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Volumn 18, Issue 5, 2011, Pages 806-816

Galectin-1 sensitizes carcinoma cells to anoikis via the fibronectin receptor α5 Β1-integrin

Author keywords

anoikis; caspase 8; fibronectin receptor; galectin; integrin; sialylation

Indexed keywords

ALPHA5 INTEGRIN; BETA1 INTEGRIN; CASPASE 8 INHIBITOR; CHOLESTEROL; FIBRONECTIN RECEPTOR; FILIPIN; GALECTIN 1; GLYCAN; PROTEIN SUBUNIT; VERY LATE ACTIVATION ANTIGEN 5;

EID: 79954422467     PISSN: 13509047     EISSN: 14765403     Source Type: Journal    
DOI: 10.1038/cdd.2010.148     Document Type: Article
Times cited : (71)

References (40)
  • 1
    • 27644484968 scopus 로고    scopus 로고
    • Clinging to life: Cell to matrix adhesion and cell survival
    • DOI 10.1007/s10555-005-5134-3
    • Reddig PJ, Juliano RL. Clinging to life: cell to matrix adhesion and cell survival. Cancer Metastasis Rev 2005; 24: 425-439. (Pubitemid 41569982)
    • (2005) Cancer and Metastasis Reviews , vol.24 , Issue.3 , pp. 425-439
    • Reddig, P.J.1    Juliano, R.L.2
  • 2
    • 0028057613 scopus 로고
    • Disruption of epithelial cell-matrix interactions induces apoptosis
    • Frisch SM, Francis H. Disruption of epithelial cell-matrix interactions induces apoptosis. J Cell Biol 1994; 124: 619-626. (Pubitemid 24064472)
    • (1994) Journal of Cell Biology , vol.124 , Issue.4 , pp. 619-626
    • Frisch, S.M.1    Francis, H.2
  • 3
    • 0036222549 scopus 로고    scopus 로고
    • Sensing the environment: A historical perspective on integrin signal transduction
    • DOI 10.1038/ncb0402-e83
    • Miranti CK, Brugge JS. Sensing the environment: a historical perspective on integrin signal transduction. Nat Cell Biol 2002; 4: E83-E90. (Pubitemid 34308848)
    • (2002) Nature Cell Biology , vol.4 , Issue.4
    • Miranti, C.K.1    Brugge, J.S.2
  • 4
    • 0033598145 scopus 로고    scopus 로고
    • Involvement of FADD and caspase-8 signalling in detachment-induced apoptosis
    • DOI 10.1016/S0960-9822(99)80454-0
    • Rytomaa M, Martins LM, Downward J. Involvement of FADD and caspase-8 signalling in detachment-induced apoptosis. Curr Biol 1999; 9: 1043-1046. (Pubitemid 29456174)
    • (1999) Current Biology , vol.9 , Issue.18 , pp. 1043-1046
    • Rytomaa, M.1    Martins, L.M.2    Downward, J.3
  • 5
    • 0033598202 scopus 로고    scopus 로고
    • Evidence for a function of death-receptor-related, death-domain- containing proteins in anoikis
    • DOI 10.1016/S0960-9822(99)80455-2
    • Frisch SM. Evidence for a function of death-receptor-related, death-domain-containing proteins in anoikis. Curr Biol 1999; 9: 1047-1049. (Pubitemid 29456175)
    • (1999) Current Biology , vol.9 , Issue.18 , pp. 1047-1049
    • Frisch, S.M.1
  • 7
    • 72949119124 scopus 로고    scopus 로고
    • Integrins in cancer: Biological implications and therapeutic opportunities
    • Desgrosellier JS, Cheresh DA. Integrins in cancer: biological implications and therapeutic opportunities. Nat Rev Cancer 2010; 10: 9-22.
    • (2010) Nat Rev Cancer , vol.10 , pp. 9-22
    • Desgrosellier, J.S.1    Cheresh, D.A.2
  • 8
    • 2442463476 scopus 로고    scopus 로고
    • Variant glycosylation: An underappreciated regulatory mechanism for β1 integrins
    • DOI 10.1016/j.bbamem.2004.03.012, PII S0005273604000951
    • Bellis SL. Variant glycosylation: an underappreciated regulatory mechanism for b1 integrins. Biochim Biophys Acta 2004; 1663: 52-60. (Pubitemid 38625579)
    • (2004) Biochimica et Biophysica Acta - Biomembranes , vol.1663 , Issue.1-2 , pp. 52-60
    • Bellis, S.L.1
  • 10
    • 22944456543 scopus 로고    scopus 로고
    • Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours
    • DOI 10.1111/j.1440-1711.2005.01351.x
    • Kobata A, Amano J. Altered glycosylation of proteins produced by malignant cells, and application for the diagnosis and immunotherapy of tumours. Immunol Cell Biol 2005; 83: 429-439. (Pubitemid 41044621)
