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Volumn 8, Issue 1, 2013, Pages 1-12

The effect of high vacuum on the mechanical properties and bioactivity of collagen fibril matrices

Author keywords

Collagen fibrils; Colloidal probe atomic force microscopy; Extracellular matrix; Principal component analysis; Quantitative cell imaging; Secondary ion mass spectrometry

Indexed keywords

ATOMIC FORCE MICROSCOPY; COLLAGEN; MECHANICAL PROPERTIES; PRINCIPAL COMPONENT ANALYSIS; SECONDARY EMISSION; SECONDARY ION MASS SPECTROMETRY;

EID: 84929942162     PISSN: 19348630     EISSN: 15594106     Source Type: Journal    
DOI: 10.1186/1559-4106-8-2     Document Type: Article
Times cited : (4)

References (52)
  • 1
    • 0034715891 scopus 로고    scopus 로고
    • Multiple roles of integrins in cell motility
    • Holly SP, Larson MK, Parise LV (2000) Multiple roles of integrins in cell motility. Exp Cell Res 261(1):69-74
    • (2000) Exp Cell Res , vol.261 , Issue.1 , pp. 69-74
    • Holly, S.P.1    Larson, M.K.2    Parise, L.V.3
  • 2
    • 33748550344 scopus 로고    scopus 로고
    • Dynamics of assembly and reorganization of extracellular matrix proteins
    • Dallas SL, Chen Q, Sivakumar P (2006) Dynamics of assembly and reorganization of extracellular matrix proteins. Curr Top Dev Biol 75:1-24. http://www.ncbi.nlm.nih.gov/pubmed/16984808
    • (2006) Curr Top Dev Biol , vol.75 , pp. 1-24
    • Dallas, S.L.1    Chen, Q.2    Sivakumar, P.3
  • 3
    • 0035999132 scopus 로고    scopus 로고
    • The dominance of the microenvironment in breast and ovarian cancer
    • Roskelley CD, Bissell MJ (2002) The dominance of the microenvironment in breast and ovarian cancer. Semin Cancer Biol 12(2):97-104
    • (2002) Semin Cancer Biol , vol.12 , Issue.2 , pp. 97-104
    • Roskelley, C.D.1    Bissell, M.J.2
  • 4
    • 18244398668 scopus 로고    scopus 로고
    • Use of embryonic stem cellderived endothelial cells as a cell source to generate vessel structures in vitro
    • McCloskey KE, Gilroy ME, Nerem RM (2005) Use of embryonic stem cellderived endothelial cells as a cell source to generate vessel structures in vitro. Tissue Eng 11(3-4):497-505
    • (2005) Tissue Eng , vol.11 , Issue.3-4 , pp. 497-505
    • McCloskey, K.E.1    Gilroy, M.E.2    Nerem, R.M.3
  • 5
    • 0029954059 scopus 로고    scopus 로고
    • Interactions of human skin fibroblasts with monomeric or fibrillar collagens induce different organization of the cytoskeleton
    • Mercier I, Lechaire J-P, Desmouliere A, Fo G, Aumailley M (1996) Interactions of human skin fibroblasts with monomeric or fibrillar collagens induce different organization of the cytoskeleton. Exp Cell Res 225(2):245-256
    • (1996) Exp Cell Res , vol.225 , Issue.2 , pp. 245-256
    • Mercier, I.1    Lechaire, J.-P.2    Desmouliere, A.3    Fo, G.4    Aumailley, M.5
  • 6
    • 0037145037 scopus 로고    scopus 로고
    • Integrins: Bidirectional, allosteric signaling machines
    • Hynes RO (2002) Integrins: bidirectional, allosteric signaling machines. Cell 110(6):673-687
    • (2002) Cell , vol.110 , Issue.6 , pp. 673-687
    • Hynes, R.O.1
  • 7
    • 0033917881 scopus 로고    scopus 로고
    • Cell movement is guided by the rigidity of the substrate
