메뉴 건너뛰기




Volumn 67, Issue 2, 2003, Pages 421-430

Modification of Ti6Al4V surfaces using collagen I, III, and fibronectin. I. Biochemical and morphological characteristics of the adsorbed matrix

Author keywords

Collagen type I and III; Fibronectin; Heterotypic fibrils; Titanium

Indexed keywords

ADSORPTION; BONE; COLLAGEN; CYTOLOGY; IMPLANTS (SURGICAL); IONIC STRENGTH; MORPHOLOGY; TITANIUM;

EID: 0348014816     PISSN: 00219304     EISSN: None     Source Type: Journal    
DOI: 10.1002/jbm.a.10080     Document Type: Article
Times cited : (48)

References (33)
  • 3
    • 0005204018 scopus 로고    scopus 로고
    • Immobilization of type I collagen on the alloy Ti6Al4V
    • Rõßler S, Scharnweber D, Worch H. Immobilization of type I collagen on the alloy Ti6Al4V. J Mater Sci Lett 1999;18:577-579.
    • (1999) J Mater Sci Lett , vol.18 , pp. 577-579
    • Rõßler, S.1    Scharnweber, D.2    Worch, H.3
  • 5
    • 0023747519 scopus 로고
    • Cell attachment of human gingival fibroblasts in vitro to porous-surfaced titanium alloy discs coated with collagen and platelet-derived growth factor
    • Lowenberg BF, Pilliar RM, Aubin JE, Sodek J, Melcher AH. Cell attachment of human gingival fibroblasts in vitro to porous-surfaced titanium alloy discs coated with collagen and platelet-derived growth factor. Biomaterials 1988;9(4):302-309.
    • (1988) Biomaterials , vol.9 , Issue.4 , pp. 302-309
    • Lowenberg, B.F.1    Pilliar, R.M.2    Aubin, J.E.3    Sodek, J.4    Melcher, A.H.5
  • 6
    • 0026673475 scopus 로고
    • Collagen types: Molecular structure and tissue distribution
    • Burgeson RE, Nimrd ME. Collagen types: molecular structure and tissue distribution. Clin Orthop Rel Res 1992;282:250-272.
    • (1992) Clin Orthop Rel Res , vol.282 , pp. 250-272
    • Burgeson, R.E.1    Nimrd, M.E.2
  • 7
    • 0021702404 scopus 로고
    • Collagen fibrillogenesis in vitro: Comparison of types I, II and III
    • Birk DE, Silver FH. Collagen fibrillogenesis in vitro: comparison of types I, II and III. Arch Biochem Biophys 1984;235(1): 178-185.
    • (1984) Arch Biochem Biophys , vol.235 , Issue.1 , pp. 178-185
    • Birk, D.E.1    Silver, F.H.2
  • 10
    • 0027230170 scopus 로고
    • Regulation of development and differentiation by the extracellular matrix
    • Adams JC, Watt F. Regulation of development and differentiation by the extracellular matrix. Development 1993;117:1183-1198.
    • (1993) Development , vol.117 , pp. 1183-1198
    • Adams, J.C.1    Watt, F.2
  • 11
    • 0025324305 scopus 로고
    • Collagens synthesized by healing fractures
    • Ashurst DE. Collagens synthesized by healing fractures. Clin Orthopaed Rel Res 1990;255:273-283.
    • (1990) Clin Orthopaed Rel Res , vol.255 , pp. 273-283
    • Ashurst, D.E.1
  • 12
    • 0026666122 scopus 로고
    • Types I and III procollagen extension peptides in serum respond to fracture in humans
    • Joerring S, Jensen LT, Andersen GR, Johansen JS. Types I and III procollagen extension peptides in serum respond to fracture in humans. Arch Orthop Trauma Surg 1992;111:265-267.
    • (1992) Arch Orthop Trauma Surg , vol.111 , pp. 265-267
    • Joerring, S.1    Jensen, L.T.2    Andersen, G.R.3    Johansen, J.S.4
  • 13
    • 0027134791 scopus 로고
    • Regulation of extracellular matrix genes during fracture healing in mice
    • Hiltunen A, Hannu TA, Vuorio E. Regulation of extracellular matrix genes during fracture healing in mice. Clin Orthop Rel Res 1993;297:23-27.