    • (2005) Immunology and Cell Biology , vol.83 , Issue.4 , pp. 429-439
    • Kobata, A.1    Amano, J.2
  • 12
    • 59149102062 scopus 로고    scopus 로고
    • Glycans: Bioactive signals decoded by lectins
    • Gabius HJ. Glycans: bioactive signals decoded by lectins. Biochem Soc Trans 2008; 36 (Part 6): 1491-1496.
    • (2008) Biochem Soc Trans , vol.36 , Issue.PART 6 , pp. 1491-1496
    • Gabius, H.J.1
  • 13
    • 5144232009 scopus 로고    scopus 로고
    • Growth-regulatory human galectin-1: Crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding
    • DOI 10.1016/j.jmb.2004.08.078, PII S0022283604010782
    • López-Lucendo MF, Solis D, André S, Hirabayashi J, Kasai K, Kaltner H et al. Growthregulatory human galectin-1: crystallographic characterisation of the structural changes induced by single-site mutations and their impact on the thermodynamics of ligand binding. J Mol Biol 2004; 343: 957-970. (Pubitemid 39345956)
    • (2004) Journal of Molecular Biology , vol.343 , Issue.4 , pp. 957-970
    • Lopez-Lucendo, M.F.1    Solis, D.2    Andre, S.3    Hirabayashi, J.4    Kasai, K.-I.5    Kaltner, H.6    Gabius, H.-J.7    Romero, A.8
  • 14
    • 33646879955 scopus 로고    scopus 로고
    • Cell surface glycans: The why and how of their functionality as biochemical signals in lectin-mediated information transfer
    • Gabius H-J. Cell surface glycans: the why and how of their functionality as biochemical signals in lectin-mediated information transfer. Crit Rev Immunol 2006; 26: 43-79. (Pubitemid 43907240)
    • (2006) Critical Reviews in Immunology , vol.26 , Issue.1 , pp. 43-79
    • Gabius, H.-J.1
  • 15
    • 0034851982 scopus 로고    scopus 로고
    • Galectins as modulators of cell adhesion
    • DOI 10.1016/S0300-9084(01)01289-5
    • Hughes RC. Galectins as modulators of cell adhesion. Biochimie 2001; 83: 667-676. (Pubitemid 32821230)
    • (2001) Biochimie , vol.83 , Issue.7 , pp. 667-676
    • Hughes, R.C.1
  • 16
    • 85047689187 scopus 로고    scopus 로고
    • Sialylation of b1 integrins blocks cell adhesion to galectin-3 and protects cells against galectin-3-induced apoptosis
    • Zhuo Y, Chammas R, Bellis SL. Sialylation of b1 integrins blocks cell adhesion to galectin-3 and protects cells against galectin-3-induced apoptosis. J Biol Chem 2008; 283: 22177-22185.
    • (2008) J Biol Chem , vol.283 , pp. 22177-22185
    • Zhuo, Y.1    Chammas, R.2    Bellis, S.L.3
  • 19
    • 71549129574 scopus 로고    scopus 로고
    • Galectin-1 Is implicated in the protein kinase C e/vimentin-controlled trafficking of integrin-b1 in glioblastoma cells
    • Fortin S, Le Mercier M, Camby I, Spiegl-Kreinecker S, Berger W, Lefranc F et al. Galectin-1 Is implicated in the protein kinase C e/vimentin-controlled trafficking of integrin-b1 in glioblastoma cells. Brain Pathol 2010; 20: 39-49.
    • (2010) Brain Pathol , vol.20 , pp. 39-49
    • Fortin, S.1    Le Mercier, M.2    Camby, I.3    Spiegl-Kreinecker, S.4    Berger, W.5    Lefranc, F.6
  • 20
    • 77951153298 scopus 로고    scopus 로고
    • Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6
    • Humphries JD, Byron A, Bass MD, Craig SE, Pinney JW, Knight D et al. Proteomic analysis of integrin-associated complexes identifies RCC2 as a dual regulator of Rac1 and Arf6. Sci Signal 2009; 2: ra51.
    • (2009) Sci Signal , vol.2
    • Humphries, J.D.1    Byron, A.2    Bass, M.D.3    Craig, S.E.4    Pinney, J.W.5    Knight, D.6
  • 22
    • 0028983407 scopus 로고
    • The a5b1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression
    • Zhang Z, Vuori K, Reed JC, Ruoslahti E. The a5b1 integrin supports survival of cells on fibronectin and up-regulates Bcl-2 expression. Proc Natl Acad Sci USA 1995; 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
  • 23
    • 0034683576 scopus 로고    scopus 로고
