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Volumn 12, Issue 8, 2005, Pages 1021-1030

Integrins as a distinct subtype of dependence receptors

Author keywords

Apoptosis; Dependence receptor; Extracellular matrix; Integrin

Indexed keywords

ALPHA INTEGRIN; ARGINYLGLYCYLASPARTIC ACID; BETA INTEGRIN; CASPASE 8; CELL RECEPTOR; COLLAGEN; IMMUNOGLOBULIN; INTEGRIN; LAMININ; MITOGEN ACTIVATED PROTEIN KINASE 1; MITOGEN ACTIVATED PROTEIN KINASE 3; PROTEIN KINASE B; RAS PROTEIN; RECEPTOR SUBTYPE; SCLEROPROTEIN; STRESS ACTIVATED PROTEIN KINASE;

EID: 23044451988     PISSN: 13509047     EISSN: None     Source Type: Journal    
DOI: 10.1038/sj.cdd.4401658     Document Type: Review
Times cited : (81)

References (114)
  • 3
    • 4143085992 scopus 로고    scopus 로고
    • Single transmembrane spanning heterotrimeric g protein-coupled receptors and their signaling cascades
    • Patel TB (2004) Single transmembrane spanning heterotrimeric g protein-coupled receptors and their signaling cascades. Pharmacol. Rev. 56: 371-385
    • (2004) Pharmacol. Rev. , vol.56 , pp. 371-385
    • Patel, T.B.1
  • 4
    • 1442295841 scopus 로고    scopus 로고
    • Apoptosis and dependence receptors: A molecular basis for cellular addiction
    • Bredesen DE, Mehlen P and Rabizadeh S (2004) Apoptosis and dependence receptors: a molecular basis for cellular addiction. Physiol. Rev. 84: 411-430
    • (2004) Physiol. Rev. , vol.84 , pp. 411-430
    • Bredesen, D.E.1    Mehlen, P.2    Rabizadeh, S.3
  • 5
    • 0036348616 scopus 로고    scopus 로고
    • Insulin-like growth factor receptor-1 as an anticancer target: Blocking transformation and inducing apoptosis
    • Wang Y and Sun Y (2002) Insulin-like growth factor receptor-1 as an anticancer target: blocking transformation and inducing apoptosis. Curr. Cancer Drug Targets 2: 191-207
    • (2002) Curr. Cancer Drug Targets , vol.2 , pp. 191-207
    • Wang, Y.1    Sun, Y.2
  • 6
    • 12144261476 scopus 로고    scopus 로고
    • Oncogenic derivatives of platelet-derived growth factor receptors
    • Jones AV and Cross NC (2004) Oncogenic derivatives of platelet-derived growth factor receptors. Cell. Mol. Life Sci. 61: 2912-2923
    • (2004) Cell. Mol. Life Sci. , vol.61 , pp. 2912-2923
    • Jones, A.V.1    Cross, N.C.2
  • 7
    • 0033371772 scopus 로고    scopus 로고
    • Neurotrophin dependence mediated by p75NTR: Contrast between rescue by BDNF and NGF
    • Rabizadeh S, Ye X, Wang JJ and Bredesen DE (1999) Neurotrophin dependence mediated by p75NTR: contrast between rescue by BDNF and NGF. Cell. Death Differ. 6: 1222-1227
    • (1999) Cell. Death Differ. , vol.6 , pp. 1222-1227
    • Rabizadeh, S.1    Ye, X.2    Wang, J.J.3    Bredesen, D.E.4
  • 8
    • 0344013003 scopus 로고    scopus 로고
    • The dependence receptors DCC and UNC5H as a link between neuronal guidance and survival
    • Mehlen P and Mazelin L (2003) The dependence receptors DCC and UNC5H as a link between neuronal guidance and survival. Biol. Cell 95: 425-436
    • (2003) Biol. Cell , vol.95 , pp. 425-436
    • Mehlen, P.1    Mazelin, L.2
  • 9
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO (2002) Integrins: bidirectional, allosteric signaling machines. Cell. 110: 673-687
    • (2002) Cell. , vol.110 , pp. 673-687
    • Hynes, R.O.1
  • 10
    • 0030777243 scopus 로고    scopus 로고
    • Integrin signaling: Specificity and control of cell survival and cell cycle progression
    • Giancotti FG (1997) Integrin signaling: specificity and control of cell survival and cell cycle progression. Curr. Opin. Cell. Biol. 9: 691-700
    • (1997) Curr. Opin. Cell. Biol. , vol.9 , pp. 691-700
    • Giancotti, F.G.1
  • 11
    • 1442331993 scopus 로고    scopus 로고
    • Integrin activation
    • Calderwood DA (2004) Integrin activation. J. Cell Sci. 117 (Part 5): 657-666
    • (2004) J. Cell Sci. , vol.117 , Issue.PART 5 , pp. 657-666
    • Calderwood, D.A.1
  • 12
    • 0036796781 scopus 로고    scopus 로고
    • Get a ligand, get a life: Integrins, signaling and cell survival
    • Stupack DG and Cheresh DA (2002) Get a ligand, get a life: integrins, signaling and cell survival. J. Cell Sci. 115 (Part 19): 3729-3738
    • (2002) J. Cell Sci. , vol.115 , Issue.PART 19 , pp. 3729-3738
    • Stupack, D.G.1    Cheresh, D.A.2
  • 13
    • 0035964805 scopus 로고    scopus 로고
    • Integrins in vascular development
    • Rupp PA and Little CD (2001) Integrins in vascular development. Circ. Res. 89: 566-572
    • (2001) Circ. Res. , vol.89 , pp. 566-572
