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Volumn 52, Issue 1, 2015, Pages 385-394

A gene expression-based comparison of cell adhesion to extracellular matrix and RGD-terminated monolayers

Author keywords

Biomimetic material; Fibronectin; Integrin; Self assembled monolayer

Indexed keywords

BIOMATERIALS; BIOMIMETIC MATERIALS; BIOMIMETICS; CELL ADHESION; CELL CULTURE; GENE EXPRESSION; PEPTIDES; SELF ASSEMBLED MONOLAYERS;

EID: 84932610372     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2015.02.045     Document Type: Article
Times cited : (25)

References (83)
  • 1
    • 84861982020 scopus 로고    scopus 로고
    • The regulation of cancer cell death and metabolism by extracellular matrix attachment
    • Buchheit C.L., Rayavarapu R.R., Schafer Z.T. The regulation of cancer cell death and metabolism by extracellular matrix attachment. Semin Cell Dev Biol 2012, 23:402-411. 10.1016/j.semcdb.2012.04.007.
    • (2012) Semin Cell Dev Biol , vol.23 , pp. 402-411
    • Buchheit, C.L.1    Rayavarapu, R.R.2    Schafer, Z.T.3
  • 2
    • 77950594400 scopus 로고    scopus 로고
    • Extracellular matrix: a gatekeeper in the transition from dormancy to metastatic growth
    • Barkan D., Green J.E., Chambers A.F. Extracellular matrix: a gatekeeper in the transition from dormancy to metastatic growth. Eur J Cancer 2010, 46:1181-1188. 10.1016/j.ejca.2010.02.027.
    • (2010) Eur J Cancer , vol.46 , pp. 1181-1188
    • Barkan, D.1    Green, J.E.2    Chambers, A.F.3
  • 3
    • 0027451706 scopus 로고
    • The extracellular matrix as a cell survival factor
    • Meredith J.E., Fazeli B., Schwartz M.A. The extracellular matrix as a cell survival factor. Mol Biol Cell 1993, 4:953-961. 10.1091/mbc.4.9.953.
    • (1993) Mol Biol Cell , vol.4 , pp. 953-961
    • Meredith, J.E.1    Fazeli, B.2    Schwartz, M.A.3
  • 4
  • 5
    • 0142122297 scopus 로고    scopus 로고
    • Role of the extracellular matrix in morphogenesis
    • Kleinman H.K., Philp D., Hoffman M.P. Role of the extracellular matrix in morphogenesis. Curr Opin Biotechnol 2003, 14:526-532. 10.1016/j.copbio.2003.08.002.
    • (2003) Curr Opin Biotechnol , vol.14 , pp. 526-532
    • Kleinman, H.K.1    Philp, D.2    Hoffman, M.P.3
  • 6
    • 19644367664 scopus 로고    scopus 로고
    • Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering
    • Lutolf M.P., Hubbell J.A. Synthetic biomaterials as instructive extracellular microenvironments for morphogenesis in tissue engineering. Nat Biotechnol 2005, 23:47-55. 10.1038/nbt1055.
    • (2005) Nat Biotechnol , vol.23 , pp. 47-55
    • Lutolf, M.P.1    Hubbell, J.A.2
  • 8
    • 0041559949 scopus 로고    scopus 로고
    • RGD modified polymers: biomaterials for stimulated cell adhesion and beyond
    • Hersel U., Dahmen C., Kessler H. RGD modified polymers: biomaterials for stimulated cell adhesion and beyond. Biomaterials 2003, 24:4385-4415. 10.1016/S0142-9612(03)00343-0.
    • (2003) Biomaterials , vol.24 , pp. 4385-4415
    • Hersel, U.1    Dahmen, C.2    Kessler, H.3
  • 9
    • 70249120017 scopus 로고    scopus 로고
    • Polymer brushes and self-assembled monolayers: versatile platforms to control cell adhesion to biomaterials (Review)
    • Raynor J.E., Capadona J.R., Collard D.M., Petrie T.A., García A.J. Polymer brushes and self-assembled monolayers: versatile platforms to control cell adhesion to biomaterials (Review). Biointerphases 2009, 4:FA3-16. 10.1116/1.3089252.
    • (2009) Biointerphases , vol.4 , pp. FA3-16
    • Raynor, J.E.1    Capadona, J.R.2    Collard, D.M.3    Petrie, T.A.4    García, A.J.5
  • 10
    • 84880917721 scopus 로고    scopus 로고
    • Dynamic cell-adhesive microenvironments and their effect on myogenic differentiation
    • Weis S., Lee T.T., del Campo A., García A.J. Dynamic cell-adhesive microenvironments and their effect on myogenic differentiation. Acta Biomater 2013, 9:8059-8066. 10.1016/j.actbio.2013.06.019.
    • (2013) Acta Biomater , vol.9 , pp. 8059-8066
    • Weis, S.1    Lee, T.T.2    del Campo, A.3    García, A.J.4
  • 11
    • 84859323531 scopus 로고    scopus 로고
    • Sequence, structure, and function of peptide self-assembled monolayers
    • Nowinski A.K., Sun F., White A.D., Keefe A.J., Jiang S. Sequence, structure, and function of peptide self-assembled monolayers. JAm Chem Soc 2012, 134:6000-6005. 10.1021/ja3006868.
    • (2012) JAm Chem Soc , vol.134 , pp. 6000-6005
    • Nowinski, A.K.1    Sun, F.2    White, A.D.3    Keefe, A.J.4    Jiang, S.5
  • 12
    • 0023378093 scopus 로고
    • Fibroblast adhesion to RGDS shows novel features compared with fibronectin
    • Streeter H.B., Rees D.A. Fibroblast adhesion to RGDS shows novel features compared with fibronectin. JCell Biol 1987, 105:507-515. 10.1083/jcb.105.1.507.