    • A novel function for the tumor suppressor p16INK4a: Induction of anoikis via upregulation of the a5b1 fibronectin receptor
    • Plath T, Detjen K, Welzel M, von Marschall Z, Murphy D, Schirner M et al. A novel function for the tumor suppressor p16INK4a: induction of anoikis via upregulation of the a5b1 fibronectin receptor. J Cell Biol 2000; 150: 1467-1478.
    • (2000) J Cell Biol , vol.150 , pp. 1467-1478
    • Plath, T.1    Detjen, K.2    Welzel, M.3    Von Marschall, Z.4    Murphy, D.5    Schirner, M.6
  • 26
    • 45849143314 scopus 로고    scopus 로고
    • Detection of a hypersialylated b1 integrin endogenously expressed in the human astrocytoma cell line A172
    • Bartik P, Maglott A, Entlicher G, Vestweber D, Takeda K, Martin S et al. Detection of a hypersialylated b1 integrin endogenously expressed in the human astrocytoma cell line A172. Int J Oncol 2008; 32: 1021-1031.
    • (2008) Int J Oncol , vol.32 , pp. 1021-1031
    • Bartik, P.1    Maglott, A.2    Entlicher, G.3    Vestweber, D.4    Takeda, K.5    Martin, S.6
  • 27
    • 0037470066 scopus 로고    scopus 로고
    • The ST6Gal I sialyltransferase selectively modifies N-glycans on CD45 to negatively regulate galectin-1-induced CD45 clustering, phosphatase modulation, and T cell death
    • DOI 10.1074/jbc.M209595200
    • Amano M, Galvan M, He J, Baum LG. The ST6Gal I sialyltransferase selectively modifies N-glycans on CD45 to negatively regulate galectin-1-induced CD45 clustering, phosphatase modulation, and T cell death. J Biol Chem 2003; 278: 7469-7475. (Pubitemid 36800753)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 7469-7475
    • Amano, M.1    Galvan, M.2    He, J.3    Baum, L.G.4
  • 29
    • 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, Vuori K. Matrix attachment regulates Fas-induced apoptosis in endothelial cells: a role for c-flip and implications for anoikis. J Cell Biol 2001; 152: 633-643. (Pubitemid 34280244)
    • (2001) Journal of Cell Biology , vol.153 , Issue.3 , pp. 633-643
    • Aoudjit, F.1    Vuori, K.2
  • 30
    • 49649096191 scopus 로고    scopus 로고
    • Caspase-8: Fly or die
    • Frisch SM. Caspase-8: fly or die. Cancer Res 2008; 68: 4491-4493.
    • (2008) Cancer Res , vol.68 , pp. 4491-4493
    • Frisch, S.M.1
  • 31
    • 77955778590 scopus 로고    scopus 로고
    • Tumor suppressor p16INK4a: Downregulation of galectin-3, an endogenous competitor of the pro-anoikis effector galectin-1, in a pancreatic carcinoma model
    • Sanchez-Ruderisch H, Fischer C, Detjen KM, Welzel M, Wimmel A, Manning JC et al. Tumor suppressor p16INK4a: downregulation of galectin-3, an endogenous competitor of the pro-anoikis effector galectin-1, in a pancreatic carcinoma model. FEBS J 2010; 277: 3552-3563.
    • (2010) FEBS J , vol.277 , pp. 3552-3563
    • Sanchez-Ruderisch, H.1    Fischer, C.2    Detjen, K.M.3    Welzel, M.4    Wimmel, A.5    Manning, J.C.6
  • 32
    • 65949097277 scopus 로고    scopus 로고
    • Caspase-8 association with the focal adhesion complex promotes tumor cell migration and metastasis
    • Barbero S, Mielgo A, Torres V, Teitz T, Shields DJ, Mikolon D et al. Caspase-8 association with the focal adhesion complex promotes tumor cell migration and metastasis. Cancer Res 2009; 69: 3755-3763.
    • (2009) Cancer Res , vol.69 , pp. 3755-3763
    • Barbero, S.1    Mielgo, A.2    Torres, V.3    Teitz, T.4    Shields, D.J.5    Mikolon, D.6
  • 33
    • 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, Dalton WS. 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 2002; 168: 2544-2553. (Pubitemid 34171863)
    • (2002) Journal of Immunology , vol.168 , Issue.5 , pp. 2544-2553
    • Shain, K.H.1    Landowski, T.H.2    Dalton, W.S.3
  • 34
    • 0035823238 scopus 로고    scopus 로고
    • Bmf: A proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis
    • DOI 10.1126/science.1062257