    • (1993) Clin Orthop Rel Res , vol.297 , pp. 23-27
    • Hiltunen, A.1    Hannu, T.A.2    Vuorio, E.3
  • 14
    • 0031990735 scopus 로고    scopus 로고
    • Serology of collagens type I and III in normal healing of tibial shaft fractures
    • Kurdy NMG, Bowles S, Marsh DR, Davies A, France M. Serology of collagens type I and III in normal healing of tibial shaft fractures. J Orthop Trauma 1998;12(2):122-126.
    • (1998) J Orthop Trauma , vol.12 , Issue.2 , pp. 122-126
    • Kurdy, N.M.G.1    Bowles, S.2    Marsh, D.R.3    Davies, A.4    France, M.5
  • 15
    • 0004043397 scopus 로고
    • New York: Springer-Verlag
    • Hynes RO. Fibronectins. New York: Springer-Verlag; 1989.
    • (1989) Fibronectins
    • Hynes, R.O.1
  • 17
    • 0023367927 scopus 로고
    • Fibronectin: A brief overview of its structure, function and physiology
    • Proctor RA. Fibronectin: a brief overview of its structure, function and physiology. Rev Infect Dis 1987;9(Suppl 4):S317-S321.
    • (1987) Rev Infect Dis , vol.9 , Issue.SUPPL. 4
    • Proctor, R.A.1
  • 19
    • 0035104786 scopus 로고    scopus 로고
    • Synergistic effect of titanium alloy and collagen type I on cell adhesion, proliferation and differentiation of osteoblast-like cells
    • Roehlecke C, Witt M, Kasper M, Schulze E, Wolf C, Hofer A, Funk RHW. Synergistic effect of titanium alloy and collagen type I on cell adhesion, proliferation and differentiation of osteoblast-like cells. Cells Tiss Org 2000;168:178-187.
    • (2000) Cells Tiss Org , vol.168 , pp. 178-187
    • Roehlecke, C.1    Witt, M.2    Kasper, M.3    Schulze, E.4    Wolf, C.5    Hofer, A.6    Funk, R.H.W.7
  • 20
    • 0027374791 scopus 로고
    • In vitro formation and aggregation of heterotypic collagen I and III fibrils
    • Notbohm H, Mosler S, Müller PK, Brinkmann J. In vitro formation and aggregation of heterotypic collagen I and III fibrils. Int J Biol Macromol 1993;15(5):299-304.
    • (1993) Int J Biol Macromol , vol.15 , Issue.5 , pp. 299-304
    • Notbohm, H.1    Mosler, S.2    Müller, P.K.3    Brinkmann, J.4
  • 21
    • 0028026619 scopus 로고
    • The in vitro interaction of proteoglycans with type I collagen is modulated by phosphate
    • Pogany G, Hernandez DJ, Vogel KG. The in vitro interaction of proteoglycans with type I collagen is modulated by phosphate. Arch Biochem Biophys 1994;313(1):102-111.
    • (1994) Arch Biochem Biophys , vol.313 , Issue.1 , pp. 102-111
    • Pogany, G.1    Hernandez, D.J.2    Vogel, K.G.3
  • 22
    • 0033579423 scopus 로고    scopus 로고
    • Does the triple helical domain of type I collagen encode molecular recognition and fiber assembly while telopeptides serve as catalytic domains?
    • Kuznetsova N, Leikins S. Does the triple helical domain of type I collagen encode molecular recognition and fiber assembly while telopeptides serve as catalytic domains? J Biol Chem 1999;274:36083-36088.
    • (1999) J Biol Chem , vol.274 , pp. 36083-36088
    • Kuznetsova, N.1    Leikins, S.2
  • 23
    • 0003005891 scopus 로고
    • Fundamentals of interstitial collagen self-assembly
    • Yurchenco P, Birk DE, Mecham RP, editors. New York: Academic Press
    • Veis A, George A. Fundamentals of interstitial collagen self-assembly. In: Yurchenco P, Birk DE, Mecham RP, editors. Extracellular matrix assembly and structure. New York: Academic Press; 1994. p 15-45.
    • (1994) Extracellular Matrix Assembly and Structure , pp. 15-45
    • Veis, A.1    George, A.2
  • 24