    • (1987) JCell Biol , vol.105 , pp. 507-515
    • Streeter, H.B.1    Rees, D.A.2
  • 13
    • 77950427004 scopus 로고    scopus 로고
    • Geometric cues for directing the differentiation of mesenchymal stem cells
    • Kilian K.A., Bugarija B., Lahn B.T., Mrksich M. Geometric cues for directing the differentiation of mesenchymal stem cells. Proc Natl Acad Sci 2010, 10.1073/pnas.0903269107.
    • (2010) Proc Natl Acad Sci
    • Kilian, K.A.1    Bugarija, B.2    Lahn, B.T.3    Mrksich, M.4
  • 14
    • 84860869042 scopus 로고    scopus 로고
    • Directing stem cell fate by controlling the affinity and density of ligand-receptor interactions at the biomaterials interface
    • Kilian K.A., Mrksich M. Directing stem cell fate by controlling the affinity and density of ligand-receptor interactions at the biomaterials interface. Angew Chem Int Ed 2012, 51:4891-4895. 10.1002/anie.201108746.
    • (2012) Angew Chem Int Ed , vol.51 , pp. 4891-4895
    • Kilian, K.A.1    Mrksich, M.2
  • 15
    • 78249280319 scopus 로고    scopus 로고
    • An inhibitor of a cell adhesion receptor stimulates cell migration
    • Shabbir S.H., Eisenberg J.L., Mrksich M. An inhibitor of a cell adhesion receptor stimulates cell migration. Angew Chem Int Ed 2010, 49:7706-7709. 10.1002/anie.201002699.
    • (2010) Angew Chem Int Ed , vol.49 , pp. 7706-7709
    • Shabbir, S.H.1    Eisenberg, J.L.2    Mrksich, M.3
  • 16
    • 0037418481 scopus 로고    scopus 로고
    • Fibronectin adsorption and cell adhesion to mixed monolayers of tri(ethylene glycol)- and methyl-terminated alkanethiols
    • Capadona J.R., Collard D.M., García A.J. Fibronectin adsorption and cell adhesion to mixed monolayers of tri(ethylene glycol)- and methyl-terminated alkanethiols. Langmuir 2003, 19:1847-1852. 10.1021/la026244+.
    • (2003) Langmuir , vol.19 , pp. 1847-1852
    • Capadona, J.R.1    Collard, D.M.2    García, A.J.3
  • 17
    • 77955874342 scopus 로고    scopus 로고
    • Multivalent integrin-specific ligands enhance tissue healing and biomaterial integration
    • Petrie T.A., Raynor J.E., Dumbauld D.W., Lee T.T., Jagtap S., Templeman K.L., et al. Multivalent integrin-specific ligands enhance tissue healing and biomaterial integration. Sci Transl Med 2010, 2:45ra60. 10.1126/scitranslmed.3001002.
    • (2010) Sci Transl Med , vol.2 , pp. 45ra60
    • Petrie, T.A.1    Raynor, J.E.2    Dumbauld, D.W.3    Lee, T.T.4    Jagtap, S.5    Templeman, K.L.6
  • 18
    • 42949130583 scopus 로고    scopus 로고
    • Integrin-dependent translational control: implication in cancer progression
    • Chung J., Kim T.H. Integrin-dependent translational control: implication in cancer progression. Microsc Res Tech 2008, 71:380-386. 10.1002/jemt.20566.
    • (2008) Microsc Res Tech , vol.71 , pp. 380-386
    • Chung, J.1    Kim, T.H.2
  • 20
    • 0032077411 scopus 로고    scopus 로고
    • Micropatterned surfaces for control of cell shape, position, and function
    • Chen C.S., Mrksich M., Huang S., Whitesides G.M., Ingber D.E. Micropatterned surfaces for control of cell shape, position, and function. Biotechnol Prog 1998, 14:356-363. 10.1021/bp980031m.
    • (1998) Biotechnol Prog , vol.14 , pp. 356-363
    • Chen, C.S.1    Mrksich, M.2    Huang, S.3    Whitesides, G.M.4    Ingber, D.E.5
  • 21
    • 0031824197 scopus 로고    scopus 로고
    • Tailored substrates for studies of attached cell culture
    • Mrksich M. Tailored substrates for studies of attached cell culture. Cell Mol Life Sci CMLS 1998, 54:653-662. 10.1007/s000180050193.
    • (1998) Cell Mol Life Sci CMLS , vol.54 , pp. 653-662
    • Mrksich, M.1
  • 22
    • 5144224487 scopus 로고    scopus 로고
    • Direct comparison of the spread area, contractility, and migration of balb/c 3T3 fibroblasts adhered to fibronectin- and RGD-modified substrata
    • Rajagopalan P., Marganski W.A., Brown X.Q., Wong J.Y. Direct comparison of the spread area, contractility, and migration of balb/c 3T3 fibroblasts adhered to fibronectin- and RGD-modified substrata. Biophys J 2004, 87:2818-2827. 10.1529/biophysj.103.037218.
    • (2004) Biophys J , vol.87 , pp. 2818-2827
    • Rajagopalan, P.1    Marganski, W.A.2    Brown, X.Q.3    Wong, J.Y.4
  • 23
    • 0023637601 scopus 로고
    • New perspectives in cell adhesion: RGD and integrins
    • Ruoslahti E., Pierschbacher M.D. New perspectives in cell adhesion: RGD and integrins. Science 1987, 238:491-497. 10.1126/science.2821619.
