메뉴 건너뛰기




Volumn 6, Issue 4, 2010, Pages 1649-1660

Effects of micrometric titanium particles on osteoblast attachment and cytoskeleton architecture

Author keywords

Cell adhesion; Confocal microscopy; Microparticles; Osteoblasts; Titanium

Indexed keywords

AMINO ACIDS; BIOCOMPATIBILITY; BIOMECHANICS; BONE; ENZYMES; MACHINERY; OSTEOBLASTS; PHOSPHORYLATION; TITANIUM ALLOYS;

EID: 76949102594     PISSN: 17427061     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.actbio.2009.10.033     Document Type: Article
Times cited : (56)

References (49)
  • 1
    • 0026641070 scopus 로고
    • Titanium wear debris in failed cemented total hip arthroplasty: an analysis of 71 cases
    • Buly R.L., Huo M.H., Salvati E.A., Brien W., and Bansal M. Titanium wear debris in failed cemented total hip arthroplasty: an analysis of 71 cases. J Arthroplasty 7 (1992) 315-323
    • (1992) J Arthroplasty , vol.7 , pp. 315-323
    • Buly, R.L.1    Huo, M.H.2    Salvati, E.A.3    Brien, W.4    Bansal, M.5
  • 3
    • 33947262218 scopus 로고    scopus 로고
    • Mechanisms of disease: molecular insights into aseptic loosening of orthopedic implants
    • Drees P., Eckardt A., Gay R.E., Gay S., and Huber L.C. Mechanisms of disease: molecular insights into aseptic loosening of orthopedic implants. Nat Clin Pract Rheumatol 3 (2007) 165-171
    • (2007) Nat Clin Pract Rheumatol , vol.3 , pp. 165-171
    • Drees, P.1    Eckardt, A.2    Gay, R.E.3    Gay, S.4    Huber, L.C.5
  • 5
    • 2942752227 scopus 로고    scopus 로고
    • Integrins as linker proteins between osteoblasts and bone replacing materials. A critical review
    • Siebers M.C., ter Brugge P.J., Walboomers X.F., and Jansen J.A. Integrins as linker proteins between osteoblasts and bone replacing materials. A critical review. Biomaterials 26 (2005) 137-146
    • (2005) Biomaterials , vol.26 , pp. 137-146
    • Siebers, M.C.1    ter Brugge, P.J.2    Walboomers, X.F.3    Jansen, J.A.4
  • 7
    • 0037509990 scopus 로고    scopus 로고
    • Focal adhesion kinase: the first ten years
    • Parsons J.T. Focal adhesion kinase: the first ten years. J Cell Sci 116 (2003) 1409-1416
    • (2003) J Cell Sci , vol.116 , pp. 1409-1416
    • Parsons, J.T.1
  • 8
    • 11244258882 scopus 로고    scopus 로고
    • Focal adhesion kinase: in command and control of cell motility
    • Mitra S.K., Hanson D.A., and Schlaepfer D.D. Focal adhesion kinase: in command and control of cell motility. Nat Rev Mol Cell Biol 6 (2005) 56-68
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 56-68
    • Mitra, S.K.1    Hanson, D.A.2    Schlaepfer, D.D.3
  • 10
    • 0842331443 scopus 로고    scopus 로고
    • Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling
    • Palazzo A.F., Eng C.H., Schlaepfer D.D., Marcantonio E.E., and Gundersen G.G. Localized stabilization of microtubules by integrin- and FAK-facilitated Rho signaling. Science 303 (2004) 836-839
    • (2004) Science , vol.303 , pp. 836-839
    • Palazzo, A.F.1    Eng, C.H.2    Schlaepfer, D.D.3    Marcantonio, E.E.4    Gundersen, G.G.5
  • 11
    • 0033666291 scopus 로고    scopus 로고
    • Paxillin and focal adhesion signalling
    • Turner C.E. Paxillin and focal adhesion signalling. Nat Cell Biol 2 (2000) 231-236
    • (2000) Nat Cell Biol , vol.2 , pp. 231-236
    • Turner, C.E.1
  • 12
    • 0036205320 scopus 로고    scopus 로고
    • SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading
    • Cary L.A., Klinghoffer R.A., Sachsenmaier C., and Cooper J.A. SRC catalytic but not scaffolding function is needed for integrin-regulated tyrosine phosphorylation, cell migration, and cell spreading. Mol Cell Biol 22 (2002) 2427-2440
    • (2002) Mol Cell Biol , vol.22 , pp. 2427-2440
    • Cary, L.A.1    Klinghoffer, R.A.2    Sachsenmaier, C.3    Cooper, J.A.4
  • 14
    • 34249851423 scopus 로고    scopus 로고
    • Focal adhesion kinase is negatively regulated by phosphorylation at tyrosine 407
    • Lim Y., Park H., Jeon J., Han I., Kim J., Jho E.H., et al. Focal adhesion kinase is negatively regulated by phosphorylation at tyrosine 407. J Biol Chem 282 (2007) 10398-10404
    • (2007) J Biol Chem , vol.282 , pp. 10398-10404
    • Lim, Y.1    Park, H.2    Jeon, J.3    Han, I.4    Kim, J.5    Jho, E.H.6
  • 15
    • 0029154733 scopus 로고
    • Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions
    • Lev S., Moreno H., Martinez R., Canoll P., Peles E., Musacchio J.M., et al. Protein tyrosine kinase PYK2 involved in Ca(2+)-induced regulation of ion channel and MAP kinase functions. Nature 376 (1995) 737-745
    • (1995) Nature , vol.376 , pp. 737-745
    • Lev, S.1    Moreno, H.2    Martinez, R.3    Canoll, P.4    Peles, E.5    Musacchio, J.M.6
  • 16
    • 0029770721 scopus 로고    scopus 로고
    • Activation of Pyk2 by stress signals and coupling with JNK signaling pathway
    • Tokiwa G., Dikic I., Lev S., and Schlessinger J. Activation of Pyk2 by stress signals and coupling with JNK signaling pathway. Science 273 (1996) 792-794
    • (1996) Science , vol.273 , pp. 792-794
    • Tokiwa, G.1    Dikic, I.2    Lev, S.3    Schlessinger, J.4
  • 17
    • 0032531732 scopus 로고    scopus 로고
    • Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK- cell migration
    • Sieg D.J., Ilić D., Jones K.C., Damsky C.H., Hunter T., and Schlaepfer D.D. Pyk2 and Src-family protein-tyrosine kinases compensate for the loss of FAK in fibronectin-stimulated signaling events but Pyk2 does not fully function to enhance FAK- cell migration. EMBO J 17 (1998) 5933-5947
    • (1998) EMBO J , vol.17 , pp. 5933-5947
    • Sieg, D.J.1    Ilić, D.2    Jones, K.C.3    Damsky, C.H.4    Hunter, T.5    Schlaepfer, D.D.6
  • 18
    • 0031917388 scopus 로고    scopus 로고
    • Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion
    • Zheng C., Xing Z., Bian Z.C., Guo C., Akbay A., Warner L., et al. Differential regulation of Pyk2 and focal adhesion kinase (FAK). The C-terminal domain of FAK confers response to cell adhesion. J Biol Chem 273 (1998) 2384-2389
    • (1998) J Biol Chem , vol.273 , pp. 2384-2389
    • Zheng, C.1    Xing, Z.2    Bian, Z.C.3    Guo, C.4    Akbay, A.5    Warner, L.6
  • 19
    • 0034851713 scopus 로고    scopus 로고
    • Inhibition of PYK2-induced actin cytoskeleton reorganization, PYK2 autophosphorylation and focal adhesion targeting by FAK
    • Du Q.S., Ren X.R., Xie Y., Wang Q., Mei L., and Xiong W.C. Inhibition of PYK2-induced actin cytoskeleton reorganization, PYK2 autophosphorylation and focal adhesion targeting by FAK. J Cell Sci 114 (2001) 2977-2987
    • (2001) J Cell Sci , vol.114 , pp. 2977-2987
    • Du, Q.S.1    Ren, X.R.2    Xie, Y.3    Wang, Q.4    Mei, L.5    Xiong, W.C.6
  • 23
    • 56349115314 scopus 로고    scopus 로고
    • In vitro biocompatibility and bacterial adhesion of physico-chemically modified Ti6Al4V surface by means of UV irradiation
