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Volumn 320, Issue 2, 2014, Pages 175-187

Interference with the contractile machinery of the fibroblastic chondrocyte cytoskeleton induces re-expression of the cartilage phenotype through involvement of PI3K, PKC and MAPKs

Author keywords

Actin cytoskeleton; Cell contractility; Chondrocyte; PI3K, PKC, MAPK, ILK; Re differentiation; Staurosporine

Indexed keywords

ACTIN; BLEBBISTATIN; CELL MARKER; COLLAGEN TYPE 2; CYTOCHALASIN D; GLYCOSAMINOGLYCAN; INTEGRIN LINKED KINASE; MIDOSTAURIN; MITOGEN ACTIVATED PROTEIN KINASE; MITOGEN ACTIVATED PROTEIN KINASE P38; MYOSIN; PHOSPHATIDYLINOSITOL 3 KINASE; PROTEIN KINASE C; SMALL INTERFERING RNA; STAUROSPORINE;

EID: 84890858742     PISSN: 00144827     EISSN: 10902422     Source Type: Journal    
DOI: 10.1016/j.yexcr.2013.11.004     Document Type: Article
Times cited : (39)

References (65)
  • 1
    • 73449085840 scopus 로고    scopus 로고
    • Correlating cell architecture with osteogenesis: first steps towards live single cell monitoring
    • Born A., et al. Correlating cell architecture with osteogenesis: first steps towards live single cell monitoring. Eur. Cells Mater. 2009, 18:49-62.
    • (2009) Eur. Cells Mater. , vol.18 , pp. 49-62
    • Born, A.1
  • 2
    • 0037376601 scopus 로고    scopus 로고
    • Nucleus alignment and cell signaling in fibroblasts: response to a micro-grooved topography
    • Dalby M.J., Riehle M.O., Yarwood S.J., Wilkinson C.D.W., Curtis A.S.G. Nucleus alignment and cell signaling in fibroblasts: response to a micro-grooved topography. Exp. Cell Res. 2003, 284:272-280.
    • (2003) Exp. Cell Res. , vol.284 , pp. 272-280
    • Dalby, M.J.1    Riehle, M.O.2    Yarwood, S.J.3    Wilkinson, C.D.W.4    Curtis, A.S.G.5
  • 3
    • 0034715919 scopus 로고    scopus 로고
    • Shape-dependent control of cell growth, differentiation, and apoptosis: switching between attractors in cell regulatory networks
    • Huang S., Ingber D.E. Shape-dependent control of cell growth, differentiation, and apoptosis: switching between attractors in cell regulatory networks. Exp. Cell Res. 2000, 261:91-103.
    • (2000) Exp. Cell Res. , vol.261 , pp. 91-103
    • Huang, S.1    Ingber, D.E.2
  • 4
    • 33645773666 scopus 로고    scopus 로고
    • Local force and geometry sensing regulate cell functions
    • Vogel V., Sheetz M. Local force and geometry sensing regulate cell functions. Nat. Rev. Mol. Cell Biol. 2006, 7:265-275.
    • (2006) Nat. Rev. Mol. Cell Biol. , vol.7 , pp. 265-275
    • Vogel, V.1    Sheetz, M.2
  • 5
    • 0018221370 scopus 로고
    • Independent regulation of collagen types by chondrocytes during the loss of differentiated function in culture
    • Benya P.D., Padilla S.R., Nimni M.E. Independent regulation of collagen types by chondrocytes during the loss of differentiated function in culture. Cell 1978, 15:1313-1321.
    • (1978) Cell , vol.15 , pp. 1313-1321
    • Benya, P.D.1    Padilla, S.R.2    Nimni, M.E.3
  • 6
    • 0017154306 scopus 로고
    • Changes in type of collagen synthesized as clones of chick chondrocytes grow and eventually lose division capacity
    • Mayne R., Vail M.S., Mayne P.M., Miller E.J. Changes in type of collagen synthesized as clones of chick chondrocytes grow and eventually lose division capacity. Proc. Natl. Acad. Sci. U.S.A. 1976, 73:1674-1678.
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 1674-1678
    • Mayne, R.1    Vail, M.S.2    Mayne, P.M.3    Miller, E.J.4
  • 7
    • 0035587094 scopus 로고    scopus 로고
    • Regulation of type-II collagen gene expression during human chondrocyte de-differentiation and recovery of chondrocyte-specific phenotype in culture involves Sry-type high-mobility-group box (SOX) transcription factors
    • Stokes D.G., et al. Regulation of type-II collagen gene expression during human chondrocyte de-differentiation and recovery of chondrocyte-specific phenotype in culture involves Sry-type high-mobility-group box (SOX) transcription factors. Biochem. J. 2001, 360:461-470.
    • (2001) Biochem. J. , vol.360 , pp. 461-470