    • (1987) Science , vol.238 , pp. 491-497
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 24
    • 0023058313 scopus 로고
    • Arg-Gly-Asp: a versatile cell recognition signal
    • Ruoslahti E., Pierschbacher M.D. Arg-Gly-Asp: a versatile cell recognition signal. Cell 1986, 44:517-518. 10.1016/0092-8674(86)90259-X.
    • (1986) Cell , vol.44 , pp. 517-518
    • Ruoslahti, E.1    Pierschbacher, M.D.2
  • 25
    • 0031430278 scopus 로고    scopus 로고
    • Enhancement of cell interactions with collagen/glycosaminoglycan matrices by RGD derivatization
    • Grzesiak J.J., Pierschbacher M.D., Amodeo M.F., Malaney T.I., Glass J.R. Enhancement of cell interactions with collagen/glycosaminoglycan matrices by RGD derivatization. Biomaterials 1997, 18:1625-1632. 10.1016/S0142-9612(97)00103-8.
    • (1997) Biomaterials , vol.18 , pp. 1625-1632
    • Grzesiak, J.J.1    Pierschbacher, M.D.2    Amodeo, M.F.3    Malaney, T.I.4    Glass, J.R.5
  • 26
    • 0021271957 scopus 로고
    • Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule
    • Pierschbacher M.D., Ruoslahti E. Cell attachment activity of fibronectin can be duplicated by small synthetic fragments of the molecule. Nature 1984, 309:30-33.
    • (1984) Nature , vol.309 , pp. 30-33
    • Pierschbacher, M.D.1    Ruoslahti, E.2
  • 27
    • 72949107796 scopus 로고    scopus 로고
    • Anovel strategy to graft RGD peptide on biomaterials surfaces for endothelization of small-diamater vascular grafts and tissue engineering blood vessel
    • Li J., Ding M., Fu Q., Tan H., Xie X., Zhong Y. Anovel strategy to graft RGD peptide on biomaterials surfaces for endothelization of small-diamater vascular grafts and tissue engineering blood vessel. JMater Sci Mater Med 2008, 19:2595-2603. 10.1007/s10856-007-3354-5.
    • (2008) JMater Sci Mater Med , vol.19 , pp. 2595-2603
    • Li, J.1    Ding, M.2    Fu, Q.3    Tan, H.4    Xie, X.5    Zhong, Y.6
  • 28
    • 0027267959 scopus 로고
    • Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library
    • Koivunen E., Gay D.A., Ruoslahti E. Selection of peptides binding to the alpha 5 beta 1 integrin from phage display library. JBiol Chem 1993, 268:20205-20210.
    • (1993) JBiol Chem , vol.268 , pp. 20205-20210
    • Koivunen, E.1    Gay, D.A.2    Ruoslahti, E.3
  • 29
    • 0028899525 scopus 로고
    • Phage libraries displaying cyclic peptides with different ring sizes: ligand specificities of the RGD-directed integrins
    • Koivunen E., Wang B., Ruoslahti E. Phage libraries displaying cyclic peptides with different ring sizes: ligand specificities of the RGD-directed integrins. Nat Biotechnol 1995, 13:265-270. 10.1038/nbt0395-265.
    • (1995) Nat Biotechnol , vol.13 , pp. 265-270
    • Koivunen, E.1    Wang, B.2    Ruoslahti, E.3
  • 30
    • 84865514143 scopus 로고    scopus 로고
    • Flexible or fixed: a comparative review of linear and cyclic cancer-targeting peptides
    • Roxin Á., Zheng G. Flexible or fixed: a comparative review of linear and cyclic cancer-targeting peptides. Future Med Chem 2012, 4:1601-1618. 10.4155/fmc.12.75.
    • (2012) Future Med Chem , vol.4 , pp. 1601-1618
    • Roxin, Á.1    Zheng, G.2
  • 31
    • 0029778085 scopus 로고    scopus 로고
    • Structural and functional aspects of RGD-containing cyclic pentapeptides as highly potent and selective integrin αVβ3 antagonists
    • Haubner R., Gratias R., Diefenbach B., Goodman S.L., Jonczyk A., Kessler H. Structural and functional aspects of RGD-containing cyclic pentapeptides as highly potent and selective integrin αVβ3 antagonists. JAm Chem Soc 1996, 118:7461-7472. 10.1021/ja9603721.
    • (1996) JAm Chem Soc , vol.118 , pp. 7461-7472
    • Haubner, R.1    Gratias, R.2    Diefenbach, B.3    Goodman, S.L.4    Jonczyk, A.5    Kessler, H.6
  • 34
    • 80054003242 scopus 로고    scopus 로고
    • Chipster: user-friendly analysis software for microarray and other high-throughput data
    • Kallio M.A., Tuimala J.T., Hupponen T., Klemelä P., Gentile M., Scheinin I., et al. Chipster: user-friendly analysis software for microarray and other high-throughput data. BMC Genomics 2011, 12:507. 10.1186/1471-2164-12-507.
    • (2011) BMC Genomics , vol.12 , pp. 507
    • Kallio, M.A.1    Tuimala, J.T.2    Hupponen, T.3    Klemelä, P.4    Gentile, M.5    Scheinin, I.6
  • 35
    • 34250705360 scopus 로고    scopus 로고
    • NuID: a universal naming scheme of oligonucleotides for illumina, affymetrix, and other microarrays
    • Du P., Kibbe W.A., Lin S.M. nuID: a universal naming scheme of oligonucleotides for illumina, affymetrix, and other microarrays. Biol Direct 2007, 2:1-7. 10.1186/1745-6150-2-16.