    • Gallardo-Moreno A.M., Pacha-Olivenza M.A., Saldaña L., Pérez-Giraldo C., Bruque J.M., Vilaboa N., et al. In vitro biocompatibility and bacterial adhesion of physico-chemically modified Ti6Al4V surface by means of UV irradiation. Acta Biomater 5 (2009) 181-192
    • (2009) Acta Biomater , vol.5 , pp. 181-192
    • Gallardo-Moreno, A.M.1    Pacha-Olivenza, M.A.2    Saldaña, L.3    Pérez-Giraldo, C.4    Bruque, J.M.5    Vilaboa, N.6
  • 25
    • 0034972652 scopus 로고    scopus 로고
    • Alterations in the adhesion behavior of osteoblasts by titanium particle loading: inhibition of cell function and gene expression
    • Kwon S.Y., Lin T., Takei H., Ma Q., Wood D.J., O'Connor D., et al. Alterations in the adhesion behavior of osteoblasts by titanium particle loading: inhibition of cell function and gene expression. Biorheology 38 (2001) 161-183
    • (2001) Biorheology , vol.38 , pp. 161-183
    • Kwon, S.Y.1    Lin, T.2    Takei, H.3    Ma, Q.4    Wood, D.J.5    O'Connor, D.6
  • 27
    • 0034333613 scopus 로고    scopus 로고
    • Combined effect of titanium particles and TNF-alpha on the production of IL-6 by osteoblast-like cells
    • Takei H., Pioletti D.P., Kwon S.Y., and Sung K.L. Combined effect of titanium particles and TNF-alpha on the production of IL-6 by osteoblast-like cells. J Biomed Mater Res 52 (2000) 382-387
    • (2000) J Biomed Mater Res , vol.52 , pp. 382-387
    • Takei, H.1    Pioletti, D.P.2    Kwon, S.Y.3    Sung, K.L.4
  • 28
    • 0037026404 scopus 로고    scopus 로고
    • Gene expression analysis of osteoblastic cells contacted by orthopedic implant particles
    • Pioletti D.P., Leoni L., Genini D., Takei H., Du P., and Corbeil J. Gene expression analysis of osteoblastic cells contacted by orthopedic implant particles. J Biomed Mater Res 61 (2002) 408-420
    • (2002) J Biomed Mater Res , vol.61 , pp. 408-420
    • Pioletti, D.P.1    Leoni, L.2    Genini, D.3    Takei, H.4    Du, P.5    Corbeil, J.6
  • 29
    • 0742266794 scopus 로고    scopus 로고
    • New insight into the mechanism of hip prosthesis loosening: effect of titanium debris size on osteoblast function
    • O'Connor D.T., Choi M.G., Kwon S.Y., and Paul Sung K.L. New insight into the mechanism of hip prosthesis loosening: effect of titanium debris size on osteoblast function. J Orthop Res 22 (2004) 229-236
    • (2004) J Orthop Res , vol.22 , pp. 229-236
    • O'Connor, D.T.1    Choi, M.G.2    Kwon, S.Y.3    Paul Sung, K.L.4
  • 30
    • 0034607170 scopus 로고    scopus 로고
    • Relationships among cell attachment, spreading, cytoskeletal organization, and migration rate for anchorage-dependent cells on model surfaces
    • Webb K., Hlady V., and Tresco P.A. Relationships among cell attachment, spreading, cytoskeletal organization, and migration rate for anchorage-dependent cells on model surfaces. J Biomed Mater Res 49 (2000) 362-368
    • (2000) J Biomed Mater Res , vol.49 , pp. 362-368
    • Webb, K.1    Hlady, V.2    Tresco, P.A.3
  • 31
    • 0033527155 scopus 로고    scopus 로고
    • The cytotoxic effect of titanium particles phagocytosed by osteoblasts
    • Pioletti D.P., Takei H., Kwon S.Y., Wood D., and Sung K.L. The cytotoxic effect of titanium particles phagocytosed by osteoblasts. J Biomed Mater Res 46 (1999) 399-407
    • (1999) J Biomed Mater Res , vol.46 , pp. 399-407
    • Pioletti, D.P.1    Takei, H.2    Kwon, S.Y.3    Wood, D.4    Sung, K.L.5
  • 32
    • 17544402788 scopus 로고    scopus 로고
