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Volumn 38, Issue 10, 2012, Pages 1734-1743

Integrin-Mediated Mechanotransduction Pathway of Low-Intensity Continuous Ultrasound in Human Chondrocytes

Author keywords

Chondrocyte; CrkII; Extracellular regulated kinase (Erk); Focal adhesion kinase (FAK); Integrin; Mechanotransduction; P130 Crk associated substrate (p130Cas); Src; Ultrasound

Indexed keywords

CHONDROCYTES; CRKII; EXTRACELLULAR-REGULATED KINASE; FOCAL ADHESION KINASE; INTEGRINS; MECHANOTRANSDUCTION; P130 CRK-ASSOCIATED SUBSTRATE (P130CAS); SRC;

EID: 84865778435     PISSN: 03015629     EISSN: 1879291X     Source Type: Journal    
DOI: 10.1016/j.ultrasmedbio.2012.06.002     Document Type: Article
Times cited : (72)

References (67)
  • 2
    • 77952705182 scopus 로고    scopus 로고
    • Biology and pathology of Rho GTPase, PI-3 kinase-Akt, and MAP kinase signaling pathways in chondrocytes
    • Beier F., Loeser R.F. Biology and pathology of Rho GTPase, PI-3 kinase-Akt, and MAP kinase signaling pathways in chondrocytes. J Cell Biochem 2010, 110:573-580.
    • (2010) J Cell Biochem , vol.110 , pp. 573-580
    • Beier, F.1    Loeser, R.F.2
  • 3
    • 0020369710 scopus 로고
    • Dedifferentiated chondrocytes re-express the differentiated collagen phenotype when cultured in agarose gels
    • Benya P.D., Shaffer J.D. Dedifferentiated chondrocytes re-express the differentiated collagen phenotype when cultured in agarose gels. Cell 1982, 30:215-224.
    • (1982) Cell , vol.30 , pp. 215-224
    • Benya, P.D.1    Shaffer, J.D.2
  • 4
    • 0035070732 scopus 로고    scopus 로고
    • The effect of dynamic compression on the response of articular cartilage to insulin-like growth factor-I
    • Bonassar L.J., Grodzinsky A.J., Frank E.H., Davila S.G., Bhaktav N.R., Trippel S.B. The effect of dynamic compression on the response of articular cartilage to insulin-like growth factor-I. J Orthop Res 2001, 19:11-17.
    • (2001) J Orthop Res , vol.19 , pp. 11-17
    • Bonassar, L.J.1    Grodzinsky, A.J.2    Frank, E.H.3    Davila, S.G.4    Bhaktav, N.R.5    Trippel, S.B.6
  • 5
    • 3142755633 scopus 로고    scopus 로고
    • Mechanical strain on osteoblasts activates autophosphorylation of focal adhesion kinase and proline-rich tyrosine kinase 2 tyrosine sites involved in ERK activation
    • Boutahar N., Guignandon A., Vico L., Lafage-Proust M.H. Mechanical strain on osteoblasts activates autophosphorylation of focal adhesion kinase and proline-rich tyrosine kinase 2 tyrosine sites involved in ERK activation. J Biol Chem 2004, 279:30588-30599.
    • (2004) J Biol Chem , vol.279 , pp. 30588-30599
    • Boutahar, N.1    Guignandon, A.2    Vico, L.3    Lafage-Proust, M.H.4
  • 6
    • 0028969166 scopus 로고
    • Mechanical compression modulates matrix biosynthesis in chondrocyte/agarose culture
    • Buschmann M.D., Gluzband Y.A., Grodzinsky A.J., Hunziker E.B. Mechanical compression modulates matrix biosynthesis in chondrocyte/agarose culture. J Cell Sci 1995, 108(Pt 4):1497-1508.