    • Lo C-M, Wang H-B, Dembo MY-LW (2000) Cell movement is guided by the rigidity of the substrate. Biophys J 79(1):144-152
    • (2000) Biophys J , vol.79 , Issue.1 , pp. 144-152
    • Lo, C.-M.1    Wang, H.-B.2    Dembo, M.Y.-L.W.3
  • 9
    • 84860538261 scopus 로고    scopus 로고
    • Holding on to stemness
    • Lathia JD, Rich JN (2012) Holding on to stemness. Nat Cell Biol 14(5):450-452
    • (2012) Nat Cell Biol , vol.14 , Issue.5 , pp. 450-452
    • Lathia, J.D.1    Rich, J.N.2
  • 11
    • 77749319323 scopus 로고    scopus 로고
    • Nanomechanical properties of thin films of type I collagen fibrils
    • Chung K-H, Bhadriraju K, Spurlin TA, Cook RF, Plant AL (2010) Nanomechanical properties of thin films of type I collagen fibrils. Langmuir 26(5):3629-3636
    • (2010) Langmuir , vol.26 , Issue.5 , pp. 3629-3636
    • Chung, K.-H.1    Bhadriraju, K.2    Spurlin, T.A.3    Cook, R.F.4    Plant, A.L.5
  • 13
    • 56349114812 scopus 로고    scopus 로고
    • Extracellular matrix as a biological scaffold material: Structure and function
    • Badylak SF, Freytes DO, Gilbert TW (2009) Extracellular matrix as a biological scaffold material: structure and function. Acta Biomater 5(1):1-13
    • (2009) Acta Biomater , vol.5 , Issue.1 , pp. 1-13
    • Badylak, S.F.1    Freytes, D.O.2    Gilbert, T.W.3
  • 15
    • 33846359644 scopus 로고    scopus 로고
    • Comparison of native extracellular matrix with adsorbed protein films using secondary ion mass spectrometry'Ć
    • Canavan HE, Graham DJ, Cheng X, Ratner BD, Castner DG (2006) Comparison of native extracellular matrix with adsorbed protein films using secondary ion mass spectrometry'Ć. Langmuir 23(1):50-56
    • (2006) Langmuir , vol.23 , Issue.1 , pp. 50-56
    • Canavan, H.E.1    Graham, D.J.2    Cheng, X.3    Ratner, B.D.4    Castner, D.G.5
  • 17
    • 33645876484 scopus 로고    scopus 로고
    • Decellularization of tissues and organs
    • Gilbert TW, Sellaro TL, Badylak SF (2006) Decellularization of tissues and organs. Biomaterials 27(19):3675-3683
    • (2006) Biomaterials , vol.27 , Issue.19 , pp. 3675-3683
    • Gilbert, T.W.1    Sellaro, T.L.2    Badylak, S.F.3
  • 18
    • 79953302272 scopus 로고    scopus 로고
    • The impact of compositional topography of amniotic membrane scaffold on tissue morphogenesis of salivary gland
    • Hsiao Y-C, Lee H-W, Chen Y-T, Young T-H, Yang T-L (2011) The impact of compositional topography of amniotic membrane scaffold on tissue morphogenesis of salivary gland. Biomaterials 32(19):4424-4432
    • (2011) Biomaterials , vol.32 , Issue.19 , pp. 4424-4432
    • Hsiao, Y.-C.1    Lee, H.-W.2    Chen, Y.-T.3    Young, T.-H.4    Yang, T.-L.5
  • 19
    • 14844325834 scopus 로고    scopus 로고
    • Surface characterization of the extracellular matrix remaining after cell detachment from a thermoresponsive polymer
    • Canavan HE, Cheng X, Graham DJ, Ratner BD, Castner DG (2004) Surface characterization of the extracellular matrix remaining after cell detachment from a thermoresponsive polymer. Langmuir 21(5):1949-1955
    • (2004) Langmuir , vol.21 , Issue.5 , pp. 1949-1955
    • Canavan, H.E.1    Cheng, X.2    Graham, D.J.3    Ratner, B.D.4    Castner, D.G.5
  • 22
    • 77952996933 scopus 로고    scopus 로고