    • Rupp, P.A.1    Little, C.D.2
  • 14
    • 0026584712 scopus 로고
    • Perturbation of beta 1 integrin-mediated adhesions results in altered somite cell shape and behavior
    • Drake CJ, Davis LA, Hungerford JE and Little CD (1992) Perturbation of beta 1 integrin-mediated adhesions results in altered somite cell shape and behavior. Dev. Biol. 149: 327-338
    • (1992) Dev. Biol. , vol.149 , pp. 327-338
    • Drake, C.J.1    Davis, L.A.2    Hungerford, J.E.3    Little, C.D.4
  • 15
    • 0028362876 scopus 로고
    • Requirement of vascular integrin alpha v beta 3 for angiogenesis
    • Brooks PC, Clark RA and Cheresh DA (1994) Requirement of vascular integrin alpha v beta 3 for angiogenesis. Science 264: 569-571
    • (1994) Science , vol.264 , pp. 569-571
    • Brooks, P.C.1    Clark, R.A.2    Cheresh, D.A.3
  • 16
    • 0037065986 scopus 로고    scopus 로고
    • ECM remodeling regulates angiogenesis: Endothelial integrins look for new ligands
    • Stupack DG and Cheresh DA (2002) ECM remodeling regulates angiogenesis: endothelial integrins look for new ligands. Sci. STKE 2002: E7
    • (2002) Sci. STKE 2002
    • Stupack, D.G.1    Cheresh, D.A.2
  • 17
    • 0037899249 scopus 로고    scopus 로고
    • The myofibroblast in wound healing and fibrocontractive diseases
    • Gabbiani G (2003) The myofibroblast in wound healing and fibrocontractive diseases. J. Pathol. 200: 500-503
    • (2003) J. Pathol. , vol.200 , pp. 500-503
    • Gabbiani, G.1
  • 18
    • 0036683057 scopus 로고    scopus 로고
    • Role of integrins in regulating epidermal adhesion, growth and differentiation
    • Watt FM (2002) Role of integrins in regulating epidermal adhesion, growth and differentiation. EMBO J. 21: 3919-3926
    • (2002) EMBO J. , vol.21 , pp. 3919-3926
    • Watt, F.M.1
  • 19
    • 0033119507 scopus 로고    scopus 로고
    • Tissue structure, nuclear organization, and gene expression in normal and malignant breast
    • discussion 1763s-1764s
    • Bissell MJ, Weaver VM, Lelievre SA, Wang F, Petersen OW and Schmeichel KL (1999) Tissue structure, nuclear organization, and gene expression in normal and malignant breast. Cancer Res. 59 (7 Suppl): 1757s-1763s; discussion 1763s-1764s.
    • (1999) Cancer Res. , vol.59 , Issue.7 SUPPL.
    • Bissell, M.J.1    Weaver, V.M.2    Lelievre, S.A.3    Wang, F.4    Petersen, O.W.5    Schmeichel, K.L.6
  • 20
  • 21
    • 0033516696 scopus 로고    scopus 로고
    • Correlation of overexpression of the low-affinity p75 neurotrophin receptor with augmented invasion and heparanase production in human malignant melanoma cells
    • Walch ET, Albino AP and Marchetti D (1999) Correlation of overexpression of the low-affinity p75 neurotrophin receptor with augmented invasion and heparanase production in human malignant melanoma cells. Int. J. Cancer 82: 112-120
    • (1999) Int. J. Cancer , vol.82 , pp. 112-120
    • Walch, E.T.1    Albino, A.P.2    Marchetti, D.3
  • 22
    • 0030601360 scopus 로고    scopus 로고
    • Comparative role of phosphotyrosine kinase domains of c-ros and c-ret protooncogenes in metanephric development with respect to growth factors and matrix morphogens
    • Liu ZZ, Wada J, Kumar A, Carone FA, Takahashi M and Kanwar YS (1996) Comparative role of phosphotyrosine kinase domains of c-ros and c-ret protooncogenes in metanephric development with respect to growth factors and matrix morphogens. Dev. Biol. 178: 133-148
    • (1996) Dev. Biol. , vol.178 , pp. 133-148
    • Liu, Z.Z.1    Wada, J.2    Kumar, A.3    Carone, F.A.4    Takahashi, M.5    Kanwar, Y.S.6
  • 25
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch SM and Francis H (1994) Disruption of epithelial cell-matrix interactions induces apoptosis. J. Cell Biol. 124: 619-626
    • (1994) J. Cell Biol. , vol.124 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 27
    • 3142521875 scopus 로고    scopus 로고
    • Control of motile and invasive cell phenotypes by focal adhesion kinase
    • Schlaepfer DD, Mitra SK and Ilic D (2004) Control of motile and invasive cell phenotypes by focal adhesion kinase. Biochim. Biophys. Acta 1692: 77-102
    • (2004) Biochim. Biophys. Acta , vol.1692 , pp. 77-102
    • Schlaepfer, D.D.1    Mitra, S.K.2    Ilic, D.3
  • 28
    • 1542328956 scopus 로고    scopus 로고
    • A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors
    • Jan Y, Matter M, Pai JT, Chen YL, Pilch J, Komatsu M, Ong E, Fukuda M and Ruoslahti E (2004) A mitochondrial protein, Bit1, mediates apoptosis regulated by integrins and Groucho/TLE corepressors. Cell 116: 751-762
