메뉴 건너뛰기




Volumn 9, Issue 10, 2010, Pages 2089-2098

Biochemical characterization of the cell-biomaterial interface by quantitative proteomics

Author keywords

[No Author keywords available]

Indexed keywords

CADHERIN; FIBRONECTIN; NUCLEOPHOSMIN; SCLEROPROTEIN; TALIN; TRANSFERRIN RECEPTOR;

EID: 77957977633     PISSN: 15359476     EISSN: 15359484     Source Type: Journal    
DOI: 10.1074/mcp.M110.001966     Document Type: Article
Times cited : (8)

References (43)
  • 2
    • 71549149979 scopus 로고    scopus 로고
    • Suppressed proliferation of mouse osteoblast-like cells by a rough-surfaced substrate leads to low differentiation and mineralization
    • Saito, T., Hayashi, H., Kameyama, T., Hishida, M., Nagai, K., Teraoka, K., and Kato, K. (2010) Suppressed proliferation of mouse osteoblast-like cells by a rough-surfaced substrate leads to low differentiation and mineralization. Materials Sci. Engineer. C 30, 1-7
    • (2010) Materials Sci. Engineer. C , vol.30 , pp. 1-7
    • Saito, T.1    Hayashi, H.2    Kameyama, T.3    Hishida, M.4    Nagai, K.5    Teraoka, K.6    Kato, K.7
  • 3
    • 0036533256 scopus 로고    scopus 로고
    • Improvement in the morphology of Ti-based surfaces: A new process to increase in vitro human osteoblast response
    • DOI 10.1016/S0142-9612(01)00271-X, PII S014296120100271X
    • Bigerelle, M., Anselme, K., NoÎl, B., Ruderman, I., Hardouin, P., and Iost, A. (2002) Improvement in the morphology of Ti-based surfaces: a new process to increase in vitro human osteoblast response. Biomaterials 23, 1563-1577 (Pubitemid 34158579)
    • (2002) Biomaterials , vol.23 , Issue.7 , pp. 1563-1577
    • Bigerelle, M.1    Anselme, K.2    Noel, B.3    Ruderman, I.4    Hardouin, P.5    Iost, A.6
  • 5
    • 57749209963 scopus 로고    scopus 로고
    • Microfeature guided skeletal muscle tissue engineering for highly organized 3-dimensional free-standing constructs
    • Lam, M. T., Huang, Y.-C., Birla, R. K., and Takayama, S. (2009) Microfeature guided skeletal muscle tissue engineering for highly organized 3-dimensional free-standing constructs. Biomaterials 30, 1150-1155
    • (2009) Biomaterials , vol.30 , pp. 1150-1155
    • Lam, M.T.1    Huang, Y.-C.2    Birla, R.K.3    Takayama, S.4
  • 6
    • 70849130059 scopus 로고    scopus 로고
    • Designing materials to direct stem-cell fate
    • Lutolf, M. P., Gilbert, P. M., and Blau, H. M. (2009) Designing materials to direct stem-cell fate. Nature 462, 433-441
    • (2009) Nature , vol.462 , pp. 433-441
    • Lutolf, M.P.1    Gilbert, P.M.2    Blau, H.M.3
  • 7
    • 34547892217 scopus 로고    scopus 로고
    • Self-assembled collagen-human mesenchymal stem cell microspheres for regenerative medicine
    • Chan, B. P., Hui, T. Y., Yeung, C. W., Li, J., Mo, I., and Chan, G. C. F. (2007) Self-assembled collagen-human mesenchymal stem cell microspheres for regenerative medicine. Biomaterials 28, 4652-4666
    • (2007) Biomaterials , vol.28 , pp. 4652-4666
    • Chan, B.P.1    Hui, T.Y.2    Yeung, C.W.3    Li, J.4    Mo, I.5    Chan, G.C.F.6
  • 8
    • 56249133490 scopus 로고    scopus 로고
    • Stem cells and biomimetic materials strategies for tissue engineering
    • Liao, S., Chan, C. K., and Ramakrishna, S. (2008) Stem cells and biomimetic materials strategies for tissue engineering. Materials Sci. Engineer. C 28, 1189-1202
    • (2008) Materials Sci. Engineer. C , vol.28 , pp. 1189-1202
    • Liao, S.1    Chan, C.K.2    Ramakrishna, S.3
  • 9
    • 42749096667 scopus 로고    scopus 로고
    • On the mechanisms of biocompatibility