    • (2007) Biol Direct , vol.2 , pp. 1-7
    • Du, P.1    Kibbe, W.A.2    Lin, S.M.3
  • 36
    • 46249088370 scopus 로고    scopus 로고
    • Lumi: a pipeline for processing illumina microarray
    • Du P., Kibbe W.A., Lin S.M. lumi: a pipeline for processing illumina microarray. Bioinformatics 2008, 24:1547-1548. 10.1093/bioinformatics/btn224.
    • (2008) Bioinformatics , vol.24 , pp. 1547-1548
    • Du, P.1    Kibbe, W.A.2    Lin, S.M.3
  • 37
    • 39149111937 scopus 로고    scopus 로고
    • Model-based variance-stabilizing transformation for illumina microarray data
    • Lin S.M., Du P., Huber W., Kibbe W.A. Model-based variance-stabilizing transformation for illumina microarray data. Nucleic Acids Res 2008, 36:e11. 10.1093/nar/gkm1075.
    • (2008) Nucleic Acids Res , vol.36 , pp. e11
    • Lin, S.M.1    Du, P.2    Huber, W.3    Kibbe, W.A.4
  • 38
    • 12344330424 scopus 로고    scopus 로고
    • LimmaGUI: a graphical user interface for linear modeling of microarray data
    • Wettenhall J.M., Smyth G.K. limmaGUI: a graphical user interface for linear modeling of microarray data. Bioinformatics 2004, 20:3705-3706. 10.1093/bioinformatics/bth449.
    • (2004) Bioinformatics , vol.20 , pp. 3705-3706
    • Wettenhall, J.M.1    Smyth, G.K.2
  • 39
    • 60649112649 scopus 로고    scopus 로고
    • Using self-assembled monolayers to model the extracellular matrix
    • Mrksich M. Using self-assembled monolayers to model the extracellular matrix. Acta Biomater 2009, 5:832-841. 10.1016/j.actbio.2009.01.016.
    • (2009) Acta Biomater , vol.5 , pp. 832-841
    • Mrksich, M.1
  • 40
    • 60549098867 scopus 로고    scopus 로고
    • Quantitative analysis of protein adsorption via atomic force microscopy and surface plasmon resonance
    • Servoli E., Maniglio D., Aguilar M.R., Motta A., Roman J.S., Belfiore L.A., et al. Quantitative analysis of protein adsorption via atomic force microscopy and surface plasmon resonance. Macromol Biosci 2008, 8:1126-1134. 10.1002/mabi.200800110.
    • (2008) Macromol Biosci , vol.8 , pp. 1126-1134
    • Servoli, E.1    Maniglio, D.2    Aguilar, M.R.3    Motta, A.4    Roman, J.S.5    Belfiore, L.A.6
  • 41
    • 0001604172 scopus 로고
    • Surface plasmon resonance permits in situ measurement of protein adsorption on self-assembled monolayers of alkanethiolates on gold
    • Mrksich M., Sigal G.B., Whitesides G.M. Surface plasmon resonance permits in situ measurement of protein adsorption on self-assembled monolayers of alkanethiolates on gold. Langmuir 1995, 11:4383-4385. 10.1021/la00011a034.
    • (1995) Langmuir , vol.11 , pp. 4383-4385
    • Mrksich, M.1    Sigal, G.B.2    Whitesides, G.M.3
  • 42
    • 0032522286 scopus 로고    scopus 로고
    • Effect of surface wettability on the adsorption of proteins and detergents
    • Sigal G.B., Mrksich M., Whitesides G.M. Effect of surface wettability on the adsorption of proteins and detergents. JAm Chem Soc 1998, 120:3464-3473. 10.1021/ja970819l.
    • (1998) JAm Chem Soc , vol.120 , pp. 3464-3473
    • Sigal, G.B.1    Mrksich, M.2    Whitesides, G.M.3
  • 43
    • 2542516863 scopus 로고    scopus 로고
    • Rewiring cell adhesion
    • Kato M., Mrksich M. Rewiring cell adhesion. JAm Chem Soc 2004, 126:6504-6505. 10.1021/ja039058e.
    • (2004) JAm Chem Soc , vol.126 , pp. 6504-6505
    • Kato, M.1    Mrksich, M.2
  • 44
    • 0026342146 scopus 로고
    • Synthesis and cell attachment activity of bioactive oligopeptides: RGD, RGDS, RGDV, and RGDT
    • Hirano Y., Kando Y., Hayashi T., Goto K., Nakajima A. Synthesis and cell attachment activity of bioactive oligopeptides: RGD, RGDS, RGDV, and RGDT. JBiomed Mater Res 1991, 25:1523-1534. 10.1002/jbm.820251209.
    • (1991) JBiomed Mater Res , vol.25 , pp. 1523-1534
    • Hirano, Y.1    Kando, Y.2    Hayashi, T.3    Goto, K.4    Nakajima, A.5
  • 45
    • 1942421295 scopus 로고    scopus 로고
    • Attachment and spreading of fibroblasts on an RGD peptide-modified injectable hyaluronan hydrogel
    • Shu X.Z., Ghosh K., Liu Y., Palumbo F.S., Luo Y., Clark R.A., et al. Attachment and spreading of fibroblasts on an RGD peptide-modified injectable hyaluronan hydrogel. JBiomed Mater Res A 2004, 68A:365-375. 10.1002/jbm.a.20002.