    • (2004) Cell , vol.116 , pp. 751-762
    • Jan, Y.1    Matter, M.2    Pai, J.T.3    Chen, Y.L.4    Pilch, J.5    Komatsu, M.6    Ong, E.7    Fukuda, M.8    Ruoslahti, E.9
  • 30
    • 0033208328 scopus 로고    scopus 로고
    • The tumor microenvironment as a determinant of drug response and resistance
    • Dalton WS (1999) The tumor microenvironment as a determinant of drug response and resistance. Drug Resist Update 2: 285-288
    • (1999) Drug Resist. Update , vol.2 , pp. 285-288
    • Dalton, W.S.1
  • 31
    • 1542467646 scopus 로고    scopus 로고
    • Integrin alpha2beta1 inhibits Fas-mediated apoptosis in T lymphocytes by protein phosphatase 2A-dependent activation of the MAPK/ERK pathway
    • Gendron S, Couture J and Aoudjit F (2003) Integrin alpha2beta1 inhibits Fas-mediated apoptosis in T lymphocytes by protein phosphatase 2A-dependent activation of the MAPK/ERK pathway. J. Biol. Chem. 278: 48633-48643
    • (2003) J. Biol. Chem. , vol.278 , pp. 48633-48643
    • Gendron, S.1    Couture, J.2    Aoudjit, F.3
  • 32
    • 0036499140 scopus 로고    scopus 로고
    • Adhesion-mediated intracellular redistribution of c-Fas-associated death domain-like IL-1-converting enzyme-like inhibitory protein-long confers resistance to CD95-induced apoptosis in hematopoietic cancer cell lines
    • Shain KH, Landowski TH and Dalton WS (2002) Adhesion-mediated intracellular redistribution of c-Fas-associated death domain-like IL-1-converting enzyme-like inhibitory protein-long confers resistance to CD95-induced apoptosis in hematopoietic cancer cell lines. J. Immunol. 168: 2544-2553
    • (2002) J. Immunol. , vol.168 , pp. 2544-2553
    • Shain, K.H.1    Landowski, T.H.2    Dalton, W.S.3
  • 33
    • 0346118914 scopus 로고    scopus 로고
    • Fibronectin protects prostate cancer cells from tumor necrosis factor-alpha-induced apoptosis via the AKT/survivin pathway
    • Fornaro M, Plescia J, Chheang S, Tallini G, Zhu YM, King M, Altieri DC and Languino LR (2003) Fibronectin protects prostate cancer cells from tumor necrosis factor-alpha-induced apoptosis via the AKT/survivin pathway. J. Biol. Chem. 278: 50402-50411
    • (2003) J. Biol. Chem. , vol.278 , pp. 50402-50411
    • Fornaro, M.1    Plescia, J.2    Chheang, S.3    Tallini, G.4    Zhu, Y.M.5    King, M.6    Altieri, D.C.7    Languino, L.R.8
  • 34
    • 0028983407 scopus 로고
    • The alpha 5 beta 1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression
    • Zhang Z, Vuori K, Reed JC and Ruoslahti E (1995) The alpha 5 beta 1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression. Proc. Natl. Acad. Sci. USA 92: 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
  • 35
    • 0030038229 scopus 로고    scopus 로고
    • Suppression of p53 activity and p21WAF1/CIP1 expression by vascular cell integrin alphaVbeta3 during angiogenesis
    • Stromblad S, Becker JC, Yebra M, Brooks PC and Cheresh DA (1996) Suppression of p53 activity and p21WAF1/CIP1 expression by vascular cell integrin alphaVbeta3 during angiogenesis. J. Clin. Invest. 98: 426-433
    • (1996) J. Clin. Invest. , vol.98 , pp. 426-433
    • Stromblad, S.1    Becker, J.C.2    Yebra, M.3    Brooks, P.C.4    Cheresh, D.A.5
  • 36
    • 0022448122 scopus 로고
    • Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin
    • Tamkun JW, DeSimone DW, Fonda D, Patel RS, Buck C, Horwitz AF and Hynes RO (1986) Structure of integrin, a glycoprotein involved in the transmembrane linkage between fibronectin and actin. Cell 46: 271-282
    • (1986) Cell , vol.46 , pp. 271-282
    • Tamkun, J.W.1    DeSimone, D.W.2    Fonda, D.3    Patel, R.S.4    Buck, C.5    Horwitz, A.F.6    Hynes, R.O.7
  • 37
    • 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 and Juliano RL (1992) Cell adhesion or integrin clustering increases phosphorylation of a focal adhesion-associated tyrosine kinase. J. Biol. Chem. 267: 23439-23442
    • (1992) J. Biol. Chem. , vol.267 , pp. 23439-23442
    • Kornberg, L.1    Earp, H.S.2    Parsons, J.T.3    Schaller, M.4    Juliano, R.L.5
  • 38
  • 39
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer DD, Hanks SK, Hunter T and van der Geer P (1994) Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 372: 786-791
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    van der Geer, P.4
  • 40
    • 0035897407 scopus 로고    scopus 로고
    • Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1