    • Phagocytosis of wear debris by osteoblasts affects differentiation and local factor production in a manner dependent on particle composition
    • Lohmann C.H., Schwartz Z., Koster G., Jahn U., Buchhorn G.H., MacDougall M.J., et al. Phagocytosis of wear debris by osteoblasts affects differentiation and local factor production in a manner dependent on particle composition. Biomaterials 21 (2000) 551-561
    • (2000) Biomaterials , vol.21 , pp. 551-561
    • Lohmann, C.H.1    Schwartz, Z.2    Koster, G.3    Jahn, U.4    Buchhorn, G.H.5    MacDougall, M.J.6
  • 33
    • 0034153235 scopus 로고    scopus 로고
    • Titanium particles inhibit osteoblast adhesion to fibronectin-coated substrates
    • Kwon S.Y., Takei H., Pioletti D.P., Lin T., Ma Q.J., Akeson W.H., et al. Titanium particles inhibit osteoblast adhesion to fibronectin-coated substrates. J Orthop Res 18 (2000) 203-211
    • (2000) J Orthop Res , vol.18 , pp. 203-211
    • Kwon, S.Y.1    Takei, H.2    Pioletti, D.P.3    Lin, T.4    Ma, Q.J.5    Akeson, W.H.6
  • 34
    • 0032537991 scopus 로고    scopus 로고
    • Assembling an actin cytoskeleton for cell attachment and movement
    • Small J.V., Rottner K., Kaverina I., and Anderson K.I. Assembling an actin cytoskeleton for cell attachment and movement. Biochim Biophys Acta 1404 (1998) 271-281
    • (1998) Biochim Biophys Acta , vol.1404 , pp. 271-281
    • Small, J.V.1    Rottner, K.2    Kaverina, I.3    Anderson, K.I.4
  • 35
    • 33646386142 scopus 로고    scopus 로고
    • Stress-fibers are generated by two distinct actin assembly mechanisms in motile cells
    • Hotulainen P., and Lappalainen P. Stress-fibers are generated by two distinct actin assembly mechanisms in motile cells. J Cell Biol 173 (2006) 383-394
    • (2006) J Cell Biol , vol.173 , pp. 383-394
    • Hotulainen, P.1    Lappalainen, P.2
  • 36
    • 0345169048 scopus 로고    scopus 로고
    • Post-translational modifications regulate microtubule function
    • Westermann S., and Weber K. Post-translational modifications regulate microtubule function. Nat Rev Mol Cell Biol 4 (2003) 938-947
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 938-947
    • Westermann, S.1    Weber, K.2
  • 37
    • 0037448671 scopus 로고    scopus 로고
    • Cell biology: tubulin acetylation and cell motility
    • Palazzo A., Ackerman B., and Gundersen G.G. Cell biology: tubulin acetylation and cell motility. Nature 421 (2003) 230
    • (2003) Nature , vol.421 , pp. 230
    • Palazzo, A.1    Ackerman, B.2    Gundersen, G.G.3
  • 39
    • 0034755942 scopus 로고    scopus 로고
    • Molecular complexity and dynamics of cell-matrix adhesions
    • Zamir E., and Geiger B. Molecular complexity and dynamics of cell-matrix adhesions. J Cell Sci 114 (2001) 3583-3590
    • (2001) J Cell Sci , vol.114 , pp. 3583-3590
    • Zamir, E.1    Geiger, B.2
  • 40
    • 4644328892 scopus 로고    scopus 로고
    • Paxillin: adapting to change
    • Brown M.C., and Turner C.E. Paxillin: adapting to change. Physiol Rev 84 (2004) 1315-1339
    • (2004) Physiol Rev , vol.84 , pp. 1315-1339
    • Brown, M.C.1    Turner, C.E.2
  • 41
    • 21344470640 scopus 로고    scopus 로고
    • Targeting of focal adhesion kinase by flavonoids and small-interfering RNAs reduces tumor cell migration ability
    • Huang Y.T., Lee L.T., Lee P.P., Lin Y.S., and Lee M.T. Targeting of focal adhesion kinase by flavonoids and small-interfering RNAs reduces tumor cell migration ability. Anticancer Res 25 (2005) 2017-2025