    • (2004) JBiomed Mater Res A , vol.68A , pp. 365-375
    • Shu, X.Z.1    Ghosh, K.2    Liu, Y.3    Palumbo, F.S.4    Luo, Y.5    Clark, R.A.6
  • 46
    • 80055068206 scopus 로고    scopus 로고
    • Role of receptor for hyaluronic acid-mediated motility (RHAMM) in low molecular weight hyaluronan (LMWHA)-mediated fibrosarcoma cell adhesion
    • Kouvidi K., Berdiaki A., Nikitovic D., Katonis P., Afratis N., Hascall V.C., et al. Role of receptor for hyaluronic acid-mediated motility (RHAMM) in low molecular weight hyaluronan (LMWHA)-mediated fibrosarcoma cell adhesion. JBiol Chem 2011, 286:38509-38520. 10.1074/jbc.M111.275875.
    • (2011) JBiol Chem , vol.286 , pp. 38509-38520
    • Kouvidi, K.1    Berdiaki, A.2    Nikitovic, D.3    Katonis, P.4    Afratis, N.5    Hascall, V.C.6
  • 47
    • 84909948417 scopus 로고    scopus 로고
    • Monoclonal antibodies to human laminin α4 chain globular domain inhibit tumor cell adhesion and migration on laminins 411 and 421, and binding of α6β1 integrin and MCAM to α4-laminins
    • Ishikawa T., Wondimu Z., Oikawa Y., Ingerpuu S., Virtanen I., Patarroyo M. Monoclonal antibodies to human laminin α4 chain globular domain inhibit tumor cell adhesion and migration on laminins 411 and 421, and binding of α6β1 integrin and MCAM to α4-laminins. Matrix Biol 2014, 36:5-14. 10.1016/j.matbio.2014.03.003.
    • (2014) Matrix Biol , vol.36 , pp. 5-14
    • Ishikawa, T.1    Wondimu, Z.2    Oikawa, Y.3    Ingerpuu, S.4    Virtanen, I.5    Patarroyo, M.6
  • 48
    • 84859875708 scopus 로고    scopus 로고
    • Matrix metalloproteinase-9 silencing by RNA interference promotes the adhesive-invasive switch in HT1080 human fibrosarcoma cells
    • Zhu X., Tai W., Shi W., Song Y., Zhang H., An G. Matrix metalloproteinase-9 silencing by RNA interference promotes the adhesive-invasive switch in HT1080 human fibrosarcoma cells. Clin Lab 2012, 58:313-322.
    • (2012) Clin Lab , vol.58 , pp. 313-322
    • Zhu, X.1    Tai, W.2    Shi, W.3    Song, Y.4    Zhang, H.5    An, G.6
  • 49
    • 77953121357 scopus 로고    scopus 로고
    • Adistinctive role for focal adhesion proteins in three-dimensional cell motility
    • Fraley S.I., Feng Y., Krishnamurthy R., Kim D.-H., Celedon A., Longmore G.D., et al. Adistinctive role for focal adhesion proteins in three-dimensional cell motility. Nat Cell Biol 2010, 12:598-604. 10.1038/ncb2062.
    • (2010) Nat Cell Biol , vol.12 , pp. 598-604
    • Fraley, S.I.1    Feng, Y.2    Krishnamurthy, R.3    Kim, D.-H.4    Celedon, A.5    Longmore, G.D.6
  • 50
    • 61449205308 scopus 로고    scopus 로고
    • Resveratrol inhibits tumor cell adhesion to endothelial cells by blocking ICAM-1 expression
    • Park J.S., Kim K.M., Kim M.H., Chang H.J., Baek M.K., Kim S.M., et al. Resveratrol inhibits tumor cell adhesion to endothelial cells by blocking ICAM-1 expression. Anticancer Res 2009, 29:355-362.
    • (2009) Anticancer Res , vol.29 , pp. 355-362
    • Park, J.S.1    Kim, K.M.2    Kim, M.H.3    Chang, H.J.4    Baek, M.K.5    Kim, S.M.6
  • 51
    • 0035930611 scopus 로고    scopus 로고
    • Selective binding of collagen subtypes by integrin α1I, α2I, and α10I domains
    • Tulla M., Pentikäinen O.T., Viitasalo T., Käpylä J., Impola U., Nykvist P., et al. Selective binding of collagen subtypes by integrin α1I, α2I, and α10I domains. JBiol Chem 2001, 276:48206-48212.
    • (2001) JBiol Chem , vol.276 , pp. 48206-48212
    • Tulla, M.1    Pentikäinen, O.T.2    Viitasalo, T.3    Käpylä, J.4    Impola, U.5    Nykvist, P.6
  • 52
    • 1642535425 scopus 로고    scopus 로고
    • αvβ3 and αvβ5 integrins bind both the proximal RGD site and non-RGD motifs within noncollagenous (NC1) domain of the α3 chain of type IV collagen implication for the mechanism of endothelial cell adhesion
    • Pedchenko V., Zent R., Hudson B.G. αvβ3 and αvβ5 integrins bind both the proximal RGD site and non-RGD motifs within noncollagenous (NC1) domain of the α3 chain of type IV collagen implication for the mechanism of endothelial cell adhesion. JBiol Chem 2004, 279:2772-2780. 10.1074/jbc.M311901200.
    • (2004) JBiol Chem , vol.279 , pp. 2772-2780
    • Pedchenko, V.1    Zent, R.2    Hudson, B.G.3
  • 53
    • 21844450866 scopus 로고    scopus 로고
    • Ahighly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia
    • Gu Z., Cui J., Brown S., Fridman R., Mobashery S., Strongin A.Y., et al. Ahighly specific inhibitor of matrix metalloproteinase-9 rescues laminin from proteolysis and neurons from apoptosis in transient focal cerebral ischemia. JNeurosci 2005, 25:6401-6408. 10.1523/JNEUROSCI.1563-05.2005.