    • Aplin AE, Stewart SA, Assoian RK and Juliano RL (2001) Integrin-mediated adhesion regulates ERK nuclear translocation and phosphorylation of Elk-1. J. Cell Biol. 153: 273-282
    • (2001) J. Cell Biol. , vol.153 , pp. 273-282
    • Aplin, A.E.1    Stewart, S.A.2    Assoian, R.K.3    Juliano, R.L.4
  • 41
    • 0034652812 scopus 로고    scopus 로고
    • Engagement of the alpha2beta1 integrin inhibits Fas ligand expression and activation-induced cell death in T cells in a focal adhesion kinase-dependent manner
    • Aoudjit F and Vuori K (2000) Engagement of the alpha2beta1 integrin inhibits Fas ligand expression and activation-induced cell death in T cells in a focal adhesion kinase-dependent manner. Blood 95: 2044-2051
    • (2000) Blood , vol.95 , pp. 2044-2051
    • Aoudjit, F.1    Vuori, K.2
  • 42
    • 0035809182 scopus 로고    scopus 로고
    • Matrix attachment regulates Fas-induced apoptosis in endothelial cells: A role for c-flip and implications for anoikis
    • Aoudjit F and Vuori K (2001) Matrix attachment regulates Fas-induced apoptosis in endothelial cells: a role for c-flip and implications for anoikis. J. Cell Biol. 152: 633-643
    • (2001) J. Cell Biol. , vol.152 , pp. 633-643
    • Aoudjit, F.1    Vuori, K.2
  • 43
    • 0035958902 scopus 로고    scopus 로고
    • A signaling pathway from the alpha5beta1 and alpha(v)beta3 integrins that elevates bcl-2 transcription
    • Matter ML and Ruoslahti E (2001) A signaling pathway from the alpha5beta1 and alpha(v)beta3 integrins that elevates bcl-2 transcription. J. Biol. Chem. 276: 27757-27763
    • (2001) J. Biol. Chem. , vol.276 , pp. 27757-27763
    • Matter, M.L.1    Ruoslahti, E.2
  • 44
    • 0033747398 scopus 로고    scopus 로고
    • Osteopontin deficiency in rat vascular smooth muscle cells is associated with an inability to adhere to collagen and increased apoptosis
    • Weintraub AS, Schnapp LM, Lin X and Taubman MB (2000) Osteopontin deficiency in rat vascular smooth muscle cells is associated with an inability to adhere to collagen and increased apoptosis. Lab. Invest. 80: 1603-1615
    • (2000) Lab. Invest. , vol.80 , pp. 1603-1615
    • Weintraub, A.S.1    Schnapp, L.M.2    Lin, X.3    Taubman, M.B.4
  • 45
    • 0034647341 scopus 로고    scopus 로고
    • Osteoprotegerin is an alpha vbeta 3-induced, NF-kappa B-dependent survival factor for endothelial cells
    • Malyankar UM, Scatena M, Suchland KL, Yun TJ, Clark EA and Giachelli CM (2000) Osteoprotegerin is an alpha vbeta 3-induced, NF-kappa B-dependent survival factor for endothelial cells. J. Biol. Chem. 275: 20959-20962
    • (2000) J. Biol. Chem. , vol.275 , pp. 20959-20962
    • Malyankar, U.M.1    Scatena, M.2    Suchland, K.L.3    Yun, T.J.4    Clark, E.A.5    Giachelli, C.M.6
  • 46
    • 0031042493 scopus 로고    scopus 로고
    • Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton
    • Tapon N and Hall A (1997) Rho, Rac and Cdc42 GTPases regulate the organization of the actin cytoskeleton. Curr. Opin. Cell Biol. 9: 86-92
    • (1997) Curr. Opin. Cell Biol. , vol.9 , pp. 86-92
    • Tapon, N.1    Hall, A.2
  • 47
    • 0038305915 scopus 로고    scopus 로고
    • ERK and RhoA differentially regulate pseudopodia growth and retraction during chemotaxis
    • Brahmbhatt AA and Klemke RL (2003) ERK and RhoA differentially regulate pseudopodia growth and retraction during chemotaxis. J. Biol. Chem. 278: 13016-13025
    • (2003) J. Biol. Chem. , vol.278 , pp. 13016-13025
    • Brahmbhatt, A.A.1    Klemke, R.L.2
  • 48
    • 0037128213 scopus 로고    scopus 로고
    • Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold
    • Cho SY and Klemke RL (2002) Purification of pseudopodia from polarized cells reveals redistribution and activation of Rac through assembly of a CAS/Crk scaffold. J. Cell Biol. 156: 725-736
    • (2002) J. Cell Biol. , vol.156 , pp. 725-736
    • Cho, S.Y.1    Klemke, R.L.2
  • 49
    • 0032531732 scopus 로고    scopus 로고
    • Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK-cell migration
    • Sieg DJ, Ilic D, Jones KC, Damsky CH, Hunter T and Schlaepfer DD (1998) Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK-cell migration. EMBO J. 17: 5933-5947
    • (1998) EMBO J. , vol.17 , pp. 5933-5947
    • Sieg, D.J.1    Ilic, D.2    Jones, K.C.3    Damsky, C.H.4    Hunter, T.5    Schlaepfer, D.D.6
  • 50
    • 0030464110 scopus 로고    scopus 로고
    • Signal transduction from the extracellular matrix -A role for the focal adhesion protein-tyrosine kinase FAK
    • Schlaepfer DD and Hunter T (1996) Signal transduction from the extracellular matrix -a role for the focal adhesion protein-tyrosine kinase FAK. Cell. Struct. Funct. 21: 445-450