    • 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, Gaill F, Aumailley M. Interactions of human skin fibroblasts with monomeric or fibrillar collagens induce different organization of the cytoskeleton. Exp Cell Res 1996;225:245-256.
    • (1996) Exp Cell Res , vol.225 , pp. 245-256
    • Mercier, I.1    Lechaire, J.-P.2    Desmouliere, A.3    Gaill, F.4    Aumailley, M.5
  • 26
    • 0025111209 scopus 로고
    • Collagen type I and III occur together in hybrid fibrils in the space of Disse of normal rat liver
    • Geerts A, Schuppan D, Lazeroms S, De Zanger R, Wisse E. Collagen type I and III occur together in hybrid fibrils in the space of Disse of normal rat liver. Hepatology 1990;12(2):233-241.
    • (1990) Hepatology , vol.12 , Issue.2 , pp. 233-241
    • Geerts, A.1    Schuppan, D.2    Lazeroms, S.3    De Zanger, R.4    Wisse, E.5
  • 27
    • 0031657808 scopus 로고    scopus 로고
    • Matrix proteoglycans: From moleculare desing to cellular function
    • Iozzo RV. Matrix proteoglycans: From moleculare desing to cellular function. Annu Rev Biochem 1998;67:609-652.
    • (1998) Annu Rev Biochem , vol.67 , pp. 609-652
    • Iozzo, R.V.1
  • 28
    • 0034834329 scopus 로고    scopus 로고
    • Fibronectin, integrins and growth control
    • Danen EH, Yamada KM. Fibronectin, integrins and growth control. J Cell Physiol 2001;189(1):1-13.
    • (2001) J Cell Physiol , vol.189 , Issue.1 , pp. 1-13
    • Danen, E.H.1    Yamada, K.M.2
  • 29
    • 0019774390 scopus 로고
    • Affinity chromatography of collagen on collagen-binding fragments of fibronectin
    • Engvall E, Bell ML, Ruoshlahti E. Affinity chromatography of collagen on collagen-binding fragments of fibronectin. Coll Rel Res 1981;6:505-516.
    • (1981) Coll Rel Res , vol.6 , pp. 505-516
    • Engvall, E.1    Bell, M.L.2    Ruoshlahti, E.3
  • 30
    • 0023359316 scopus 로고
    • Influence of fibronectin on the fibrillogenesis of type I and type III collagen
    • Speranza ML, Valentini G, Calligaro A. Influence of fibronectin on the fibrillogenesis of type I and type III collagen. Coll Rel Res 1987;7:115-123.
    • (1987) Coll Rel Res , vol.7 , pp. 115-123
    • Speranza, M.L.1    Valentini, G.2    Calligaro, A.3
  • 31
    • 0027164507 scopus 로고
    • Further characterization of the binding of fibronectin to gelatin reveals the presence of different binding interactions
    • Garcia-Pardo A, Gold LI. Further characterization of the binding of fibronectin to gelatin reveals the presence of different binding interactions. Arch Biochem Biophys 1993;304(1):181-188.
    • (1993) Arch Biochem Biophys , vol.304 , Issue.1 , pp. 181-188
    • Garcia-Pardo, A.1    Gold, L.I.2
  • 32
    • 0018185067 scopus 로고
    • Affinity of fibronectin to collagens of different genetic types and to fibrinogen
    • Engvall E, Ruoslathi E, Miller EJ. Affinity of fibronectin to collagens of different genetic types and to fibrinogen. J Exp Med 1978;78:1584-1595.
    • (1978) J Exp Med , vol.78 , pp. 1584-1595
    • Engvall, E.1    Ruoslathi, E.2    Miller, E.J.3
  • 33
    • 0032935413 scopus 로고    scopus 로고
    • Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation
    • Garcia J, Vega MD, Boettiger D. Modulation of cell proliferation and differentiation through substrate-dependent changes in fibronectin conformation. Mol Biol Cell 1999;10:785-798.
    • (1999) Mol Biol Cell , vol.10 , pp. 785-798
    • Garcia, J.1    Vega, M.D.2    Boettiger, D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.