    • (1995) J Cell Sci , vol.108 , Issue.PART. 4 , pp. 1497-1508
    • Buschmann, M.D.1    Gluzband, Y.A.2    Grodzinsky, A.J.3    Hunziker, E.B.4
  • 7
    • 0033585409 scopus 로고    scopus 로고
    • Increasing extracellular matrix production in regenerating cartilage with intermittent physiological pressure
    • Carver S.E., Heath C.A. Increasing extracellular matrix production in regenerating cartilage with intermittent physiological pressure. Biotechnol Bioeng 1999, 62:166-174.
    • (1999) Biotechnol Bioeng , vol.62 , pp. 166-174
    • Carver, S.E.1    Heath, C.A.2
  • 8
    • 0032973177 scopus 로고    scopus 로고
    • Semi-continuous perfusion system for delivering intermittent physiological pressure to regenerating cartilage
    • Carver S.E., Heath C.A. Semi-continuous perfusion system for delivering intermittent physiological pressure to regenerating cartilage. Tissue Eng 1999, 5:1-11.
    • (1999) Tissue Eng , vol.5 , pp. 1-11
    • Carver, S.E.1    Heath, C.A.2
  • 10
    • 34548131565 scopus 로고    scopus 로고
    • Mechanotransduction pathways of low-intensity ultrasound in C-28/I2 human chondrocyte cell line
    • Choi B.H., Choi M.H., Kwak M.G., Min B.H., Woo Z.H., Park S.R. Mechanotransduction pathways of low-intensity ultrasound in C-28/I2 human chondrocyte cell line. Proc Inst Mech Eng H 2007, 221:527-535.
    • (2007) Proc Inst Mech Eng H , vol.221 , pp. 527-535
    • Choi, B.H.1    Choi, M.H.2    Kwak, M.G.3    Min, B.H.4    Woo, Z.H.5    Park, S.R.6
  • 11
    • 0032947058 scopus 로고    scopus 로고
    • MAP kinase pathways
    • Cobb M.H. MAP kinase pathways. Prog Biophys Mol Biol 1999, 71:479-500.
    • (1999) Prog Biophys Mol Biol , vol.71 , pp. 479-500
    • Cobb, M.H.1
  • 12
    • 0141544141 scopus 로고
    • Potential positive and negative autoregulation of p60c-src by intermolecular autophosphorylation
    • Cooper J.A., MacAuley A. Potential positive and negative autoregulation of p60c-src by intermolecular autophosphorylation. Proc Natl Acad Sci U S A 1988, 85:4232-4236.
    • (1988) Proc Natl Acad Sci U S A , vol.85 , pp. 4232-4236
    • Cooper, J.A.1    MacAuley, A.2
  • 13
    • 0033986923 scopus 로고    scopus 로고
    • Bi-directional signal transduction by integrin receptors
    • Coppolino M.G., Dedhar S. Bi-directional signal transduction by integrin receptors. Int J Biochem Cell Biol 2000, 32:171-188.
    • (2000) Int J Biochem Cell Biol , vol.32 , pp. 171-188
    • Coppolino, M.G.1    Dedhar, S.2
  • 14
    • 0036333485 scopus 로고    scopus 로고
    • Rac-PAK signaling stimulates extracellular signal-regulated kinase (ERK) activation by regulating formation of MEK1-ERK complexes
    • Eblen S.T., Slack J.K., Weber M.J., Catling A.D. Rac-PAK signaling stimulates extracellular signal-regulated kinase (ERK) activation by regulating formation of MEK1-ERK complexes. Mol Cell Biol 2002, 22:6023-6033.
    • (2002) Mol Cell Biol , vol.22 , pp. 6023-6033
    • Eblen, S.T.1    Slack, J.K.2    Weber, M.J.3    Catling, A.D.4
  • 15
    • 0031585877 scopus 로고    scopus 로고
    • Vinculin promotes cell spreading by mechanically coupling integrins to the cytoskeleton
    • Ezzell R.M., Goldmann W.H., Wang N., Parashurama N., Ingber D.E. Vinculin promotes cell spreading by mechanically coupling integrins to the cytoskeleton. Exp Cell Res 1997, 231:14-26.