    • Williams, D. F. (2008) On the mechanisms of biocompatibility. Biomaterials 29, 2941-2953
    • (2008) Biomaterials , vol.29 , pp. 2941-2953
    • Williams, D.F.1
  • 10
    • 69249206554 scopus 로고    scopus 로고
    • On the nature of biomaterials
    • Williams, D. F. (2009) On the nature of biomaterials. Biomaterials 30, 5897-5909
    • (2009) Biomaterials , vol.30 , pp. 5897-5909
    • Williams, D.F.1
  • 11
    • 45249093434 scopus 로고    scopus 로고
    • Tensegrity-based mechanosensing from macro to micro
    • Ingber, D. E. Tensegrity-based mechanosensing from macro to micro. Prog. Biophysics Mol. Biol. 97, 163-179
    • Prog. Biophysics Mol. Biol. , vol.97 , pp. 163-179
    • Ingber, D.E.1
  • 12
    • 33846281120 scopus 로고    scopus 로고
    • Cellular tensegrity models and cell-substrate interactions
    • King, M. R. (ed). Burlington, MA: Academic Press
    • Stamenovic, D., Wang, N., Ingber, D. E., and Michael, R. K. Cellular tensegrity models and cell-substrate interactions. In: King, M. R. (ed). Principles of Cellular Engineering. Burlington, MA: Academic Press; 2006: 81-101
    • (2006) Principles of Cellular Engineering , pp. 81-101
    • Stamenovic, D.1    Wang, N.2    Ingber, D.E.3    Michael, R.K.4
  • 14
    • 33644524918 scopus 로고    scopus 로고
    • Mass spectrometry-based proteomics turns quantitative
    • Ong, S. E., and Mann, M. (2005) Mass spectrometry-based proteomics turns quantitative. Nat. Chem. Biol. 1, 252-262
    • (2005) Nat. Chem. Biol. , vol.1 , pp. 252-262
    • Ong, S.E.1    Mann, M.2
  • 15
    • 34247391127 scopus 로고    scopus 로고
    • Analysis of Nucleolar Protein Dynamics Reveals the Nuclear Degradation of Ribosomal Proteins
    • DOI 10.1016/j.cub.2007.03.064, PII S096098220701202X
    • Lam, Y. W., Lamond, A. I., Mann, M., and Andersen, J. S. (2007) Analysis of nucleolar protein dynamics reveals the nuclear degradation of ribosomal proteins. Curr. Biol. 17, 749-760 (Pubitemid 46635118)
    • (2007) Current Biology , vol.17 , Issue.9 , pp. 749-760
    • Lam, Y.W.1    Lamond, A.I.2    Mann, M.3    Andersen, J.S.4
  • 18
    • 70549103107 scopus 로고    scopus 로고
    • Quantitative proteomics: A tool to assess cell differentiation
    • Vermeulen, M., and Selbach, M. (2009) Quantitative proteomics: a tool to assess cell differentiation. Curr. Opin. Cell Biol. 21, 761-766
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 761-766
    • Vermeulen, M.1    Selbach, M.2
  • 19
    • 64549132104 scopus 로고    scopus 로고
    • Differential in-gel electrophoresis (DIGE) analysis of human bone marrow osteoprogenitor cell contact guidance
    • Kantawong, F., Burchmore, R., Wilkinson, C. D. W., Oreffo, R. O. C., and Dalby, M. J. (2009) Differential in-gel electrophoresis (DIGE) analysis of human bone marrow osteoprogenitor cell contact guidance. Acta Biomaterialia 5, 1137-1146
    • (2009) Acta Biomaterialia , vol.5 , pp. 1137-1146
    • Kantawong, F.1    Burchmore, R.2    Wilkinson, C.D.W.3    Oreffo, R.O.C.4    Dalby, M.J.5
  • 20
    • 68549109358 scopus 로고    scopus 로고
    • Protein expression profiles in osteoblasts in response to differentially shaped hydroxyapatite nanoparticles
    • Xu, J. L., Khor, K. A., Sui, J. J., Zhang, J. H., and Chen, W. N. (2009) Protein expression profiles in osteoblasts in response to differentially shaped hydroxyapatite nanoparticles. Biomaterials 30, 5385-5391
    • (2009) Biomaterials , vol.30 , pp. 5385-5391
    • Xu, J.L.1    Khor, K.A.2    Sui, J.J.3    Zhang, J.H.4    Chen, W.N.5
  • 21
    • 0036583926 scopus 로고    scopus 로고
    • Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics
    • Ong Se, Blagoev, B., Kratchmarova, I., Kristensen, D. B., Steen, H., Pandey, A., Pandey A., and Mann, M. (2002) Stable isotope labeling by amino acids in cell culture, SILAC, as a simple and accurate approach to expression proteomics. Mol. Cell. Proteomics 1, 376-386
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 376-386
    • Ong, Se.1    Blagoev, B.2    Kratchmarova, I.3    Kristensen, D.B.4    Steen, H.5    Pandey, A.6    Pandey, A.7    Mann, M.8
  • 22
    • 0024933611 scopus 로고
    • Strategy and tactics in electron microscopy of cell surfaces
    • Nermut, M. V. (1989) Strategy and tactics in electron microscopy of cell surfaces. Electron. Microsc. Rev. 2, 171-196
    • (1989) Electron. Microsc. Rev. , vol.2 , pp. 171-196
    • Nermut, M.V.1
  • 23
    • 0027525927 scopus 로고
    • Focal-adhesion components are enriched in ventral membranes isolated from transformed keratinocytes in culture
    • Gates, R. E., Hanks, S. K., and King, L. E., Jr. (1993) Focal-adhesion components are enriched in ventral membranes isolated from transformed keratinocytes in culture. Biochem. J. 289 (Pt 1), 221-226
    • (1993) Biochem. J. , vol.289 , Issue.PART 1 , pp. 221-226
    • Gates, R.E.1    Hanks, S.K.2    King Jr., L.E.3
  • 24
    • 34548178909 scopus 로고    scopus 로고
    • In-gel digestion for mass spectrometric characterization of proteins and proteomes
    • Shevchenko, A., Tomas, H., Havlis, J., Olsen, J. V., and Mann, M. (2006) In-gel digestion for mass spectrometric characterization of proteins and proteomes. Nat. Protoc. 1, 2856-2860
    • (2006) Nat. Protoc. , vol.1 , pp. 2856-2860
    • Shevchenko, A.1    Tomas, H.2    Havlis, J.3    Olsen, J.V.4    Mann, M.5
  • 25
    • 45649083365 scopus 로고    scopus 로고
    • Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study
    • Bindschedler, L. V., Palmblad, M., and Cramer, R. (2008) Hydroponic isotope labelling of entire plants (HILEP) for quantitative plant proteomics; an oxidative stress case study. Phytochemistry 69, 1962-1972
    • (2008) Phytochemistry , vol.69 , pp. 1962-1972
    • Bindschedler, L.V.1    Palmblad, M.2    Cramer, R.3
  • 26
    • 23944477893 scopus 로고    scopus 로고
    • Large scale analysis of MASCOT results using a mass accuracy-based threshold (MATH) effectively improves data interpretation
    • Rudnick, P. A., Wang, Y., Evans, E., Lee, C. S., and Balgley, B. M. (2005) Large scale analysis of MASCOT results using a mass accuracy-based threshold (MATH) effectively improves data interpretation. J. Proteome Res. 4, 1353-1360
    • (2005) J. Proteome Res. , vol.4 , pp. 1353-1360
    • Rudnick, P.A.1    Wang, Y.2    Evans, E.3    Lee, C.S.4    Balgley, B.M.5
  • 27
    • 0025943932 scopus 로고
    • Organization of talin and vinculin in adhesion plaques of wet-cleaved chicken embryo fibroblasts
    • Feltkamp, C. A., Pijnenburg, M. A., and Roos, E. (1991) Organization of talin and vinculin in adhesion plaques of wet-cleaved chicken embryo fibroblasts. J. Cell Sci. 100 (Pt 3), 579-587
    • (1991) J. Cell Sci. , vol.100 , Issue.PART 3 , pp. 579-587
    • Feltkamp, C.A.1    Pijnenburg, M.A.2    Roos, E.3
  • 28
    • 21644472900 scopus 로고    scopus 로고
    • Cell-adhesion assays: Fabrication of an E-cadherin substratum and isolation of lateral and Basal membrane patches
    • Drees, F., Reilein, A., and Nelson, W. J. (2005) Cell-adhesion assays: fabrication of an E-cadherin substratum and isolation of lateral and Basal membrane patches. Methods Mol. Biol. 294, 303-320