    • (1996) Cell. Struct. Funct. , vol.21 , pp. 445-450
    • Schlaepfer, D.D.1    Hunter, T.2
  • 51
    • 0034599542 scopus 로고    scopus 로고
    • Extracellular-regulated kinase activation and CAS/Crk coupling regulate cell migration and suppress apoptosis during invasion of the extracellular matrix
    • Cho SY and Klemke RL (2000) Extracellular-regulated kinase activation and CAS/Crk coupling regulate cell migration and suppress apoptosis during invasion of the extracellular matrix. J. Cell Biol. 149: 223-236
    • (2000) J. Cell Biol. , vol.149 , pp. 223-236
    • Cho, S.Y.1    Klemke, R.L.2
  • 53
    • 0034704174 scopus 로고    scopus 로고
    • Platelet-derived growth factor receptor beta and vascular endothelial growth factor receptor 2 bind to the beta 3 integrin through its extracellular domain
    • Borges E, Jan Y and Ruoslahti E (2000) Platelet-derived growth factor receptor beta and vascular endothelial growth factor receptor 2 bind to the beta 3 integrin through its extracellular domain. J. Biol. Chem. 275: 39867-39873
    • (2000) J. Biol. Chem. , vol.275 , pp. 39867-39873
    • Borges, E.1    Jan, Y.2    Ruoslahti, E.3
  • 54
    • 0030814976 scopus 로고    scopus 로고
    • Alphavbeta3 integrin associates with activated insulin and PDGFbeta receptors and potentiates the biological activity of PDGF
    • Schneller M, Vuori K and Ruoslahti E (1997) Alphavbeta3 integrin associates with activated insulin and PDGFbeta receptors and potentiates the biological activity of PDGF. EMBO J. 16: 5600-5607
    • (1997) EMBO J. , vol.16 , pp. 5600-5607
    • Schneller, M.1    Vuori, K.2    Ruoslahti, E.3
  • 55
    • 9444223282 scopus 로고    scopus 로고
    • Stimulation of endothelial cell proliferation by FGF-2 in the presence of fibrinogen requires alphavbeta3
    • Sahni A and Francis CW (2004) Stimulation of endothelial cell proliferation by FGF-2 in the presence of fibrinogen requires alphavbeta3. Blood 104: 3635-3641
    • (2004) Blood , vol.104 , pp. 3635-3641
    • Sahni, A.1    Francis, C.W.2
  • 56
    • 0033943076 scopus 로고    scopus 로고
    • Role of alpha v integrins during angiogenesis
    • Eliceiri BP and Cheresh DA (2000) Role of alpha v integrins during angiogenesis. Cancer J. 6 (Suppl. 3): S245-S249
    • (2000) Cancer J. , vol.6 , Issue.SUPPL. 3
    • Eliceiri, B.P.1    Cheresh, D.A.2
  • 57
    • 0036142782 scopus 로고    scopus 로고
    • The alpha(1)beta(1) and alpha(2)beta(1) integrins provide critical support for vascular endothelial growth factor signaling, endothelial cell migration, and tumor angiogenesis
    • Senger DR, Perruzzi CA, Streit M, Koteliansky VE, de Fougerolles AR and Detmar M (2002) The alpha(1)beta(1) and alpha(2)beta(1) integrins provide critical support for vascular endothelial growth factor signaling, endothelial cell migration, and tumor angiogenesis. Am. J. Pathol. 160: 195-204
    • (2002) Am. J. Pathol. , vol.160 , pp. 195-204
    • Senger, D.R.1    Perruzzi, C.A.2    Streit, M.3    Koteliansky, V.E.4    de Fougerolles, A.R.5    Detmar, M.6
  • 61
    • 14844317695 scopus 로고    scopus 로고
    • Unoccupied alpha v beta 3 integrin regulates osteoclast apoptosis by transmitting a positive death signal
    • Zhao H, Ross FP and Teitelbaum SL (2005) Unoccupied alpha v beta 3 integrin regulates osteoclast apoptosis by transmitting a positive death signal. Mol. Endocrinol. 19: 771-780
    • (2005) Mol. Endocrinol. , vol.19 , pp. 771-780
    • Zhao, H.1    Ross, F.P.2    Teitelbaum, S.L.3
  • 62
    • 0036792466 scopus 로고    scopus 로고
    • Inhibition of endothelial cell survival and angiogenesis by protein kinase A
    • Kim S, Bakre M, Yin H and Varner JA (2002) Inhibition of endothelial cell survival and angiogenesis by protein kinase A. J. Clin. Invest. 110: 933-941
    • (2002) J. Clin. Invest. , vol.110 , pp. 933-941
    • Kim, S.1    Bakre, M.2    Yin, H.3    Varner, J.A.4
  • 63
  • 64
    • 0032537124 scopus 로고    scopus 로고
    • Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions
    • Chicurel ME, Singer RH, Meyer CJ and Ingber DE (1998) Integrin binding and mechanical tension induce movement of mRNA and ribosomes to focal adhesions. Nature 392: 730-733
    • (1998) Nature , vol.392 , pp. 730-733
    • Chicurel, M.E.1    Singer, R.H.2    Meyer, C.J.3    Ingber, D.E.4
  • 68
    • 0036792466 scopus 로고    scopus 로고
    • Inhibition of endothelial cell survival and angiogenesis by protein kinase A
