메뉴 건너뛰기




Volumn 51, Issue 5, 1997, Pages 1413-1417

Integrins as signaling molecules and targets for tumor therapy

Author keywords

[No Author keywords available]

Indexed keywords

FIBRONECTIN; INTEGRIN;

EID: 0030908029     PISSN: 00852538     EISSN: None     Source Type: Journal    
DOI: 10.1038/ki.1997.193     Document Type: Article
Times cited : (87)

References (44)
  • 2
    • 0026770377 scopus 로고
    • Integrin: Versatility, modulation, and signaling in cell adhesion
    • R.O. Hynes Integrin: Versatility, modulation, and signaling in cell adhesion Cell 69 1992 11 25
    • (1992) Cell , vol.69 , pp. 11-25
    • Hynes, R.O.1
  • 3
    • 0029775681 scopus 로고    scopus 로고
    • RGD and other recognition sequences for integrins
    • E. Ruoslahti RGD and other recognition sequences for integrins Ann Rev Cell Biol 12 1996 697 715
    • (1996) Ann Rev Cell Biol , vol.12 , pp. 697-715
    • Ruoslahti, E.1
  • 4
    • 0027459771 scopus 로고
    • Signal transduction from the extracellular matrix
    • R.L. Juliano S. Haskill Signal transduction from the extracellular matrix J Cell Biol 120 1993 5777-5585
    • (1993) J Cell Biol , vol.120
    • Juliano, R.L.1    Haskill, S.2
  • 6
    • 0027982876 scopus 로고
    • Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm
    • T.A. Springer Traffic signals for lymphocyte recirculation and leukocyte emigration: The multistep paradigm Cell 76 1994 301 314
    • (1994) Cell , vol.76 , pp. 301-314
    • Springer, T.A.1
  • 8
    • 0029907050 scopus 로고    scopus 로고
    • A polymeric form of fibronectin has anti-metastatic effects against multiple tumor types
    • R. Pasqualini S. Bourdoulous E. Koivunen V.L. Woods Jr E. Ruoslahti A polymeric form of fibronectin has anti-metastatic effects against multiple tumor types Nature Med 2 1996 1197 1203
    • (1996) Nature Med , vol.2 , pp. 1197-1203
    • Pasqualini, R.1    Bourdoulous, S.2    Koivunen, E.3    Woods, V.L.4    Ruoslahti, E.5
  • 9
    • 0025291522 scopus 로고
    • An interaction between α-actinin and the β1 subunit in vitro
    • C.A. Otey F.M. Pavalko K. Burridge An interaction between α -actinin and the β 1 subunit in vitro J Cell Biol 111 1990 721 729
    • (1990) J Cell Biol , vol.111 , pp. 721-729
    • Otey, C.A.1    Pavalko, F.M.2    Burridge, K.3
  • 10
    • 0028958438 scopus 로고
    • Direct interaction of filamin (ABP-280) with the β2-integrin subunit CD18
    • C.P. Sharma R.M. Essell M.A. Arnaout Direct interaction of filamin (ABP-280) with the β 2-integrin subunit CD18 J Immunol 154 1995 3461 3470
    • (1995) J Immunol , vol.154 , pp. 3461-3470
    • Sharma, C.P.1    Essell, R.M.2    Arnaout, M.A.3
  • 11
    • 0026445719 scopus 로고
    • Tyrosine phosphorylation of paxillin and pp125FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly
    • FAK accompanies cell adhesion to extracellular matrix: A role in cytoskeletal assembly J Cell Biol 119 1992 893 903
    • (1992) J Cell Biol , vol.119 , pp. 893-903
    • Burridge, K.1    Turner, C.E.2    Romer, L.H.3
  • 12
    • 0028981376 scopus 로고
    • Tyrosine phosphorylation of p130Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix
    • Cas and cortactin accompanies integrin-mediated cell adhesion to extracellular matrix J Biol Chem 270 1995 22259 22262
    • (1995) J Biol Chem , vol.270 , pp. 22259-22262
    • Vuori, K.1    Ruoslahti, E.2
  • 13
    • 0028036684 scopus 로고
    • The small GTP-binding protein Rho regulates phosphatidylinositol 4-phosphate 5-kinase in mammalian cells