    • (2005) Methods Mol. Biol. , vol.294 , pp. 303-320
    • Drees, F.1    Reilein, A.2    Nelson, W.J.3
  • 29
    • 0021112527 scopus 로고
    • Coating cells with colloidal silica for high yield isolation of plasma membrane sheets and identification of transmembrane proteins
    • Chaney, L. K., and Jacobson, B. S. (1983) Coating cells with colloidal silica for high yield isolation of plasma membrane sheets and identification of transmembrane proteins. J. Biol. Chem. 258, 10062-10072
    • (1983) J. Biol. Chem. , vol.258 , pp. 10062-10072
    • Chaney, L.K.1    Jacobson, B.S.2
  • 30
    • 62449194097 scopus 로고    scopus 로고
    • Purification of basolateral integral membrane proteins by cationic colloidal silica-based apical membrane subtraction
    • Goode, R. J., and Simpson, R. J. (2009) Purification of basolateral integral membrane proteins by cationic colloidal silica-based apical membrane subtraction. Methods Mol. Biol. 528, 177-187
    • (2009) Methods Mol. Biol. , vol.528 , pp. 177-187
    • Goode, R.J.1    Simpson, R.J.2
  • 31
    • 0019731246 scopus 로고
    • Ultrastructure of sheep erythrocyte plasma membranes and cytoskeletons bound to solid supports
    • Lang, R. D., Nermut, M. V., and Williams, L. D. (1981) Ultrastructure of sheep erythrocyte plasma membranes and cytoskeletons bound to solid supports. J. Cell Sci. 49, 383-399
    • (1981) J. Cell Sci. , vol.49 , pp. 383-399
    • Lang, R.D.1    Nermut, M.V.2    Williams, L.D.3
  • 32
    • 0023157697 scopus 로고
    • Labeling of structural elements at the ventral plasma membrane of fibroblasts with the immunogold technique
    • Nicol, A., Nermut, M. V., Doeinck, A., Robenek, H., Wiegand, C., and Jockusch, B. M. (1987) Labeling of structural elements at the ventral plasma membrane of fibroblasts with the immunogold technique. J. Histochem. Cytochem. 35, 499-506
    • (1987) J. Histochem. Cytochem. , vol.35 , pp. 499-506
    • Nicol, A.1    Nermut, M.V.2    Doeinck, A.3    Robenek, H.4    Wiegand, C.5    Jockusch, B.M.6
  • 33
    • 0032894575 scopus 로고    scopus 로고
    • A cell-free system to study regulation of focal adhesions and of the connected actin cytoskeleton
    • Cattelino, A., Albertinazzi, C., Bossi, M., Critchley, D. R., and de Curtis, I. (1999) A cell-free system to study regulation of focal adhesions and of the connected actin cytoskeleton. Mol. Biol. Cell 10, 373-391 (Pubitemid 29156479)
    • (1999) Molecular Biology of the Cell , vol.10 , Issue.2 , pp. 373-391
    • Cattelino, A.1    Albertinazzi, C.2    Bossi, M.3    Critchley, D.R.4    De Curtis, I.5
  • 34
    • 0017695990 scopus 로고
    • Membrane isolation on polylysine-coated beads. Plasma membrane from HeLa cells
    • DOI 10.1083/jcb.75.1.119
    • Cohen, C. M., Kalish, D. I., Jacobson, B. S., and Branton, D. (1977) Membrane isolation on polylysine-coated beads. Plasma membrane from HeLa cells. J. Cell Biol. 75, 119-134 (Pubitemid 8190663)
    • (1977) Journal of Cell Biology , vol.75 , Issue.1 , pp. 119-134
    • Cohen, C.M.1    Kalish, D.I.2    Jacobson, B.S.3    Branton, D.4
  • 35
    • 0017342078 scopus 로고
    • Plasma membrane: Rapid isolation and exposure of the cytoplasmic surface by use of positively charged beads
    • Jacobson, B. S., and Branton, D. (1977) Plasma membrane: rapid isolation and exposure of the cytoplasmic surface by use of positively charged beads. Science 195, 302-304
    • (1977) Science , vol.195 , pp. 302-304
    • Jacobson, B.S.1    Branton, D.2
  • 36
    • 0020462085 scopus 로고