    • (1997) Exp Cell Res , vol.231 , pp. 14-26
    • Ezzell, R.M.1    Goldmann, W.H.2    Wang, N.3    Parashurama, N.4    Ingber, D.E.5
  • 16
    • 0028243505 scopus 로고
    • C-Abl kinase regulates the protein binding activity of c-Crk
    • Feller S.M., Knudsen B., Hanafusa H. c-Abl kinase regulates the protein binding activity of c-Crk. Embo J 1994, 13:2341-2351.
    • (1994) Embo J , vol.13 , pp. 2341-2351
    • Feller, S.M.1    Knudsen, B.2    Hanafusa, H.3
  • 17
    • 2442531856 scopus 로고    scopus 로고
    • Mechanical compression of cartilage explants induces multiple time-dependent gene expression patterns and involves intracellular calcium and cyclic AMP
    • Fitzgerald J.B., Jin M., Dean D., Wood D.J., Zheng M.H., Grodzinsky A.J. Mechanical compression of cartilage explants induces multiple time-dependent gene expression patterns and involves intracellular calcium and cyclic AMP. J Biol Chem 2004, 279:19502-19511.
    • (2004) J Biol Chem , vol.279 , pp. 19502-19511
    • Fitzgerald, J.B.1    Jin, M.2    Dean, D.3    Wood, D.J.4    Zheng, M.H.5    Grodzinsky, A.J.6
  • 18
    • 33747635985 scopus 로고    scopus 로고
    • Shear and compression differentially regulate clusters of functionally related temporal transcription patterns in cartilage tissue
    • Fitzgerald J.B., Jin M., Grodzinsky A.J. Shear and compression differentially regulate clusters of functionally related temporal transcription patterns in cartilage tissue. J Biol Chem 2006, 281:24095-24103.
    • (2006) J Biol Chem , vol.281 , pp. 24095-24103
    • Fitzgerald, J.B.1    Jin, M.2    Grodzinsky, A.J.3
  • 19
    • 0027406842 scopus 로고
    • Cultivation of cell-polymer cartilage implants in bioreactors
    • Freed L.E., Vunjak-Novakovic G., Langer R. Cultivation of cell-polymer cartilage implants in bioreactors. J Cell Biochem 1993, 51:257-264.
    • (1993) J Cell Biochem , vol.51 , pp. 257-264
    • Freed, L.E.1    Vunjak-Novakovic, G.2    Langer, R.3
  • 20
  • 22
    • 0019210491 scopus 로고
    • Behaviour of epiphyseal mouse chondrocyte populations in monolayer culture. Morphological and immunohistochemical studies
    • Grundmann K., Zimmermann B., Barrach H.J., Merker H.J. Behaviour of epiphyseal mouse chondrocyte populations in monolayer culture. Morphological and immunohistochemical studies. Virchow Arch A Pathol Anat Histol 1980, 389:167-187.
    • (1980) Virchow Arch A Pathol Anat Histol , vol.389 , pp. 167-187
    • Grundmann, K.1    Zimmermann, B.2    Barrach, H.J.3    Merker, H.J.4
  • 25
    • 4344628956 scopus 로고    scopus 로고
    • Annexin V disruption impairs mechanically induced calcium signaling in osteoblastic cells
    • Haut Donahue T.L., Genetos D.C., Jacobs C.R., Donahue H.J., Yellowley C.E. Annexin V disruption impairs mechanically induced calcium signaling in osteoblastic cells. Bone 2004, 35:656-663.
    • (2004) Bone , vol.35 , pp. 656-663
    • Haut Donahue, T.L.1    Genetos, D.C.2    Jacobs, C.R.3    Donahue, H.J.4    Yellowley, C.E.5
  • 26
    • 0028214665 scopus 로고
    • Acceleration of tibial fracture-healing by non-invasive, low-intensity pulsed ultrasound
    • Heckman J.D., Ryaby J.P., McCabe J., Frey J.J., Kilcoyne R.F. Acceleration of tibial fracture-healing by non-invasive, low-intensity pulsed ultrasound. J Bone Joint Surg Am 1994, 76:26-34.