    • TOF-secondary Ion mass spectrometry imaging of polymeric scaffolds with surrounding tissue after in vivo implantation
    • Klerk LA, Dankers PYW, Popa ER, Bosman AW, Sanders ME, Reedquist KA, Heeren RMA (2010) TOF-secondary Ion mass spectrometry imaging of polymeric scaffolds with surrounding tissue after in vivo implantation. Anal Chem 82(11):4337-4343
    • (2010) Anal Chem , vol.82 , Issue.11 , pp. 4337-4343
    • Klerk, L.A.1    Dankers, P.Y.W.2    Popa, E.R.3    Bosman, A.W.4    Sanders, M.E.5    Reedquist, K.A.6    Heeren, R.M.A.7
  • 23
    • 77955304310 scopus 로고    scopus 로고
    • Probing the orientation of surface-immobilized protein G B1 using ToF-SIMS, sum frequency generation, and NEXAFS spectroscopy
    • Baugh L, Weidner T, Baio JE, Nguyen P-CT, Gamble LJ, Stayton PS, Castner DG (2010) Probing the orientation of surface-immobilized protein G B1 using ToF-SIMS, sum frequency generation, and NEXAFS spectroscopy. Langmuir 26(21):16434-16441
    • (2010) Langmuir , vol.26 , Issue.21 , pp. 16434-16441
    • Baugh, L.1    Weidner, T.2    Baio, J.E.3    Nguyen, P.-C.T.4    Gamble, L.J.5    Stayton, P.S.6    Castner, D.G.7
  • 24
    • 0035943196 scopus 로고    scopus 로고
    • Characterization of adsorbed protein films by time-of-flight secondary ion mass spectrometry with principal component analysis
    • Wagner MS, Castner DG (2001) Characterization of adsorbed protein films by time-of-flight secondary ion mass spectrometry with principal component analysis. Langmuir 17:4649-4660
    • (2001) Langmuir , vol.17 , pp. 4649-4660
    • Wagner, M.S.1    Castner, D.G.2
  • 25
    • 0037090357 scopus 로고    scopus 로고
    • Interpretation of static time-of-flight secondary ion mass spectra of adsorbed protein films by multivariate pattern recognition
    • Wagner MS, Tyler BJ, Castner DG (2002) Interpretation of static time-of-flight secondary ion mass spectra of adsorbed protein films by multivariate pattern recognition. Anal Chem 74:1824-1835
    • (2002) Anal Chem , vol.74 , pp. 1824-1835
    • Wagner, M.S.1    Tyler, B.J.2    Castner, D.G.3
  • 26
    • 0037076669 scopus 로고    scopus 로고
    • Time-of-flight secondary Ion mass spectrometry analysis of conformational changes in adsorbed protein films
    • Xia N, May CJ, McArthur SL, Castner DG (2002) Time-of-flight secondary Ion mass spectrometry analysis of conformational changes in adsorbed protein films. Langmuir 18(10):4090-4097
    • (2002) Langmuir , vol.18 , Issue.10 , pp. 4090-4097
    • Xia, N.1    May, C.J.2    McArthur, S.L.3    Castner, D.G.4
  • 27
    • 33748772847 scopus 로고    scopus 로고
    • Distinguishing monosaccharide stereo-and structural isomers with TOFSIMS and multivariate statistical analysis
    • Berman ESF, Kulp KS, Knize MG, Wu L, Nelson EJ, Nelson DO, Wu KJ (2006) Distinguishing monosaccharide stereo-and structural isomers with TOFSIMS and multivariate statistical analysis. Anal Chem 78(18):6497-6503
    • (2006) Anal Chem , vol.78 , Issue.18 , pp. 6497-6503
    • Berman, E.S.F.1    Kulp, K.S.2    Knize, M.G.3    Wu, L.4    Nelson, E.J.5    Nelson, D.O.6    Wu, K.J.7
  • 28
    • 84857029698 scopus 로고    scopus 로고