    • Initial events during phagocytosis by macrophages viewed from outside and inside the cell: Membrane particle interactions and clathrin
    • DOI 10.1083/jcb.94.3.613
    • Aggeler, J., and Werb, Z. (1982) Initial events during phagocytosis by macrophages viewed from outside and inside the cell: membrane-particle interactions and clathrin. J. Cell Biol. 94, 613-623 (Pubitemid 13241194)
    • (1982) Journal of Cell Biology , vol.94 , Issue.3 , pp. 613-623
    • Aggeler, J.1    Werb, Z.2
  • 37
    • 0024397823 scopus 로고
    • Multiple domains of the large fibroblast proteoglycan, versican
    • Zimmermann, D. R., and Ruoslahti, E. (1989) Multiple domains of the large fibroblast proteoglycan, versican. EMBO J. 8, 2975-2981
    • (1989) EMBO J. , vol.8 , pp. 2975-2981
    • Zimmermann, D.R.1    Ruoslahti, E.2
  • 38
    • 0029037896 scopus 로고
    • The complete primary structure of human nebulin and its correlation to muscle structure
    • Labeit, S., and Kolmerer, B. (1995) The complete primary structure of human nebulin and its correlation to muscle structure. J. Mol. Biol. 248, 308-315
    • (1995) J. Mol. Biol. , vol.248 , pp. 308-315
    • Labeit, S.1    Kolmerer, B.2
  • 39
    • 0037132502 scopus 로고    scopus 로고
    • Interaction of nebulin SH3 domain with titin PEVK and myopalladin: Implications for the signaling and assembly role of titin and nebulin
    • DOI 10.1016/S0014-5793(02)03655-4, PII S0014579302036554
    • Ma, K., and Wang, K. (2002) Interaction of nebulin SH3 domain with titin PEVK and myopalladin: implications for the signaling and assembly role of titin and nebulin. FEBS Lett. 532, 273-278 (Pubitemid 35441360)
    • (2002) FEBS Letters , vol.532 , Issue.3 , pp. 273-278
    • Ma, K.1    Wang, K.2
  • 40
    • 0037418837 scopus 로고    scopus 로고
    • Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation
    • DOI 10.1016/S0092-8674(03)00163-6
    • Tu, Y., Wu, S., Shi, X., Chen, K., and Wu, C. (2003) Migfilin and Mig-2 link focal adhesions to filamin and the actin cytoskeleton and function in cell shape modulation. Cell 113, 37-47 (Pubitemid 36411958)
    • (2003) Cell , vol.113 , Issue.1 , pp. 37-47
    • Tu, Y.1    Wu, S.2    Shi, X.3    Chen, K.4    Wu, C.5
  • 41
    • 0037809280 scopus 로고    scopus 로고
    • A new member of the LIM protein family binds to filamin B and localizes at stress fibers
    • Takafuta T., Saeki, M., Fujimoto, T., Fujimura, K., and Shapiro, S. (2003) A new member of the LIM protein family binds to filamin B and localizes at stress fibers. J. Biol. Chem. 278, 12175-12181
    • (2003) J. Biol. Chem. , vol.278 , pp. 12175-12181
    • Takafuta, T.1    Saeki, M.2    Fujimoto, T.3    Fujimura, K.4    Shapiro, S.5
  • 42
    • 33751011645 scopus 로고    scopus 로고
    • Na+, K+-ATPase: An Indispensable IOCn Pumping-Signaling Mechanism Across Mammalian Cell Membranes
    • Jaitovich, A. A., and Bertorello, A. M. (2006) Na+, K+-ATPase: An Indispensable IOCn Pumping-Signaling Mechanism Across Mammalian Cell Membranes, Seminars in Nephrology 26, 386-392
    • (2006) Seminars in Nephrology , vol.26 , pp. 386-392
    • Jaitovich, A.A.1    Bertorello, A.M.2
  • 43
    • 2542477014 scopus 로고    scopus 로고
    • RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers
    • de Hoog, C. L., Foster, L. J., and Mann, M. (2004) RNA and RNA binding proteins participate in early stages of cell spreading through spreading initiation centers. Cell 117, 649-662
    • (2004) Cell , vol.117 , pp. 649-662
    • De Hoog, C.L.1    Foster, L.J.2    Mann, M.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.