    • Puthalakath H, Villunger A, O'Reilly LA, Beaumont JG, Coultas L, Cheney RE et al. Bmf: a proapoptotic BH3-only protein regulated by interaction with the myosin V actin motor complex, activated by anoikis. Science 2001; 293: 1829-1832. (Pubitemid 32845780)
    • (2001) Science , vol.293 , Issue.5536 , pp. 1829-1832
    • Puthalakath, H.1    Villunger, A.2    O'Reilly, L.A.3    Beaumont, J.G.4    Coultas, L.5    Cheney, R.E.6    Huang, D.C.S.7    Strasser, A.8
  • 35
    • 47749089820 scopus 로고    scopus 로고
    • Regulation of TNFR1 and CD95 signalling by receptor compartmentalization
    • DOI 10.1038/nrm2430, PII NRM2430
    • Schutze S, Tchikov V, Schneider-Brachert W. Regulation of TNFR1 and CD95 signalling by receptor compartmentalization. Nat Rev Mol Cell Biol 2008; 9: 655-662. (Pubitemid 352032925)
    • (2008) Nature Reviews Molecular Cell Biology , vol.9 , Issue.8 , pp. 655-662
    • Schutze, S.1    Tchikov, V.2    Schneider-Brachert, W.3
  • 36
    • 64249146003 scopus 로고    scopus 로고
    • Cross-linking of GM1 ganglioside by galectin-1 mediates regulatory T cell activity involving TRPC5 channel activation: Possible role in suppressing experimental autoimmune encephalomyelitis
    • Wang J, Lu ZH, Gabius HJ, Rohowsky-Kochan C, Ledeen RW, Wu G. Cross-linking of GM1 ganglioside by galectin-1 mediates regulatory T cell activity involving TRPC5 channel activation: possible role in suppressing experimental autoimmune encephalomyelitis. J Immunol 2009; 182: 4036-4045.
    • (2009) J Immunol , vol.182 , pp. 4036-4045
    • Wang, J.1    Zh, L.2    Gabius, H.J.3    Rohowsky-Kochan, C.4    Ledeen, R.W.5    Wu, G.6
  • 37
    • 77955873679 scopus 로고    scopus 로고
    • How adhesion/growth-regulatory galectins-1 and -3 attain cell specificity: Case study defining their target on neuroblastoma cells (SK-N-MC) and marked affinity regulation by affecting microdomain organization of the membrane
    • Kopitz J, Bergmann M, Gabius HJ. How adhesion/growth-regulatory galectins-1 and -3 attain cell specificity: case study defining their target on neuroblastoma cells (SK-N-MC) and marked affinity regulation by affecting microdomain organization of the membrane. IUBMB Life 2010; 62: 624-628.
    • (2010) IUBMB Life , vol.62 , pp. 624-628
    • Kopitz, J.1    Bergmann, M.2    Gabius, H.J.3
  • 38
    • 33747134305 scopus 로고    scopus 로고
    • Glycosyldisulfides from dynamic combinatorial libraries as O-glycoside mimetics for plant and endogenous lectins: Their reactivities in solid-phase and cell assays and conformational analysis by molecular dynamics simulations
    • DOI 10.1016/j.bmc.2006.05.045, PII S0968089606004196, Tetrahedron Prize for Creativity in Organic Chemistry 2005: B. Giese
    • André S, Pei Z, Siebert HC, Ramström O, Gabius HJ. Glycosyldisulfides from dynamic combinatorial libraries as O-glycoside mimetics for plant and endogenous lectins: their reactivities in solid-phase and cell assays and conformational analysis by molecular dynamics simulations. Bioorg Med Chem 2006; 14: 6314-6326. (Pubitemid 44224074)
    • (2006) Bioorganic and Medicinal Chemistry , vol.14 , Issue.18 , pp. 6314-6326
    • Andre, S.1    Pei, Z.2    Siebert, H.-C.3    Ramstrom, O.4    Gabius, H.-J.5
  • 39
    • 66249106029 scopus 로고    scopus 로고
    • Compensation of loss of protein function in microsatellite-unstable colon cancer cells (HCT116): A gene-dependent effect on the cell surface glycan profile
    • Patsos G, André S, Roeckel N, Gromes R, Gebert J, Kopitz J et al. Compensation of loss of protein function in microsatellite-unstable colon cancer cells (HCT116): a gene-dependent effect on the cell surface glycan profile. Glycobiology 2009; 19: 726-734.
    • (2009) Glycobiology , vol.19 , pp. 726-734
    • Patsos, G.1    André, S.2    Roeckel, N.3    Gromes, R.4    Gebert, J.5    Kopitz, J.6


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