    • Identification of a lipid-related peak set to enhance the interpretation of TOF-SIMS data from model and cellular membranes
    • Anderton CR, Vaezian B, Lou K, Frisz JF, Kraft ML (2011) Identification of a lipid-related peak set to enhance the interpretation of TOF-SIMS data from model and cellular membranes. Surf Interface Anal 44(3):322-333
    • (2011) Surf Interface Anal , vol.44 , Issue.3 , pp. 322-333
    • Anderton, C.R.1    Vaezian, B.2    Lou, K.3    Frisz, J.F.4    Kraft, M.L.5
  • 29
    • 78650335118 scopus 로고    scopus 로고
    • Discriminating and imaging different phosphatidylcholine species within phase-separated model membranes by principal component analysis of TOF-secondary Ion mass spectrometry images
    • Vaezian B, Anderton CR, Kraft ML (2010) Discriminating and imaging different phosphatidylcholine species within phase-separated model membranes by principal component analysis of TOF-secondary Ion mass spectrometry images. Anal Chem 82(24):10006-10014
    • (2010) Anal Chem , vol.82 , Issue.24 , pp. 10006-10014
    • Vaezian, B.1    Anderton, C.R.2    Kraft, M.L.3
  • 30
    • 33744916551 scopus 로고    scopus 로고
    • Chemical and biological differentiation of three human breast cancer cell types using time-of-flight secondary Ion mass spectrometry
    • Kulp KS, Berman ESF, Knize MG, Shattuck DL, Nelson EJ, Wu L, Montgomery JL, Felton JS, Wu KJ (2006) Chemical and biological differentiation of three human breast cancer cell types using time-of-flight secondary Ion mass spectrometry. Anal Chem 78(11):3651-3658
    • (2006) Anal Chem , vol.78 , Issue.11 , pp. 3651-3658
    • Kulp, K.S.1    Berman, E.S.F.2    Knize, M.G.3    Shattuck, D.L.4    Nelson, E.J.5    Wu, L.6    Montgomery, J.L.7    Felton, J.S.8    Wu, K.J.9
  • 31
    • 0345600993 scopus 로고    scopus 로고
    • Preserving the structure of adsorbed protein films for time-of-flight secondary ion mass spectrometry analysis
    • Xia N, Castner DG (2003) Preserving the structure of adsorbed protein films for time-of-flight secondary ion mass spectrometry analysis. J Biomed Mater Res A 67A(1):179-190
    • (2003) J Biomed Mater Res A , vol.67 A , Issue.1 , pp. 179-190
    • Xia, N.1    Castner, D.G.2
  • 33
    • 68549101861 scopus 로고    scopus 로고
    • Evaluating the performance of fibrillar collagen films formed at polystyrene surfaces as cell culture substrates
    • Elliott JT, Halter M, Plant AL, Woodward JT, Langenbach KJ, Tona A (2008) Evaluating the performance of fibrillar collagen films formed at polystyrene surfaces as cell culture substrates. Biointerphases 3(2):19-28
    • (2008) Biointerphases , vol.3 , Issue.2 , pp. 19-28
    • Elliott, J.T.1    Halter, M.2    Plant, A.L.3    Woodward, J.T.4    Langenbach, K.J.5    Tona, A.6
  • 34
    • 0344088272 scopus 로고    scopus 로고
    • Thin films of collagen affect smooth muscle cell morphology
    • Elliott JT, Tona A, Woodward JT, Jones PL, Plant AL (2003) Thin films of collagen affect smooth muscle cell morphology. Langmuir 19(5):1506-1514
    • (2003) Langmuir , vol.19 , Issue.5 , pp. 1506-1514
    • Elliott, J.T.1    Tona, A.2    Woodward, J.T.3    Jones, P.L.4    Plant, A.L.5
  • 35
    • 13944265302 scopus 로고    scopus 로고
    • Basic mechanism of three-dimensional collagen fibre transport by fibroblasts