    • Kim S, Bakre M, Yin H and Varner JA (2002) Inhibition of endothelial cell survival and angiogenesis by protein kinase A. J. Clin. Invest. 110: 933-941
    • (2002) J. Clin. Invest. , vol.110 , pp. 933-941
    • Kim, S.1    Bakre, M.2    Yin, H.3    Varner, J.A.4
  • 70
    • 0031020284 scopus 로고    scopus 로고
    • Cell surface amyloid beta-protein precursor colocalizes with beta 1 integrins at substrate contact sites in neural cells
    • Yamazaki T, Koo EH and Selkoe DJ (1997) Cell surface amyloid beta-protein precursor colocalizes with beta 1 integrins at substrate contact sites in neural cells. J. Neurosci. 17: 1004-1010
    • (1997) J. Neurosci. , vol.17 , pp. 1004-1010
    • Yamazaki, T.1    Koo, E.H.2    Selkoe, D.J.3
  • 73
    • 0029759727 scopus 로고    scopus 로고
    • Protein kinase C regulates alpha v beta 5-dependent cytoskeletal associations and focal adhesion kinase phosphorylation
    • Lewis JM, Cheresh DA and Schwartz MA (1996) Protein kinase C regulates alpha v beta 5-dependent cytoskeletal associations and focal adhesion kinase phosphorylation. J. Cell Biol. 134: 1323-1332
    • (1996) J. Cell Biol. , vol.134 , pp. 1323-1332
    • Lewis, J.M.1    Cheresh, D.A.2    Schwartz, M.A.3
  • 74
    • 0033575287 scopus 로고    scopus 로고
    • PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway
    • Tamura M, Gu J, Danen EH, Takino T, Miyamoto S and Yamada KM (1999) PTEN interactions with focal adhesion kinase and suppression of the extracellular matrix-dependent phosphatidylinositol 3-kinase/Akt cell survival pathway. J. Biol. Chem. 274: 20693-20703
    • (1999) J. Biol. Chem. , vol.274 , pp. 20693-20703
    • Tamura, M.1    Gu, J.2    Danen, E.H.3    Takino, T.4    Miyamoto, S.5    Yamada, K.M.6
  • 76
    • 0032479435 scopus 로고    scopus 로고
    • Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide
    • Gervais FG, Thornberry NA, Ruffolo SC, Nicholson DW and Roy S (1998) Caspases cleave focal adhesion kinase during apoptosis to generate a FRNK-like polypeptide. J. Biol. Chem. 273: 17102-17108
    • (1998) J. Biol. Chem. , vol.273 , pp. 17102-17108
    • Gervais, F.G.1    Thornberry, N.A.2    Ruffolo, S.C.3    Nicholson, D.W.4    Roy, S.5
  • 79
  • 80
    • 0037177799 scopus 로고    scopus 로고
    • Linkage of caspase-mediated degradation of paxillin to apoptosis in Ba/F3 murine pro-B lymphocytes
    • Chay KO, Park SS and Mushinski JF (2002) Linkage of caspase-mediated degradation of paxillin to apoptosis in Ba/F3 murine pro-B lymphocytes. J. Biol. Chem. 277: 14521-14529
    • (2002) J. Biol. Chem. , vol.277 , pp. 14521-14529
    • Chay, K.O.1    Park, S.S.2    Mushinski, J.F.3
  • 81
    • 0035919756 scopus 로고    scopus 로고
    • Disruption of focal adhesions mediates detachment during neuronal apoptosis
    • Lesay A, Hickman JA and Gibson RM (2001) Disruption of focal adhesions mediates detachment during neuronal apoptosis. NeuroReport 12: 2111-2115
    • (2001) NeuroReport , vol.12 , pp. 2111-2115
    • Lesay, A.1    Hickman, J.A.2    Gibson, R.M.3
  • 83
    • 4444352570 scopus 로고    scopus 로고
    • Structures of integrin domains and concerted conformational changes in the bidirectional signaling mechanism of alphaIIbbeta3
    • Calvete JJ (2004) Structures of integrin domains and concerted conformational changes in the bidirectional signaling mechanism of alphaIIbbeta3. Exp. Biol. Med. (Maywood) 229: 732-744
    • (2004) Exp. Biol. Med. (Maywood) , vol.229 , pp. 732-744
    • Calvete, J.J.1
  • 85
    • 14744273494 scopus 로고    scopus 로고
    • The three-dimensional structure of integrins and their ligands, and conformational regulation of cell adhesion
    • Springer TA and Wang JH (2004) The three-dimensional structure of integrins and their ligands, and conformational regulation of cell adhesion. Adv. Protein Chem. 68: 29-63
    • (2004) Adv. Protein Chem. , vol.68 , pp. 29-63
    • Springer, T.A.1    Wang, J.H.2
  • 86
    • 0037031551 scopus 로고    scopus 로고
    • A structural mechanism of integrin alpha(IIb)beta(3) 'inside-out' activation as regulated by its cytoplasmic face
    • Vinogradova O, Velyvis A, Velyviene A, Hu B, Haas T, Plow E and Qin J (2002) A structural mechanism of integrin alpha(IIb)beta(3) 'inside-out' activation as regulated by its cytoplasmic face. Cell 110: 587-597
    • (2002) Cell , vol.110 , pp. 587-597
    • Vinogradova, O.1    Velyvis, A.2    Velyviene, A.3    Hu, B.4    Haas, T.5    Plow, E.6    Qin, J.7
  • 87
    • 0036538656 scopus 로고    scopus 로고