    • (2005) JNeurosci , vol.25 , pp. 6401-6408
    • Gu, Z.1    Cui, J.2    Brown, S.3    Fridman, R.4    Mobashery, S.5    Strongin, A.Y.6
  • 54
    • 2342551058 scopus 로고    scopus 로고
    • Cell adhesion and signaling on the fibronectin 1st type III repeat; requisite roles for cell surface proteoglycans and integrins
    • Mercurius K.O., Morla A.O. Cell adhesion and signaling on the fibronectin 1st type III repeat; requisite roles for cell surface proteoglycans and integrins. BMC Cell Biol 2001, 2:1-13. 10.1186/1471-2121-2-18.
    • (2001) BMC Cell Biol , vol.2 , pp. 1-13
    • Mercurius, K.O.1    Morla, A.O.2
  • 55
    • 0028213868 scopus 로고
    • Conformation dependence of integrin-type II collagen binding. Inability of collagen peptides to support alpha 2 beta 1 binding, and mediation of adhesion to denatured collagen by a novel alpha 5 beta 1-fibronectin bridge
    • Tuckwell D.S., Ayad S., Grant M.E., Takigawa M., Humphries M.J. Conformation dependence of integrin-type II collagen binding. Inability of collagen peptides to support alpha 2 beta 1 binding, and mediation of adhesion to denatured collagen by a novel alpha 5 beta 1-fibronectin bridge. JCell Sci 1994, 107:993-1005.
    • (1994) JCell Sci , vol.107 , pp. 993-1005
    • Tuckwell, D.S.1    Ayad, S.2    Grant, M.E.3    Takigawa, M.4    Humphries, M.J.5
  • 56
    • 0025264295 scopus 로고
    • The alpha 2 beta 1 integrin cell surface collagen receptor binds to the alpha 1 (I)-CB3 peptide of collagen
    • Staatz W.D., Walsh J.J., Pexton T., Santoro S.A. The alpha 2 beta 1 integrin cell surface collagen receptor binds to the alpha 1 (I)-CB3 peptide of collagen. JBiol Chem 1990, 265:4778-4781.
    • (1990) JBiol Chem , vol.265 , pp. 4778-4781
    • Staatz, W.D.1    Walsh, J.J.2    Pexton, T.3    Santoro, S.A.4
  • 57
  • 58
    • 84861376261 scopus 로고    scopus 로고
    • Integrin structure and function
    • Springer, New York, R. Zent, A. Pozzi (Eds.)
    • Srichai M.B., Zent R. Integrin structure and function. Cell-extracell. Matrix interact. Cancer 2010, 19-41. Springer, New York. R. Zent, A. Pozzi (Eds.).
    • (2010) Cell-extracell. Matrix interact. Cancer , pp. 19-41
    • Srichai, M.B.1    Zent, R.2
  • 59
    • 34648847301 scopus 로고    scopus 로고
    • Adsorption and viscoelastic properties of fractionated mucin (BSM) and bovine serum albumin (BSA) studied with quartz crystal microbalance (QCM-D)
    • Feiler A.A., Sahlholm A., Sandberg T., Caldwell K.D. Adsorption and viscoelastic properties of fractionated mucin (BSM) and bovine serum albumin (BSA) studied with quartz crystal microbalance (QCM-D). JColloid Interface Sci 2007, 315:475-481. 10.1016/j.jcis.2007.07.029.
    • (2007) JColloid Interface Sci , vol.315 , pp. 475-481
    • Feiler, A.A.1    Sahlholm, A.2    Sandberg, T.3    Caldwell, K.D.4
  • 60
    • 0023613971 scopus 로고
    • Modification of material surfaces to affect how they interact with blood
    • Hoffman A.S. Modification of material surfaces to affect how they interact with blood. Ann N Y Acad Sci 1987, 516:96-101. 10.1111/j.1749-6632.1987.tb33033.x.
    • (1987) Ann N Y Acad Sci , vol.516 , pp. 96-101
    • Hoffman, A.S.1
  • 61
    • 0028072225 scopus 로고
    • Inhibition of anchorage-dependent cell spreading triggers apoptosis in cultured human endothelial cells
    • Re F., Zanetti A., Sironi M., Polentarutti N., Lanfrancone L., Dejana E., et al. Inhibition of anchorage-dependent cell spreading triggers apoptosis in cultured human endothelial cells. JCell Biol 1994, 127:537-546. 10.1083/jcb.127.2.537.
    • (1994) JCell Biol , vol.127 , pp. 537-546
    • Re, F.1    Zanetti, A.2    Sironi, M.3    Polentarutti, N.4    Lanfrancone, L.5    Dejana, E.6
  • 62
    • 67349089040 scopus 로고    scopus 로고
    • From mechanotransduction to extracellular matrix gene expression in fibroblasts
    • Chiquet M., Gelman L., Lutz R., Maier S. From mechanotransduction to extracellular matrix gene expression in fibroblasts. Biochim Biophys Acta BBA - Mol Cell Res 2009, 1793:911-920. 10.1016/j.bbamcr.2009.01.012.
    • (2009) Biochim Biophys Acta BBA - Mol Cell Res , vol.1793 , pp. 911-920
    • Chiquet, M.1    Gelman, L.2    Lutz, R.3    Maier, S.4
  • 63
    • 22744448697 scopus 로고    scopus 로고
    • Mechanical signals regulating extracellular matrix gene expression in fibroblasts
    • Sarasa-Renedo A., Chiquet M. Mechanical signals regulating extracellular matrix gene expression in fibroblasts. Scand J Med Sci Sports 2005, 15:223-230. 10.1111/j.1600-0838.2005.00461.x.