    • (2005) Anticancer Res , vol.25 , pp. 2017-2025
    • Huang, Y.T.1    Lee, L.T.2    Lee, P.P.3    Lin, Y.S.4    Lee, M.T.5
  • 42
    • 33749485761 scopus 로고    scopus 로고
    • Disruption of focal adhesion kinase slows transendothelial migration of AU-565 breast cancer cells
    • Earley S., and Plopper G.E. Disruption of focal adhesion kinase slows transendothelial migration of AU-565 breast cancer cells. Biochem Biophys Res Commun 350 (2006) 405-412
    • (2006) Biochem Biophys Res Commun , vol.350 , pp. 405-412
    • Earley, S.1    Plopper, G.E.2
  • 43
    • 33845660854 scopus 로고    scopus 로고
    • FAK phosphorylation at Ser-843 inhibits Tyr-397 phosphorylation, cell spreading and migration
    • Jacamo R., Jiang X., Lunn J.A., and Rozengurt E. FAK phosphorylation at Ser-843 inhibits Tyr-397 phosphorylation, cell spreading and migration. J Cell Physiol 210 (2007) 436-444
    • (2007) J Cell Physiol , vol.210 , pp. 436-444
    • Jacamo, R.1    Jiang, X.2    Lunn, J.A.3    Rozengurt, E.4
  • 45
    • 38349058006 scopus 로고    scopus 로고
    • Pyk2 and FAK connections to p190Rho guanine nucleotide exchange factor regulate RhoA activity, focal adhesion formation, and cell motility
    • Lim Y., Lim S.T., Tomar A., Gardel M., Bernard-Trifilo J.A., Chen X.L., et al. Pyk2 and FAK connections to p190Rho guanine nucleotide exchange factor regulate RhoA activity, focal adhesion formation, and cell motility. J Cell Biol 180 (2008) 187-203
    • (2008) J Cell Biol , vol.180 , pp. 187-203
    • Lim, Y.1    Lim, S.T.2    Tomar, A.3    Gardel, M.4    Bernard-Trifilo, J.A.5    Chen, X.L.6
  • 46
    • 33748291515 scopus 로고    scopus 로고
    • From the membrane to the nucleus and back again: bifunctional focal adhesion proteins
    • Hervy M., Hoffman L., and Beckerle M.C. From the membrane to the nucleus and back again: bifunctional focal adhesion proteins. Curr Opin Cell Biol 18 (2006) 524-532
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 524-532
    • Hervy, M.1    Hoffman, L.2    Beckerle, M.C.3
  • 47
    • 33645126422 scopus 로고    scopus 로고
    • Cyclic strain promotes shuttling of PYK2/Hic-5 complex from focal contacts in osteoblast-like cells
    • Guignandon A., Boutahar N., Rattner A., Vico L., and Lafage-Proust M.H. Cyclic strain promotes shuttling of PYK2/Hic-5 complex from focal contacts in osteoblast-like cells. Biochem Biophys Res Commun 343 (2006) 407-414
    • (2006) Biochem Biophys Res Commun , vol.343 , pp. 407-414
    • Guignandon, A.1    Boutahar, N.2    Rattner, A.3    Vico, L.4    Lafage-Proust, M.H.5
  • 48
    • 16644390786 scopus 로고    scopus 로고
    • Particle bioreactivity and wear-mediated osteolysis
    • Wang M.L., Sharkey P.F., and Tuan R.S. Particle bioreactivity and wear-mediated osteolysis. J Arthroplasty 19 (2004) 1028-1038
    • (2004) J Arthroplasty , vol.19 , pp. 1028-1038
    • Wang, M.L.1    Sharkey, P.F.2    Tuan, R.S.3
  • 49
    • 40649128716 scopus 로고    scopus 로고
    • Modulation of the cross-talk between macrophages and osteoblasts by titanium-based particles
    • Vallés G., Gil-Garay E., Munuera L., and Vilaboa N. Modulation of the cross-talk between macrophages and osteoblasts by titanium-based particles. Biomaterials 29 (2008) 2326-2335
    • (2008) Biomaterials , vol.29 , pp. 2326-2335
    • Vallés, G.1    Gil-Garay, E.2    Munuera, L.3    Vilaboa, N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.