    • L.D. Chong A. Traynor-Kaplan G.M. Bokoch M.A. Schwartz The small GTP-binding protein Rho regulates phosphatidylinositol 4-phosphate 5-kinase in mammalian cells Cell 79 1994 507 513
    • (1994) Cell , vol.79 , pp. 507-513
    • Chong, L.D.1    Traynor-Kaplan, A.2    Bokoch, G.M.3    Schwartz, M.A.4
  • 14
    • 0029943112 scopus 로고    scopus 로고
    • Regulation of vinculin binding to talin and actin by phosphatidylinositol-4–5-bisphosphate
    • A.P. Gilmore K. Burridge Regulation of vinculin binding to talin and actin by phosphatidylinositol-4–5-bisphosphate Nature 381 1996 531 535
    • (1996) Nature , vol.381 , pp. 531-535
    • Gilmore, A.P.1    Burridge, K.2
  • 16
    • 0028533592 scopus 로고
    • Tensin: A potential link between the cytoskeleton and signal transduction
    • S.H. Lo E. Weisberg L.B. Chen Tensin: A potential link between the cytoskeleton and signal transduction BioEssays 16 1994 817 823
    • (1994) BioEssays , vol.16 , pp. 817-823
    • Lo, S.H.1    Weisberg, E.2    Chen, L.B.3
  • 18
    • 0027451706 scopus 로고
    • The extracellular matrix as a cell survival factor
    • J.E. Meredith B. Fazeli M.A. Schwartz The extracellular matrix as a cell survival factor Mol Biol Cell 4 1993 953 961
    • (1993) Mol Biol Cell , vol.4 , pp. 953-961
    • Meredith, J.E.1    Fazeli, B.2    Schwartz, M.A.3
  • 19
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • S.M. Frisch H. Francis Disruption of epithelial cell-matrix interactions induces apoptosis J Cell Biol 124 1994 619 626
    • (1994) J Cell Biol , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 20
    • 0028335948 scopus 로고
    • Anchorage dependence, integrins and apoptosis
    • E. Ruoslahti J.C. Reed Anchorage dependence, integrins and apoptosis Cell 77 1994 477 478
    • (1994) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.C.2
  • 21
    • 0029739950 scopus 로고    scopus 로고
    • Control of adhesion-dependent cell survival by focal adhesion kinase
    • S.M. Frisch K. Vuori E. Ruoslahti P.-Y. Chan-Hui Control of adhesion-dependent cell survival by focal adhesion kinase J Cell Biol 134 1996 793 799
    • (1996) J Cell Biol , vol.134 , pp. 793-799
    • Frisch, S.M.1    Vuori, K.2    Ruoslahti, E.3    Chan-Hui, P.-Y.4
  • 22
    • 0029115343 scopus 로고
    • Signal transduction by the α6β4 integrin: Distinct b4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes
    • F. Mainiero A. Pepe K.K. Wary L. Spinardi M. Mohammadi J. Schlessinger F. Giancotti Signal transduction by the α 6 β 4 integrin: Distinct b4 subunit sites mediate recruitment of Shc/Grb2 and association with the cytoskeleton of hemidesmosomes EMBO J 14 1995 4470 4481
    • (1995) EMBO J , vol.14 , pp. 4470-4481
    • Mainiero, F.1    Pepe, A.2    Wary, K.K.3    Spinardi, L.4    Mohammadi, M.5    Schlessinger, J.6    Giancotti, F.7
  • 23
    • 0028982923 scopus 로고
    • Soluble ligands of the αvβ3 integrin mediate enhanced tyrosine phosphorylation of multiple proteins in adherent bovine pulmonary artery endothelial cells
    • S. Bhattacharya C. Fu J. Bhattacharya S. Greenberg Soluble ligands of the α v β 3 integrin mediate enhanced tyrosine phosphorylation of multiple proteins in adherent bovine pulmonary artery endothelial cells J Biol Chem 270 1995 16781 16787
    • (1995) J Biol Chem , vol.270 , pp. 16781-16787
    • Bhattacharya, S.1    Fu, C.2    Bhattacharya, J.3    Greenberg, S.4
  • 24
    • 0028641601 scopus 로고