    • (2005) Scand J Med Sci Sports , vol.15 , pp. 223-230
    • Sarasa-Renedo, A.1    Chiquet, M.2
  • 64
    • 0032835380 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 activation in human hepatic fibrosis regulation by cell-matrix interactions
    • Préaux A.-M., Mallat A., Van Nhieu J.T., d'Ortho M.-P., Hembry R.M., Mavier P. Matrix metalloproteinase-2 activation in human hepatic fibrosis regulation by cell-matrix interactions. Hepatology 1999, 30:944-950. 10.1002/hep.510300432.
    • (1999) Hepatology , vol.30 , pp. 944-950
    • Préaux, A.-M.1    Mallat, A.2    Van Nhieu, J.T.3    d'Ortho, M.-P.4    Hembry, R.M.5    Mavier, P.6
  • 65
    • 0031727149 scopus 로고    scopus 로고
    • The activation of ProMMP-2 (gelatinase A) by HT1080 fibrosarcoma cells is promoted by culture on a fibronectin substrate and is concomitant with an increase in processing of MT1-MMP (MMP-14) to a 45 kDa form
    • Stanton H., Gavrilovic J., Atkinson S., d'Ortho M., Yamada K., Zardi L., et al. The activation of ProMMP-2 (gelatinase A) by HT1080 fibrosarcoma cells is promoted by culture on a fibronectin substrate and is concomitant with an increase in processing of MT1-MMP (MMP-14) to a 45 kDa form. JCell Sci 1998, 111:2789-2798.
    • (1998) JCell Sci , vol.111 , pp. 2789-2798
    • Stanton, H.1    Gavrilovic, J.2    Atkinson, S.3    d'Ortho, M.4    Yamada, K.5    Zardi, L.6
  • 66
    • 0026647568 scopus 로고
    • Mechanism of human keratinocyte migration on fibronectin: unique roles of RGD site and integrins
    • Kim J.P., Zhang K., Chen J.D., Wynn K.C., Kramer R.H., Woodley D.T. Mechanism of human keratinocyte migration on fibronectin: unique roles of RGD site and integrins. JCell Physiol 1992, 151:443-450. 10.1002/jcp.1041510303.
    • (1992) JCell Physiol , vol.151 , pp. 443-450
    • Kim, J.P.1    Zhang, K.2    Chen, J.D.3    Wynn, K.C.4    Kramer, R.H.5    Woodley, D.T.6
  • 68
    • 84888639329 scopus 로고    scopus 로고
    • Acomparative study of polyethylene glycol hydrogels derivatized with the RGD peptide and the cell-binding domain of fibronectin
    • Zhang C., Hekmatfer S., Karuri N.W. Acomparative study of polyethylene glycol hydrogels derivatized with the RGD peptide and the cell-binding domain of fibronectin. JBiomed Mater Res A 2014, 102:170-179. 10.1002/jbm.a.34687.
    • (2014) JBiomed Mater Res A , vol.102 , pp. 170-179
    • Zhang, C.1    Hekmatfer, S.2    Karuri, N.W.3
  • 69
    • 1542267780 scopus 로고    scopus 로고
    • Using model substrates to study the dependence of focal adhesion formation on the affinity of integrin-ligand complexes
    • Kato M., Mrksich M. Using model substrates to study the dependence of focal adhesion formation on the affinity of integrin-ligand complexes. Biochemistry (Mosc) 2004, 43:2699-2707. 10.1021/bi0352670.
    • (2004) Biochemistry (Mosc) , vol.43 , pp. 2699-2707
    • Kato, M.1    Mrksich, M.2
  • 70
    • 24944436269 scopus 로고    scopus 로고
    • Cell tension, matrix mechanics, and cancer development
    • Huang S., Ingber D.E. Cell tension, matrix mechanics, and cancer development. Cancer Cell 2005, 8:175-176. 10.1016/j.ccr.2005.08.009.
    • (2005) Cancer Cell , vol.8 , pp. 175-176
    • Huang, S.1    Ingber, D.E.2
  • 71
    • 33745245989 scopus 로고    scopus 로고
    • Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration
    • Gupton S.L., Waterman-Storer C.M. Spatiotemporal feedback between actomyosin and focal-adhesion systems optimizes rapid cell migration. Cell 2006, 125:1361-1374. 10.1016/j.cell.2006.05.029.
    • (2006) Cell , vol.125 , pp. 1361-1374
    • Gupton, S.L.1    Waterman-Storer, C.M.2
  • 72
    • 19944428596 scopus 로고    scopus 로고
    • Effects of substrate stiffness on cell morphology, cytoskeletal structure, and adhesion
    • Yeung T., Georges P.C., Flanagan L.A., Marg B., Ortiz M., Funaki M., et al. Effects of substrate stiffness on cell morphology, cytoskeletal structure, and adhesion. Cell Motil Cytoskelet 2005, 60:24-34. 10.1002/cm.20041.
    • (2005) Cell Motil Cytoskelet , vol.60 , pp. 24-34
    • Yeung, T.1    Georges, P.C.2    Flanagan, L.A.3    Marg, B.4    Ortiz, M.5    Funaki, M.6
  • 73
    • 0027752979 scopus 로고
    • Alink between cyclin A expression and adhesion-dependent cell cycle progression
    • Guadagno T.M., Ohtsubo M., Roberts J.M., Assoian R.K. Alink between cyclin A expression and adhesion-dependent cell cycle progression. Science 1993, 262:1572-1575. 10.1126/science.8248807.