    • (1994) J Bone Joint Surg Am , vol.76 , pp. 26-34
    • Heckman, J.D.1    Ryaby, J.P.2    McCabe, J.3    Frey, J.J.4    Kilcoyne, R.F.5
  • 27
    • 58149177451 scopus 로고    scopus 로고
    • Induction of cell retraction by the combined actions of Abl-CrkII and Rho-ROCK1 signaling
    • Huang X., Wu D., Jin H., Stupack D., Wang J.Y. Induction of cell retraction by the combined actions of Abl-CrkII and Rho-ROCK1 signaling. J Cell Biol 2008, 183:711-723.
    • (2008) J Cell Biol , vol.183 , pp. 711-723
    • Huang, X.1    Wu, D.2    Jin, H.3    Stupack, D.4    Wang, J.Y.5
  • 29
    • 0035844250 scopus 로고    scopus 로고
    • Inhibition of cell migration by Abl family tyrosine kinases through uncoupling of Crk-CAS complexes
    • Kain K.H., Klemke R.L. Inhibition of cell migration by Abl family tyrosine kinases through uncoupling of Crk-CAS complexes. J Biol Chem 2001, 276:16185-16192.
    • (2001) J Biol Chem , vol.276 , pp. 16185-16192
    • Kain, K.H.1    Klemke, R.L.2
  • 30
    • 0023913279 scopus 로고
    • Moderate running exercise augments glycosaminoglycans and thickness of articular cartilage in the knee joint of young beagle dogs
    • Kiviranta I., Tammi M., Jurvelin J., Saamanen A.M., Helminen H.J. Moderate running exercise augments glycosaminoglycans and thickness of articular cartilage in the knee joint of young beagle dogs. J Orthop Res 1988, 6:188-195.
    • (1988) J Orthop Res , vol.6 , pp. 188-195
    • Kiviranta, I.1    Tammi, M.2    Jurvelin, J.3    Saamanen, A.M.4    Helminen, H.J.5
  • 32
    • 0028606468 scopus 로고
    • Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk
    • Knudsen B.S., Feller S.M., Hanafusa H. Four proline-rich sequences of the guanine-nucleotide exchange factor C3G bind with unique specificity to the first Src homology 3 domain of Crk. J Biol Chem 1994, 269:32781-32787.
    • (1994) J Biol Chem , vol.269 , pp. 32781-32787
    • Knudsen, B.S.1    Feller, S.M.2    Hanafusa, H.3
  • 33
    • 0035958030 scopus 로고    scopus 로고
    • Erk is essential for growth, differentiation, integrin expression, and cell function in human osteoblastic cells
    • Lai C.F., Chaudhary L., Fausto A., Halstead L.R., Ory D.S., Avioli L.V., Cheng S.L. Erk is essential for growth, differentiation, integrin expression, and cell function in human osteoblastic cells. J Biol Chem 2001, 276:14443-14450.
    • (2001) J Biol Chem , vol.276 , pp. 14443-14450
    • Lai, C.F.1    Chaudhary, L.2    Fausto, A.3    Halstead, L.R.4    Ory, D.S.5    Avioli, L.V.6    Cheng, S.L.7
  • 34
    • 0028122971 scopus 로고
    • CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells
    • Matsuda M., Hashimoto Y., Muroya K., Hasegawa H., Kurata T., Tanaka S., Nakamura S., Hattori S. CRK protein binds to two guanine nucleotide-releasing proteins for the Ras family and modulates nerve growth factor-induced activation of Ras in PC12 cells. Mol Cell Biol 1994, 14:5495-5500.
    • (1994) Mol Cell Biol , vol.14 , pp. 5495-5500
    • Matsuda, M.1    Hashimoto, Y.2    Muroya, K.3    Hasegawa, H.4    Kurata, T.5    Tanaka, S.6    Nakamura, S.7    Hattori, S.8
  • 35
    • 33748286819 scopus 로고    scopus 로고
    • Integrin-regulated FAK-Src signaling in normal and cancer cells
    • Mitra S.K., Schlaepfer D.D. Integrin-regulated FAK-Src signaling in normal and cancer cells. Curr Opin Cell Biol 2006, 18:516-523.