    • Meshel AS, Wei Q, Adelstein RS, Sheetz MP (2005) Basic mechanism of three-dimensional collagen fibre transport by fibroblasts. Nat Cell Biol 7(2):157-164
    • (2005) Nat Cell Biol , vol.7 , Issue.2 , pp. 157-164
    • Meshel, A.S.1    Wei, Q.2    Adelstein, R.S.3    Sheetz, M.P.4
  • 36
    • 70349859994 scopus 로고    scopus 로고
    • The relative roles of collagen adhesive receptor DDR2 activation and matrix stiffness on the downregulation of focal adhesion kinase in vascular smooth muscle cells
    • Bhadriraju K, Chung K-H, Spurlin TA, Haynes RJ, Elliott JT, Plant AL (2009) The relative roles of collagen adhesive receptor DDR2 activation and matrix stiffness on the downregulation of focal adhesion kinase in vascular smooth muscle cells. Biomaterials 30(35):6687-6694
    • (2009) Biomaterials , vol.30 , Issue.35 , pp. 6687-6694
    • Bhadriraju, K.1    Chung, K.-H.2    Spurlin, T.A.3    Haynes, R.J.4    Elliott, J.T.5    Plant, A.L.6
  • 37
    • 68549094202 scopus 로고    scopus 로고
    • The treatment of collagen fibrils by tissue transglutaminase to promote vascular smooth muscle cell contractile signaling
    • Spurlin TA, Bhadriraju K, Chung K-H, Tona A, Plant AL (2009) The treatment of collagen fibrils by tissue transglutaminase to promote vascular smooth muscle cell contractile signaling. Biomaterials 30(29):5486-5496
    • (2009) Biomaterials , vol.30 , Issue.29 , pp. 5486-5496
    • Spurlin, T.A.1    Bhadriraju, K.2    Chung, K.-H.3    Tona, A.4    Plant, A.L.5
  • 38
    • 0037040286 scopus 로고    scopus 로고
    • Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen
    • Di Lullo GA, Sweeney SM, Korkko J, Ala-Kokko L, San Antonio JD (2002) Mapping the ligand-binding sites and disease-associated mutations on the most abundant protein in the human, type I collagen. J Biol Chem 277(6):4223-4231
    • (2002) J Biol Chem , vol.277 , Issue.6 , pp. 4223-4231
    • Di Lullo, G.A.1    Sweeney, S.M.2    Korkko, J.3    Ala-Kokko, L.4    San Antonio, J.D.5
  • 39
    • 0004289209 scopus 로고
    • CRC, Boca Raton, FL
    • Nimni ME (1988) Collagen. CRC, Boca Raton, FL. http://www.amazon.com/ Collagen-Biochemistry-Vol-Marcel-Nimni/dp/0849346010
    • (1988) Collagen
    • Nimni, M.E.1
  • 41
    • 33746624303 scopus 로고    scopus 로고
    • Thin films of type 1 collagen for cell by cell analysis of morphology and tenascin-C promoter activity
    • Langenbach K, Elliott J, Tona A, McDaniel D, Plant A (2006) Thin films of type 1 collagen for cell by cell analysis of morphology and tenascin-C promoter activity. BMC Biotechnol 6(1):14
    • (2006) BMC Biotechnol , vol.6 , Issue.1 , pp. 14
    • Langenbach, K.1    Elliott, J.2    Tona, A.3    McDaniel, D.4    Plant, A.5
  • 42
    • 0347505006 scopus 로고    scopus 로고
    • Comparison of reagents for shape analysis of fixed cells by automated fluorescence microscopy
    • Elliott JT, Tona A, Plant AL (2003) Comparison of reagents for shape analysis of fixed cells by automated fluorescence microscopy. Cytometry A 52A (2):90-100
    • (2003) Cytometry A , vol.52 A , Issue.2 , pp. 90-100
    • Elliott, J.T.1    Tona, A.2    Plant, A.L.3
  • 43
    • 12044257837 scopus 로고