    • (1993) Science , vol.262 , pp. 1572-1575
    • Guadagno, T.M.1    Ohtsubo, M.2    Roberts, J.M.3    Assoian, R.K.4
  • 74
    • 68049105101 scopus 로고    scopus 로고
    • Rab GTPases as coordinators of vesicle traffic
    • Stenmark H. Rab GTPases as coordinators of vesicle traffic. Nat Rev Mol Cell Biol 2009, 10:513-525. 10.1038/nrm2728.
    • (2009) Nat Rev Mol Cell Biol , vol.10 , pp. 513-525
    • Stenmark, H.1
  • 75
    • 52549126992 scopus 로고    scopus 로고
    • Membrane traffic in the secretory pathway
    • Fukuda M. Membrane traffic in the secretory pathway. Cell Mol Life Sci 2008, 65:2801-2813. 10.1007/s00018-008-8351-4.
    • (2008) Cell Mol Life Sci , vol.65 , pp. 2801-2813
    • Fukuda, M.1
  • 76
    • 84863628119 scopus 로고    scopus 로고
    • Ferritin blocks inhibitory effects of two-chain high molecular weight kininogen (HKa) on adhesion and survival signaling in endothelial cells
    • Tesfay L., Huhn A.J., Hatcher H., Torti F.M., Torti S.V. Ferritin blocks inhibitory effects of two-chain high molecular weight kininogen (HKa) on adhesion and survival signaling in endothelial cells. PLoS One 2012, 7:e40030. 10.1371/journal.pone.0040030.
    • (2012) PLoS One , vol.7 , pp. e40030
    • Tesfay, L.1    Huhn, A.J.2    Hatcher, H.3    Torti, F.M.4    Torti, S.V.5
  • 77
    • 0027132348 scopus 로고
    • Use of recombinant and synthetic peptides as attachment factors for cells on microcarriers
    • Varani J., Inman D.R., Fligiel S.E.G., Hillegas W.J. Use of recombinant and synthetic peptides as attachment factors for cells on microcarriers. Cytotechnology 1993, 13:89-98. 10.1007/BF00749935.
    • (1993) Cytotechnology , vol.13 , pp. 89-98
    • Varani, J.1    Inman, D.R.2    Fligiel, S.E.G.3    Hillegas, W.J.4
  • 78
    • 0032721971 scopus 로고    scopus 로고
    • Surface modification for controlled studies of cell-ligand interactions
    • Neff J.A., Tresco P.A., Caldwell K.D. Surface modification for controlled studies of cell-ligand interactions. Biomaterials 1999, 20:2377-2393. 10.1016/S0142-9612(99)00166-0.
    • (1999) Biomaterials , vol.20 , pp. 2377-2393
    • Neff, J.A.1    Tresco, P.A.2    Caldwell, K.D.3
  • 79
    • 0035128654 scopus 로고    scopus 로고
    • Poly(l-lysine)-GRGDS as a biomimetic surface modifier for poly(lactic acid)
    • Quirk R.A., Chan W.C., Davies M.C., Tendler S.J.B., Shakesheff K.M. Poly(l-lysine)-GRGDS as a biomimetic surface modifier for poly(lactic acid). Biomaterials 2001, 22:865-872. 10.1016/S0142-9612(00)00250-7.
    • (2001) Biomaterials , vol.22 , pp. 865-872
    • Quirk, R.A.1    Chan, W.C.2    Davies, M.C.3    Tendler, S.J.B.4    Shakesheff, K.M.5
  • 80
    • 0035205503 scopus 로고    scopus 로고
    • Human osteoprogenitor growth and differentiation on synthetic biodegradable structures after surface modification
    • Yang X.B., Roach H.I., Clarke N.M.P., Howdle S.M., Quirk R., Shakesheff K.M., et al. Human osteoprogenitor growth and differentiation on synthetic biodegradable structures after surface modification. Bone 2001, 29:523-531. 10.1016/S8756-3282(01)00617-2.
    • (2001) Bone , vol.29 , pp. 523-531
    • Yang, X.B.1    Roach, H.I.2    Clarke, N.M.P.3    Howdle, S.M.4    Quirk, R.5    Shakesheff, K.M.6
  • 81
    • 36248974279 scopus 로고    scopus 로고
    • Rapid evaluation and screening of interfacial reactions on self-assembled monolayers
    • Li J., Thiara P.S., Mrksich M. Rapid evaluation and screening of interfacial reactions on self-assembled monolayers. Langmuir 2007, 23:11826-11835. 10.1021/la701638d.
    • (2007) Langmuir , vol.23 , pp. 11826-11835
    • Li, J.1    Thiara, P.S.2    Mrksich, M.3
  • 82
    • 34247131744 scopus 로고    scopus 로고
    • Effect of wettability and surface functional groups on protein adsorption and cell adhesion using well-defined mixed self-assembled monolayers
    • Arima Y., Iwata H. Effect of wettability and surface functional groups on protein adsorption and cell adhesion using well-defined mixed self-assembled monolayers. Biomaterials 2007, 28:3074-3082. 10.1016/j.biomaterials.2007.03.013.
    • (2007) Biomaterials , vol.28 , pp. 3074-3082
    • Arima, Y.1    Iwata, H.2
  • 83
    • 70449732251 scopus 로고    scopus 로고
    • Human mesenchymal stem cell differentiation on self-assembled monolayers presenting different surface chemistries
    • Phillips J.E., Petrie T.A., Creighton F.P., García A.J. Human mesenchymal stem cell differentiation on self-assembled monolayers presenting different surface chemistries. Acta Biomater 2010, 6:12-20. 10.1016/j.actbio.2009.07.023.
    • (2010) Acta Biomater , vol.6 , pp. 12-20
    • Phillips, J.E.1    Petrie, T.A.2    Creighton, F.P.3    García, A.J.4


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