    • (2006) Curr Opin Cell Biol , vol.18 , pp. 516-523
    • Mitra, S.K.1    Schlaepfer, D.D.2
  • 36
    • 33846003138 scopus 로고    scopus 로고
    • Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas
    • Modzelewska K., Newman L.P., Desai R., Keely P.J. Ack1 mediates Cdc42-dependent cell migration and signaling to p130Cas. J Biol Chem 2006, 281:37527-37535.
    • (2006) J Biol Chem , vol.281 , pp. 37527-37535
    • Modzelewska, K.1    Newman, L.P.2    Desai, R.3    Keely, P.J.4
  • 37
    • 79952785070 scopus 로고    scopus 로고
    • Mechanisms of fluid-flow-induced matrix production in bone tissue engineering
    • Morris H.L., Reed C.I., Haycock J.W., Reilly G.C. Mechanisms of fluid-flow-induced matrix production in bone tissue engineering. Proc Inst Mech Eng H 2010, 224:1509-1521.
    • (2010) Proc Inst Mech Eng H , vol.224 , pp. 1509-1521
    • Morris, H.L.1    Reed, C.I.2    Haycock, J.W.3    Reilly, G.C.4
  • 38
    • 0029945648 scopus 로고    scopus 로고
    • Direct binding of C-terminal region of p130Cas to SH2 and SH3 domains of Src kinase
    • Nakamoto T., Sakai R., Ozawa K., Yazaki Y., Hirai H. Direct binding of C-terminal region of p130Cas to SH2 and SH3 domains of Src kinase. J Biol Chem 1996, 271:8959-8965.
    • (1996) J Biol Chem , vol.271 , pp. 8959-8965
    • Nakamoto, T.1    Sakai, R.2    Ozawa, K.3    Yazaki, Y.4    Hirai, H.5
  • 39
    • 0036132636 scopus 로고    scopus 로고
    • Effects of low-intensity pulsed ultrasound on proliferation and chondroitin sulfate synthesis of cultured chondrocytes embedded in atelocollagen gel
    • Nishikori T., Ochi M., Uchio Y., Maniwa S., Kataoka H., Kawasaki K., Katsube K., Kuriwaka M. Effects of low-intensity pulsed ultrasound on proliferation and chondroitin sulfate synthesis of cultured chondrocytes embedded in atelocollagen gel. J Biomed Mater Res 2002, 59:201-206.
    • (2002) J Biomed Mater Res , vol.59 , pp. 201-206
    • Nishikori, T.1    Ochi, M.2    Uchio, Y.3    Maniwa, S.4    Kataoka, H.5    Kawasaki, K.6    Katsube, K.7    Kuriwaka, M.8
  • 40
    • 34147195785 scopus 로고    scopus 로고
    • Intermittent applications of continuous ultrasound on the viability, proliferation, morphology, and matrix production of chondrocytes in 3-D matrices
    • Noriega S., Mamedov T., Turner J.A., Subramanian A. Intermittent applications of continuous ultrasound on the viability, proliferation, morphology, and matrix production of chondrocytes in 3-D matrices. Tissue Eng 2007, 13:611-618.
    • (2007) Tissue Eng , vol.13 , pp. 611-618
    • Noriega, S.1    Mamedov, T.2    Turner, J.A.3    Subramanian, A.4
  • 41
    • 84857914754 scopus 로고    scopus 로고
    • Effect of fiber diameter on the spreading, proliferation and differentiation of chondrocytes on electrospun chitosan matrices
    • Noriega S.E., Hasanova G.I., Schneider M.J., Larsen G.F., Subramanian A. Effect of fiber diameter on the spreading, proliferation and differentiation of chondrocytes on electrospun chitosan matrices. Cells Tissues Organs 2012, 195:207-221.