    • Association of insulin receptor substrate-1 with integrins
    • K. Vuori E. Ruoslahti Association of insulin receptor substrate-1 with integrins Science 266 1994 1576 1578
    • (1994) Science , vol.266 , pp. 1576-1578
    • Vuori, K.1    Ruoslahti, E.2
  • 25
    • 0028085078 scopus 로고
    • The insulin signaling system
    • M.F. White C.R. Kahn The insulin signaling system J Biol Chem 269 1994 1 4
    • (1994) J Biol Chem , vol.269 , pp. 1-4
    • White, M.F.1    Kahn, C.R.2
  • 26
    • 0027203057 scopus 로고
    • The αvβ3 integrin associates with a 190-kDa protein that is phosphorylated on tyrosine in response to platelet-derived growth factor
    • N.S. Bartfeld E.B. Pasquale J.E. Geltosky L.L. Languino The α v β 3 integrin associates with a 190-kDa protein that is phosphorylated on tyrosine in response to platelet-derived growth factor J Biol Chem 268 1993 17270 17276
    • (1993) J Biol Chem , vol.268 , pp. 17270-17276
    • Bartfeld, N.S.1    Pasquale, E.B.2    Geltosky, J.E.3    Languino, L.L.4
  • 27
    • 0028670833 scopus 로고
    • Integrin αvβ3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels
    • P.C. Brooks A.M.P. Montgomery M. Rosenfeld R.A. Reisfeld T. Hu G. Klier D.A. Cheresh Integrin α v β 3 antagonists promote tumor regression by inducing apoptosis of angiogenic blood vessels Cell 79 1994 1157 1164
    • (1994) Cell , vol.79 , pp. 1157-1164
    • Brooks, P.C.1    Montgomery, A.M.P.2    Rosenfeld, M.3    Reisfeld, R.A.4    Hu, T.5    Klier, G.6    Cheresh, D.A.7
  • 28
    • 0028983407 scopus 로고
    • The α5β1 integrin supports survival of cells on fibronectin and upregulates Bcl-2 expression
    • Z. Zhang K. Vuori J.C. Reed E. Ruoslahti The α 5 β 1 integrin supports survival of cells on fibronectin and upregulates Bcl-2 expression Proc Natl Acad Sci USA 92 1995 6161 6165
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 6161-6165
    • Zhang, Z.1    Vuori, K.2    Reed, J.C.3    Ruoslahti, E.4
  • 29
    • 0028927484 scopus 로고
    • Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix
    • N. Boudreau C.J. Sympson Z. Werb M.J. Bissell Suppression of ICE and apoptosis in mammary epithelial cells by extracellular matrix Science 267 1995 891 893
    • (1995) Science , vol.267 , pp. 891-893
    • Boudreau, N.1    Sympson, C.J.2    Werb, Z.3    Bissell, M.J.4
  • 30
    • 0026938957 scopus 로고
    • Signal transduction by integrin receptors for extracellular matrix: Cooperative processing of extracellular information
    • C.H. Damsky Z. Werb Signal transduction by integrin receptors for extracellular matrix: Cooperative processing of extracellular information Cur Opin Cell Biol 4 1992 772 781
    • (1992) Cur Opin Cell Biol , vol.4 , pp. 772-781
    • Damsky, C.H.1    Werb, Z.2
  • 33
    • 0027497502 scopus 로고
    • Multiple functional forms of the integrin VLA-2 can be derived from a single α2 cDNA clone: Interconversion of forms induced by an anti-b1 antibody
    • B.M.C. Chan M.E. Hemler Multiple functional forms of the integrin VLA-2 can be derived from a single α 2 cDNA clone: Interconversion of forms induced by an anti-b1 antibody J Cell Biol 120 1993 537 543
    • (1993) J Cell Biol , vol.120 , pp. 537-543
    • Chan, B.M.C.1    Hemler, M.E.2
  • 34
    • 0027235439 scopus 로고
    • Regulation of vascular integrins
    • S.S. Smyth C.C. Joneckis L.V. Parise Regulation of vascular integrins Blood 81 1993 2827 2843
    • (1993) Blood , vol.81 , pp. 2827-2843