    • Direct measurement of colloidal forces using an atomic force microscope
    • Ducker WA, Senden TJ, Pashley RM (1991) Direct measurement of colloidal forces using an atomic force microscope. Nature 353(6341):239-241
    • (1991) Nature , vol.353 , Issue.6341 , pp. 239-241
    • Ducker, W.A.1    Senden, T.J.2    Pashley, R.M.3
  • 45
    • 45949123735 scopus 로고
    • Principal component analysis
    • Wold S (1987) Principal component analysis. Chemom Intell Lab Syst 2:37-52
    • (1987) Chemom Intell Lab Syst , vol.2 , pp. 37-52
    • Wold, S.1
  • 46
    • 1842581540 scopus 로고    scopus 로고
    • Poly-dimethyl-siloxame (PDMS) contamination of polystyrene (PS) oligomers samples: A comparison of time-of-flight static secondary ion mass spectrometry (TOF-SSIMS) and X-ray photoelectron spectroscopy (XPS) results
    • Oran U, Unveren E, Wirth T, Unger WES (2004) Poly-dimethyl-siloxame (PDMS) contamination of polystyrene (PS) oligomers samples: a comparison of time-of-flight static secondary ion mass spectrometry (TOF-SSIMS) and X-ray photoelectron spectroscopy (XPS) results. Appl Sur Sci 227:318-324
    • (2004) Appl Sur Sci , vol.227 , pp. 318-324
    • Oran, U.1    Unveren, E.2    Wirth, T.3    Unger, W.E.S.4
  • 47
    • 0028518897 scopus 로고
    • Injectable collagen as a pH-sensitive hydrogel
    • Rosenblatt J, Devereux B, Wallace DG (1994) Injectable collagen as a pH-sensitive hydrogel. Biomaterials 15(12):985-995
    • (1994) Biomaterials , vol.15 , Issue.12 , pp. 985-995
    • Rosenblatt, J.1    Devereux, B.2    Wallace, D.G.3
  • 48
    • 79951640923 scopus 로고    scopus 로고
    • Compositional mapping of the surface and interior of mammalian cells at submicrometer resolution
    • Szakal C, Narayan K, Fu J, Lefman J, Subramaniam S (2011) Compositional mapping of the surface and interior of mammalian cells at submicrometer resolution. Anal Chem 83(4):1207-1213
    • (2011) Anal Chem , vol.83 , Issue.4 , pp. 1207-1213
    • Szakal, C.1    Narayan, K.2    Fu, J.3    Lefman, J.4    Subramaniam, S.5
  • 49
    • 77956439984 scopus 로고    scopus 로고
    • Directed self-assembly at the 10 nm scale by using capillary force-induced nanocohesion
    • Duan H, Berggren KK (2010) Directed self-assembly at the 10 nm scale by using capillary force-induced nanocohesion. Nano Lett 10(9):3710-3716
    • (2010) Nano Lett , vol.10 , Issue.9 , pp. 3710-3716
    • Duan, H.1    Berggren, K.K.2
  • 51
    • 52749086091 scopus 로고    scopus 로고
    • Challenges of biological sample preparation for SIMS imaging of elements and molecules at subcellular resolution
    • Chandra S (2008) Challenges of biological sample preparation for SIMS imaging of elements and molecules at subcellular resolution. Appl Surf Sci 255(4):1273-1284
    • (2008) Appl Surf Sci , vol.255 , Issue.4 , pp. 1273-1284
    • Chandra, S.1
  • 52
    • 2942562361 scopus 로고    scopus 로고
    • Enhancing and automating TOF-SIMS data interpretation using principal component analysis
    • Pachuta SJ (2004) Enhancing and automating TOF-SIMS data interpretation using principal component analysis. Appl Sur Sci 231-232:217-223
    • (2004) Appl Sur Sci , vol.231-232 , pp. 217-223
    • Pachuta, S.J.1


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