    • (2012) Cells Tissues Organs , vol.195 , pp. 207-221
    • Noriega, S.E.1    Hasanova, G.I.2    Schneider, M.J.3    Larsen, G.F.4    Subramanian, A.5
  • 42
    • 0018583502 scopus 로고
    • Development and reversal of a proteoglycan aggregation defect in normal canine knee cartilage after immobilization
    • Palmoski M., Perricone E., Brandt K.D. Development and reversal of a proteoglycan aggregation defect in normal canine knee cartilage after immobilization. Arthritis Rheum 1979, 22:508-517.
    • (1979) Arthritis Rheum , vol.22 , pp. 508-517
    • Palmoski, M.1    Perricone, E.2    Brandt, K.D.3
  • 43
    • 0018843805 scopus 로고
    • Joint motion in the absence of normal loading does not maintain normal articular cartilage
    • Palmoski M.J., Colyer R.A., Brandt K.D. Joint motion in the absence of normal loading does not maintain normal articular cartilage. Arthritis Rheum 1980, 23:325-334.
    • (1980) Arthritis Rheum , vol.23 , pp. 325-334
    • Palmoski, M.J.1    Colyer, R.A.2    Brandt, K.D.3
  • 44
    • 0032817692 scopus 로고    scopus 로고
    • Low-intensity ultrasound stimulates proteoglycan synthesis in rat chondrocytes by increasing aggrecan gene expression
    • Parvizi J., Wu C.C., Lewallen D.G., Greenleaf J.F., Bolander M.E. Low-intensity ultrasound stimulates proteoglycan synthesis in rat chondrocytes by increasing aggrecan gene expression. J Orthop Res 1999, 17:488-494.
    • (1999) J Orthop Res , vol.17 , pp. 488-494
    • Parvizi, J.1    Wu, C.C.2    Lewallen, D.G.3    Greenleaf, J.F.4    Bolander, M.E.5
  • 46
    • 0034762203 scopus 로고    scopus 로고
    • The Raf/MEK/ERK pathway: New concepts of activation
    • Peyssonnaux C., Eychene A. The Raf/MEK/ERK pathway: New concepts of activation. Biol Cell 2001, 93:53-62.
    • (2001) Biol Cell , vol.93 , pp. 53-62
    • Peyssonnaux, C.1    Eychene, A.2
  • 47
    • 0028889436 scopus 로고
    • Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas
    • Polte T.R., Hanks S.K. Interaction between focal adhesion kinase and Crk-associated tyrosine kinase substrate p130Cas. Proc Natl Acad Sci U S A 1995, 92:10678-10682.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 10678-10682
    • Polte, T.R.1    Hanks, S.K.2
  • 48
    • 0031047981 scopus 로고    scopus 로고
    • Complexes of focal adhesion kinase (FAK) and Crk-associated substrate (p130(Cas)) are elevated in cytoskeleton-associated fractions following adhesion and Src transformation. Requirements for Src kinase activity and FAK proline-rich motifs
    • Polte T.R., Hanks S.K. Complexes of focal adhesion kinase (FAK) and Crk-associated substrate (p130(Cas)) are elevated in cytoskeleton-associated fractions following adhesion and Src transformation. Requirements for Src kinase activity and FAK proline-rich motifs. J Biol Chem 1997, 272:5501-5509.
    • (1997) J Biol Chem , vol.272 , pp. 5501-5509
    • Polte, T.R.1    Hanks, S.K.2
  • 49
    • 48149108919 scopus 로고    scopus 로고
    • Low intensity pulsed ultrasound for fracture healing: A review of the clinical evidence and the associated biological mechanism of action
    • Pounder N.M., Harrison A.J. Low intensity pulsed ultrasound for fracture healing: A review of the clinical evidence and the associated biological mechanism of action. Ultrasonics 2008, 48:330-338.
    • (2008) Ultrasonics , vol.48 , pp. 330-338
    • Pounder, N.M.1    Harrison, A.J.2
  • 50
    • 0028916892 scopus 로고
    • Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein
    • Rosen M.K., Yamazaki T., Gish G.D., Kay C.M., Pawson T., Kay L.E. Direct demonstration of an intramolecular SH2-phosphotyrosine interaction in the Crk protein. Nature 1995, 374:477-479.
