vol.1 , pp. 119-126
    • Ruoslahti, E.1    Giancotti, F.G.2
  • 34
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti E, Pierschbacher MD. New perspectives in cell adhesion: RGD and integrins. Science 1987;238:491-7
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 35
    • 0026343904 scopus 로고
    • Regulation of integrin-type cell adhesion receptors by cytokines
    • Santala P, Heino J. Regulation of integrin-type cell adhesion receptors by cytokines. J Biol Chem 1991;34:23505-9
    • (1991) J Biol Chem , vol.34 , pp. 23505-23509
    • Santala, P.1    Heino, J.2
  • 36
    • 0023664709 scopus 로고
    • A complex of platelet glycoproteins Ic and IIa identified by a rat monoclonal antibody
    • Sonnenberg A, Janssen H, Hogervorst F, Calafat J, Hilgers J. A complex of platelet glycoproteins Ic and IIa identified by a rat monoclonal antibody. J Biol Chem 1987;262: 10376-83
    • (1987) J Biol Chem , vol.262 , pp. 10376-10383
    • Sonnenberg, A.1    Janssen, H.2    Hogervorst, F.3    Calafat, J.4    Hilgers, J.5
  • 37
    • 0025214681 scopus 로고
    • A novel fibronectin receptor with an unexpected subunit composition (αvβ1)
    • Vogel BE, Tarone G, Giancotti FG, Gaillit J, Ruoslahti E. A novel fibronectin receptor with an unexpected subunit composition (αvβ1). J Biol Chem 1990;265:5934-7
    • (1990) J Biol Chem , vol.265 , pp. 5934-5937
    • Vogel, B.E.1    Tarone, G.2    Giancotti, F.G.3    Gaillit, J.4    Ruoslahti, E.5
  • 38
    • 0028173629 scopus 로고
    • Role of the integrin αvβ6 in cell attachment to fibronectin. Heterologous expression of intact and secreted forms of the receptor
    • Weinacker A, Chen A, Agrez M et al. Role of the integrin αvβ6 in cell attachment to fibronectin. Heterologous expression of intact and secreted forms of the receptor. J Biol Chem 1994;269:6940-8
    • (1994) J Biol Chem , vol.269 , pp. 6940-6948
    • Weinacker, A.1    Chen, A.2    Agrez, M.3
  • 39
    • 0021267179 scopus 로고
    • Dualistic nature of adhesive protein function: Fibronectin and its biologically active peptide fragments can auto inhibit fibronectin function
    • Yamada KM, Kennedy DW. Dualistic nature of adhesive protein function: fibronectin and its biologically active peptide fragments can auto inhibit fibronectin function. J Cell Biol 1984;99:29-36
    • (1984) J Cell Biol , vol.99 , pp. 29-36
    • Yamada, K.M.1    Kennedy, D.W.2
  • 40
    • 0024790913 scopus 로고
    • The cholinergic neuronal differentiation factor from heart cells is identical to leukemia inhibitory factor
    • Yamamori T, Fukada K, Aebersold R, Korshing S, Fann MJ, Patterson P. The cholinergic neuronal differentiation factor from heart cells is identical to leukemia inhibitory factor. Science 1989;246:1412-6
    • (1989) Science , vol.246 , pp. 1412-1416
    • Yamamori, T.1    Fukada, K.2    Aebersold, R.3    Korshing, S.4    Fann, M.J.5    Patterson, P.6
  • 41
    • 0027175838 scopus 로고
    • The αvβ1 integrin functions as a fibronectin receptor but does not support fibronectin matrix assembly and cell migration on fibronectin
    • Zhang Z, Morla AO, Vuori K, Bauer JS, Juliano RL, Ruoslahti E. The αvβ1 integrin functions as a fibronectin receptor but does not support fibronectin matrix assembly and cell migration on fibronectin. J Cell Biol 1993;122:235-42
    • (1993) J Cell Biol , vol.122 , pp. 235-242
    • Zhang, Z.1    Morla, A.O.2    Vuori, K.3    Bauer, J.S.4    Juliano, R.L.5    Ruoslahti, E.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.