    • Co-regulation of cell adhesion by nanoscale RGD organization and mechanical stimulus
    • Koo LY, Irvine DJ, Mayes AM, Lauffenburger DA and Griffith LG (2002) Co-regulation of cell adhesion by nanoscale RGD organization and mechanical stimulus. J. Cell Sci. 115 (Part 7): 1423-1433
    • (2002) J. Cell Sci. , vol.115 , Issue.PART 7 , pp. 1423-1433
    • Koo, L.Y.1    Irvine, D.J.2    Mayes, A.M.3    Lauffenburger, D.A.4    Griffith, L.G.5
  • 89
    • 0030994017 scopus 로고    scopus 로고
    • Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages
    • Choquet D, Felsenfeld DP and Sheetz MP (1997) Extracellular matrix rigidity causes strengthening of integrin-cytoskeleton linkages. Cell 88: 39-48
    • (1997) Cell , vol.88 , pp. 39-48
    • Choquet, D.1    Felsenfeld, D.P.2    Sheetz, M.P.3
  • 90
    • 0041461882 scopus 로고    scopus 로고
    • Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin
    • Jiang G, Giannone G, Critchley DR, Fukumoto E and Sheetz MP (2003) Two-piconewton slip bond between fibronectin and the cytoskeleton depends on talin. Nature 424: 334-337
    • (2003) Nature , vol.424 , pp. 334-337
    • Jiang, G.1    Giannone, G.2    Critchley, D.R.3    Fukumoto, E.4    Sheetz, M.P.5
  • 91
    • 0037175402 scopus 로고    scopus 로고
    • The relationship between force and focal complex development
    • Galbraith CG, Yamada KM and Sheetz MP (2002) The relationship between force and focal complex development. J. Cell Biol. 159: 695-705
    • (2002) J. Cell Biol. , vol.159 , pp. 695-705
    • Galbraith, C.G.1    Yamada, K.M.2    Sheetz, M.P.3
  • 92
    • 0031426154 scopus 로고    scopus 로고
    • In vitro angiogenesis is modulated by the mechanical properties of fibrin gels and is related to alpha(v)beta3 integrin localization
    • Vailhe B, Ronot X, Tracqui P, Usson Y and Tranqui L (1997) In vitro angiogenesis is modulated by the mechanical properties of fibrin gels and is related to alpha(v)beta3 integrin localization. In Vitro Cell. Dev. Biol. Anim. 33: 763-773
    • (1997) In Vitro Cell. Dev. Biol. Anim. , vol.33 , pp. 763-773
    • Vailhe, B.1    Ronot, X.2    Tracqui, P.3    Usson, Y.4    Tranqui, L.5
  • 94
    • 0034708456 scopus 로고    scopus 로고
    • The Ras/phosphatidylinositol 3-kinase and Ras/ERK pathways function as independent survival modules each of which inhibits a distinct apoptotic signaling pathway in sympathetic neurons
    • Xue L, Murray JH and Tolkovsky AM (2000) The Ras/phosphatidylinositol 3-kinase and Ras/ERK pathways function as independent survival modules each of which inhibits a distinct apoptotic signaling pathway in sympathetic neurons. J. Biol. Chem. 275: 8817-8824
    • (2000) J. Biol. Chem. , vol.275 , pp. 8817-8824
    • Xue, L.1    Murray, J.H.2    Tolkovsky, A.M.3
  • 95
    • 0036467578 scopus 로고    scopus 로고
    • Anchorage-dependent ERK signaling - Mechanisms and consequences
    • Howe AK, Aplin AE and Juliano RL (2002) Anchorage-dependent ERK signaling - mechanisms and consequences. Curr. Opin. Genet. Dev. 12: 30-35
    • (2002) Curr. Opin. Genet. Dev. , vol.12 , pp. 30-35
    • Howe, A.K.1    Aplin, A.E.2    Juliano, R.L.3
  • 98
    • 0035815649 scopus 로고    scopus 로고
    • Elevated AKT activity protects the prostate cancer cell line LNCaP from TRAIL-induced apoptosis
    • Nesterov A, Lu X, Johnson M, Miller GJ, Ivashchenko Y and Kraft AS (2001) Elevated AKT activity protects the prostate cancer cell line LNCaP from TRAIL-induced apoptosis. J. Biol. Chem. 276: 10767-10774
    • (2001) J. Biol. Chem. , vol.276 , pp. 10767-10774
    • Nesterov, A.1    Lu, X.2    Johnson, M.3    Miller, G.J.4    Ivashchenko, Y.5    Kraft, A.S.6
  • 99
    • 0036064773 scopus 로고    scopus 로고
    • Regulation of Akt by EGF-R inhibitors, a possible mechanism of EGF-R inhibitor-enhanced TRAIL-induced apoptosis
    • Park SY and Seol DW (2002) Regulation of Akt by EGF-R inhibitors, a possible mechanism of EGF-R inhibitor-enhanced TRAIL-induced apoptosis. Biochem. Biophys. Res. Commun. 295: 515-518
    • (2002) Biochem. Biophys. Res. Commun. , vol.295 , pp. 515-518
    • Park, S.Y.1    Seol, D.W.2
  • 101
    • 0036146543 scopus 로고    scopus 로고
    • Focal adhesions require catalytic activity of Src family kinases to mediate integrin-matrix adhesion
    • Li L, Okura M and Imamoto A (2002) Focal adhesions require catalytic activity of Src family kinases to mediate integrin-matrix adhesion. Mol. Cell. Biol. 22: 1203-1217
    • (2002) Mol. Cell. Biol. , vol.22 , pp. 1203-1217
    • Li, L.1    Okura, M.2    Imamoto, A.3