    • (1995) Nature , vol.374 , pp. 477-479
    • Rosen, M.K.1    Yamazaki, T.2    Gish, G.D.3    Kay, C.M.4    Pawson, T.5    Kay, L.E.6
  • 51
    • 0035113549 scopus 로고    scopus 로고
    • The use of low-intensity ultrasound to accelerate the healing of fractures
    • Rubin C., Bolander M., Ryaby J.P., Hadjiargyrou M. The use of low-intensity ultrasound to accelerate the healing of fractures. J Bone Joint Surg Am 2001, 83-A:259-270.
    • (2001) J Bone Joint Surg Am , pp. 259-270
    • Rubin, C.1    Bolander, M.2    Ryaby, J.P.3    Hadjiargyrou, M.4
  • 52
    • 0034769929 scopus 로고    scopus 로고
    • Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src
    • Ruest P.J., Shin N.Y., Polte T.R., Zhang X., Hanks S.K. Mechanisms of CAS substrate domain tyrosine phosphorylation by FAK and Src. Mol Cell Biol 2001, 21:7641-7652.
    • (2001) Mol Cell Biol , vol.21 , pp. 7641-7652
    • Ruest, P.J.1    Shin, N.Y.2    Polte, T.R.3    Zhang, X.4    Hanks, S.K.5
  • 53
    • 0035475321 scopus 로고    scopus 로고
    • Paxillin: A focal adhesion-associated adaptor protein
    • Schaller M.D. Paxillin: A focal adhesion-associated adaptor protein. Oncogene 2001, 20:6459-6472.
    • (2001) Oncogene , vol.20 , pp. 6459-6472
    • Schaller, M.D.1
  • 54
    • 0028350859 scopus 로고
    • Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src
    • Schaller M.D., Hildebrand J.D., Shannon J.D., Fox J.W., Vines R.R., Parsons J.T. Autophosphorylation of the focal adhesion kinase, pp125FAK, directs SH2-dependent binding of pp60src. Mol Cell Biol 1994, 14:1680-1688.
    • (1994) Mol Cell Biol , vol.14 , pp. 1680-1688
    • Schaller, M.D.1    Hildebrand, J.D.2    Shannon, J.D.3    Fox, J.W.4    Vines, R.R.5    Parsons, J.T.6
  • 55
    • 0028609382 scopus 로고
    • Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase
    • Schlaepfer D.D., Hanks S.K., Hunter T., van der Geer P. Integrin-mediated signal transduction linked to Ras pathway by GRB2 binding to focal adhesion kinase. Nature 1994, 372:786-791.
    • (1994) Nature , vol.372 , pp. 786-791
    • Schlaepfer, D.D.1    Hanks, S.K.2    Hunter, T.3    van der Geer, P.4
  • 56
    • 0031921101 scopus 로고    scopus 로고
    • Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2/mitogen-activated protein kinase: Summation of both c-Src- and focal adhesion kinase-initiated tyrosine phosphorylation events
    • Schlaepfer D.D., Jones K.C., Hunter T. Multiple Grb2-mediated integrin-stimulated signaling pathways to ERK2/mitogen-activated protein kinase: Summation of both c-Src- and focal adhesion kinase-initiated tyrosine phosphorylation events. Mol Cell Biol 1998, 18:2571-2585.
    • (1998) Mol Cell Biol , vol.18 , pp. 2571-2585
    • Schlaepfer, D.D.1    Jones, K.C.2    Hunter, T.3
  • 57
    • 4644305806 scopus 로고    scopus 로고
    • Subsets of the major tyrosine phosphorylation sites in Crk-associated substrate (CAS) are sufficient to promote cell migration
    • Shin N.Y., Dise R.S., Schneider-Mergener J., Ritchie M.D., Kilkenny D.M., Hanks S.K. Subsets of the major tyrosine phosphorylation sites in Crk-associated substrate (CAS) are sufficient to promote cell migration. J Biol Chem 2004, 279:38331-38337.