    • Smyth, S.S.1    Joneckis, C.C.2    Parise, L.V.3
  • 35
    • 0030602819 scopus 로고    scopus 로고
    • α1β2 Integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule
    • W. Kolanus W. Nagel B. Schiller L. Zeitlmann S. Godar H. Stockinger B. Seed α 1 β 2 Integrin/LFA-1 binding to ICAM-1 induced by cytohesin-1, a cytoplasmic regulatory molecule Cell 86 1996 233 242
    • (1996) Cell , vol.86 , pp. 233-242
    • Kolanus, W.1    Nagel, W.2    Schiller, B.3    Zeitlmann, L.4    Godar, S.5    Stockinger, H.6    Seed, B.7
  • 37
    • 85114525191 scopus 로고    scopus 로고
    • Wu C, Keivens VM, O'Toole TE, McDonald JA, Ginsberg MH: Integrin activation and cytoskeletal interaction are essential for the assembly of a flbronectin matrix. Cell 83:715–724
  • 38
    • 0025214421 scopus 로고
    • Elevated levels of the α5β1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells
    • F.G. Giancotti E. Ruoslahti Elevated levels of the α 5 β 1 fibronectin receptor suppress the transformed phenotype of Chinese hamster ovary cells Cell 60 1990 849 859
    • (1990) Cell , vol.60 , pp. 849-859
    • Giancotti, F.G.1    Ruoslahti, E.2
  • 39
    • 0028979701 scopus 로고
    • Integrin α5β1 expression negatively regulates cell growth: reversal by attachment to fibronectin
    • J.A. Varner D.A. Emerson R.L. Juliano Integrin α 5 β 1 expression negatively regulates cell growth: reversal by attachment to fibronectin Molec Biol cell 6 1995 725 740
    • (1995) Molec Biol cell , vol.6 , pp. 725-740
    • Varner, J.A.1    Emerson, D.A.2    Juliano, R.L.3
  • 40
    • 0025729036 scopus 로고
    • Increased tumorigenicity of fibronectin receptor deficient Chinese hamster ovary cell variants
    • C. Schreiner M. Fisher S. Hussein R.L. Juliano Increased tumorigenicity of fibronectin receptor deficient Chinese hamster ovary cell variants Cancer Res 51 1991 1738 1740
    • (1991) Cancer Res , vol.51 , pp. 1738-1740
    • Schreiner, C.1    Fisher, M.2    Hussein, S.3    Juliano, R.L.4
  • 41
    • 0028069348 scopus 로고
    • Superfibronectin, a functionally distinct form of fibronectin
    • A. Morla Z. Zhang E. Ruoslahti Superfibronectin, a functionally distinct form of fibronectin Nature 367 1994 193 196
    • (1994) Nature , vol.367 , pp. 193-196
    • Morla, A.1    Zhang, Z.2    Ruoslahti, E.3
  • 42
    • 0022508987 scopus 로고
    • A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells
    • M.J. Humphries K. Olden K. Yamada A synthetic peptide from fibronectin inhibits experimental metastasis of murine melanoma cells Science 233 1986 467 470
    • (1986) Science , vol.233 , pp. 467-470
    • Humphries, M.J.1    Olden, K.2    Yamada, K.3
  • 43
    • 0026793951 scopus 로고
    • RGD-directed attachment of isolated rat osteoclasts to osteopontin, bone sialoprotein and fibronectin
    • M.E. Flores M. Norgård D. Heinegård F. Reinholt G. Anderson RGD-directed attachment of isolated rat osteoclasts to osteopontin, bone sialoprotein and fibronectin Exp Cell Res 201 1992 526 530
    • (1992) Exp Cell Res , vol.201 , pp. 526-530
    • Flores, M.E.1    Norgård, M.2    Heinegård, D.3    Reinholt, F.4    Anderson, G.5
  • 44
    • 0028362876 scopus 로고
    • Requirement of vascular integrin αvβ3 for angiogenesis
    • P.C. Brooks R.A.F. Clark D.A. Cheresh Requirement of vascular integrin α v β 3 for angiogenesis Science 264 1994 569 571
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.F.2    Cheresh, D.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.