  • 102
    • 2142645056 scopus 로고    scopus 로고
    • Protein kinase B inhibits apoptosis induced by actinomycin D in ECV304 cells through phosphorylation of caspase 8
    • Shim D, Kang HY, Jeon BW, Kang SS, Chang SI and Kim HY (2004) Protein kinase B inhibits apoptosis induced by actinomycin D in ECV304 cells through phosphorylation of caspase 8. Arch. Biochem. Biophys. 425: 214-220
    • (2004) Arch. Biochem. Biophys. , vol.425 , pp. 214-220
    • Shim, D.1    Kang, H.Y.2    Jeon, B.W.3    Kang, S.S.4    Chang, S.I.5    Kim, H.Y.6
  • 104
    • 1342342989 scopus 로고    scopus 로고
    • Human cancer, PTEN and the PI-3 kinase pathway
    • Parsons R (2004) Human cancer, PTEN and the PI-3 kinase pathway. Semin. Cell Dev. Biol. 15: 171-176
    • (2004) Semin. Cell Dev. Biol. , vol.15 , pp. 171-176
    • Parsons, R.1
  • 105
    • 0034601436 scopus 로고    scopus 로고
    • The integrin-linked kinase (ILK) suppresses anoikis
    • Attwell S, Roskelley C and Dedhar S (2000) The integrin-linked kinase (ILK) suppresses anoikis. Oncogene 19: 3811-3815
    • (2000) Oncogene , vol.19 , pp. 3811-3815
    • Attwell, S.1    Roskelley, C.2    Dedhar, S.3
  • 106
    • 0036943329 scopus 로고    scopus 로고
    • Blockade of signaling via the very late antigen (VLA-4) and its counterligand vascular cell adhesion molecule-1 (VCAM-1) causes increased T cell apoptosis in experimental autoimmune neuritis
    • Leussink VI, Zettl UK, Jander S, Pepinsky RB, Lobb RR, Stoll G, Toyka KV and Gold R (2002) Blockade of signaling via the very late antigen (VLA-4) and its counterligand vascular cell adhesion molecule-1 (VCAM-1) causes increased T cell apoptosis in experimental autoimmune neuritis. Acta Neuropathol. (Berl) 103: 131-136
    • (2002) Acta Neuropathol. (Berl.) , vol.103 , pp. 131-136
    • Leussink, V.I.1    Zettl, U.K.2    Jander, S.3    Pepinsky, R.B.4    Lobb, R.R.5    Stoll, G.6    Toyka, K.V.7    Gold, R.8
  • 107
    • 16644395075 scopus 로고    scopus 로고
    • The CD11/CD18 (beta2) integrins modulate neutrophil caspase activation and survival following TNF-alpha or endotoxin induced transendothelial migration
    • Yan SR, Sapru K and Issekutz AC (2004) The CD11/CD18 (beta2) integrins modulate neutrophil caspase activation and survival following TNF-alpha or endotoxin induced transendothelial migration. Immunol. Cell Biol. 82: 435-446
    • (2004) Immunol. Cell Biol. , vol.82 , pp. 435-446
    • Yan, S.R.1    Sapru, K.2    Issekutz, A.C.3
  • 108
    • 1642553456 scopus 로고    scopus 로고
    • Apoptotic cues from the extracellular matrix: Regulators of angiogenesis
    • Stupack DG and Cheresh DA (2003) Apoptotic cues from the extracellular matrix: regulators of angiogenesis. Oncogene 22: 9022-9029
    • (2003) Oncogene , vol.22 , pp. 9022-9029
    • Stupack, D.G.1    Cheresh, D.A.2
  • 109
    • 1042292614 scopus 로고    scopus 로고
    • Regulation of mammary gland branching morphogenesis by the extracellular matrix and its remodeling enzymes
    • Fate JE, Werb Z and Bissell MJ (2004) Regulation of mammary gland branching morphogenesis by the extracellular matrix and its remodeling enzymes. Breast Cancer Res. 6: 1-11
    • (2004) Breast Cancer Res. , vol.6 , pp. 1-11
    • Fate, J.E.1    Werb, Z.2    Bissell, M.J.3
  • 110
    • 0242456170 scopus 로고    scopus 로고
    • Axis of evil: Molecular mechanisms of cancer metastasis
    • Bogenrieder T and Herlyn M (2003) Axis of evil: molecular mechanisms of cancer metastasis. Oncogene 22: 6524-6536
    • (2003) Oncogene , vol.22 , pp. 6524-6536
    • Bogenrieder, T.1    Herlyn, M.2
  • 111
    • 0026334978 scopus 로고
    • Glioblastoma expression of vitronectin and the alpha v beta 3 integrin. Adhesion mechanism for transformed glial cells
    • Gladson CL and Cheresh DA (1991) Glioblastoma expression of vitronectin and the alpha v beta 3 integrin. Adhesion mechanism for transformed glial cells. J. Clin. Invest. 88: 1924-1932
    • (1991) J. Clin. Invest. , vol.88 , pp. 1924-1932
    • Gladson, C.L.1    Cheresh, D.A.2
  • 112
    • 0036329807 scopus 로고    scopus 로고
    • New insights into the role of extracellular matrix during tumor onset and progression
    • Pupa SM, Menard S, Forti S and Tagliabue E (2002) New insights into the role of extracellular matrix during tumor onset and progression. J. Cell Physiol. 192: 259-267
    • (2002) J. Cell Physiol. , vol.192 , pp. 259-267
    • Pupa, S.M.1    Menard, S.2    Forti, S.3    Tagliabue, E.4


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