    • (2004) J Biol Chem , vol.279 , pp. 38331-38337
    • Shin, N.Y.1    Dise, R.S.2    Schneider-Mergener, J.3    Ritchie, M.D.4    Kilkenny, D.M.5    Hanks, S.K.6
  • 59
    • 0027689352 scopus 로고
    • Effects of exercise and polysulfated glycosaminoglycan on repair of articular cartilage defects in the equine carpus
    • Todhunter R.J., Minor R.R., Wootton J.A., Krook L., Burton-Wurster N., Lust G. Effects of exercise and polysulfated glycosaminoglycan on repair of articular cartilage defects in the equine carpus. J Orthop Res 1993, 11:782-795.
    • (1993) J Orthop Res , vol.11 , pp. 782-795
    • Todhunter, R.J.1    Minor, R.R.2    Wootton, J.A.3    Krook, L.4    Burton-Wurster, N.5    Lust, G.6
  • 61
    • 0031694935 scopus 로고    scopus 로고
    • Integrin signaling: Tyrosine phosphorylation events in focal adhesions
    • Vuori K. Integrin signaling: Tyrosine phosphorylation events in focal adhesions. J Membr Biol 1998, 165:191-199.
    • (1998) J Membr Biol , vol.165 , pp. 191-199
    • Vuori, K.1
  • 63
    • 0030032790 scopus 로고    scopus 로고
    • Effects of intermittent pressure-induced strain on the electrophysiology of cultured human chondrocytes: Evidence for the presence of stretch-activated membrane ion channels
    • Wright M., Jobanputra P., Bavington C., Salter D.M., Nuki G. Effects of intermittent pressure-induced strain on the electrophysiology of cultured human chondrocytes: Evidence for the presence of stretch-activated membrane ion channels. Clin Sci (Lond) 1996, 90:61-71.
    • (1996) Clin Sci (Lond) , vol.90 , pp. 61-71
    • Wright, M.1    Jobanputra, P.2    Bavington, C.3    Salter, D.M.4    Nuki, G.5
  • 65
    • 0347928765 scopus 로고    scopus 로고
    • The influence of pulsed low-intensity ultrasound on matrix production of chondrocytes at different stages of differentiation: An explant study
    • Zhang Z.J., Huckle J., Francomano C.A., Spencer R.G. The influence of pulsed low-intensity ultrasound on matrix production of chondrocytes at different stages of differentiation: An explant study. Ultrasound Med Biol 2002, 28:1547-1553.
    • (2002) Ultrasound Med Biol , vol.28 , pp. 1547-1553
    • Zhang, Z.J.1    Huckle, J.2    Francomano, C.A.3    Spencer, R.G.4
  • 66
    • 0345707656 scopus 로고    scopus 로고
    • The effects of pulsed low-intensity ultrasound on chondrocyte viability, proliferation, gene expression and matrix production
    • Zhang Z.J., Huckle J., Francomano C.A., Spencer R.G. The effects of pulsed low-intensity ultrasound on chondrocyte viability, proliferation, gene expression and matrix production. Ultrasound Med Biol 2003, 29:1645-1651.
    • (2003) Ultrasound Med Biol , vol.29 , pp. 1645-1651
    • Zhang, Z.J.1    Huckle, J.2    Francomano, C.A.3    Spencer, R.G.4
  • 67
    • 11144226218 scopus 로고    scopus 로고
    • Molecular mechanisms of low intensity pulsed ultrasound in human skin fibroblasts
    • Zhou S., Schmelz A., Seufferlein T., Li Y., Zhao J., Bachem M.G. Molecular mechanisms of low intensity pulsed ultrasound in human skin fibroblasts. J Biol Chem 2004, 279:54463-54469.
    • (2004) J Biol Chem , vol.279 , pp. 54463-54469
    • Zhou, S.1    Schmelz, A.2    Seufferlein, T.3    Li, Y.4    Zhao, J.5    Bachem, M.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.