    • Stokes, D.G.1
  • 8
    • 0020369710 scopus 로고
    • Dedifferentiated chondrocytes reexpress the differentiated collagen phenotype when cultured in agarose gels
    • Benya P.D., Shaffer J.D. Dedifferentiated chondrocytes reexpress 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
  • 9
    • 0028276648 scopus 로고
    • Reexpression of cartilage-specific genes by dedifferentiated human articular chondrocytes cultured in alginate beads
    • Bonaventure J., et al. Reexpression of cartilage-specific genes by dedifferentiated human articular chondrocytes cultured in alginate beads. Exp. Cell Res. 1994, 212:97-104.
    • (1994) Exp. Cell Res. , vol.212 , pp. 97-104
    • Bonaventure, J.1
  • 10
    • 17644387150 scopus 로고    scopus 로고
    • Characterization of human nasal septal chondrocytes cultured in alginate
    • Chia S.H., et al. Characterization of human nasal septal chondrocytes cultured in alginate. J. Am. Coll. Surg. 2005, 200:691-704.
    • (2005) J. Am. Coll. Surg. , vol.200 , pp. 691-704
    • Chia, S.H.1
  • 11
    • 0035047449 scopus 로고    scopus 로고
    • Specific growth factors during the expansion and redifferentiation of adult human articular chondrocytes enhance chondrogenesis and cartilaginous tissue formation in vitro
    • Jakob M., et al. Specific growth factors during the expansion and redifferentiation of adult human articular chondrocytes enhance chondrogenesis and cartilaginous tissue formation in vitro. J. Cell. Biochem. 2001, 81:368-377.
    • (2001) J. Cell. Biochem. , vol.81 , pp. 368-377
    • Jakob, M.1
  • 12
    • 0035989141 scopus 로고    scopus 로고
    • Redifferentiation of dedifferentiated human chondrocytes in high-density cultures
    • Schulze-Tanzil G., et al. Redifferentiation of dedifferentiated human chondrocytes in high-density cultures. Cell Tissue Res. 2002, 308:371-379.
    • (2002) Cell Tissue Res. , vol.308 , pp. 371-379
    • Schulze-Tanzil, G.1
  • 13
    • 0023902202 scopus 로고
    • Microfilament modification by dihydrocytochalasin B causes retinoic acid-modulated chondrocytes to reexpress the differentiated collagen phenotype without a change in shape
    • Benya P.D., Brown P.D., Padilla S.R. Microfilament modification by dihydrocytochalasin B causes retinoic acid-modulated chondrocytes to reexpress the differentiated collagen phenotype without a change in shape. J. Cell Biol. 1988, 106:161-170.
    • (1988) J. Cell Biol. , vol.106 , pp. 161-170
    • Benya, P.D.1    Brown, P.D.2    Padilla, S.R.3
  • 14
    • 0023931326 scopus 로고
    • Alterations in chondrocyte cytoskeletal architecture during phenotypic modulation by retinoic acid and dihydrocytochalasin B-induced reexpression
    • Brown P.D., Benya P.D. Alterations in chondrocyte cytoskeletal architecture during phenotypic modulation by retinoic acid and dihydrocytochalasin B-induced reexpression. J. Cell Biol. 1988, 106:171-179.
    • (1988) J. Cell Biol. , vol.106 , pp. 171-179
    • Brown, P.D.1    Benya, P.D.2
  • 15
    • 0030725884 scopus 로고    scopus 로고
    • Restoration of the differentiated functions of serially passaged chondrocytes using staurosporine
    • Borge L., Lemare F., Demignot S., Adolphe M. Restoration of the differentiated functions of serially passaged chondrocytes using staurosporine. In Vitro Cell. Dev. Biol. Anim. 1997, 33:703-709.
    • (1997) In Vitro Cell. Dev. Biol. Anim. , vol.33 , pp. 703-709
    • Borge, L.1    Lemare, F.2    Demignot, S.3    Adolphe, M.4
  • 16
    • 0037326195 scopus 로고    scopus 로고
    • Modulation of the contractile and biosynthetic activity of chondrocytes seeded in collagen-glycosaminoglycan matrices
    • Lee C.R., Grodzinsky A.J., Spector M. Modulation of the contractile and biosynthetic activity of chondrocytes seeded in collagen-glycosaminoglycan matrices. Tissue Eng. 2003, 9:27-36.
    • (2003) Tissue Eng. , vol.9 , pp. 27-36
    • Lee, C.R.1    Grodzinsky, A.J.2    Spector, M.3
  • 17
    • 0019829488 scopus 로고
    • Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change
    • Casella J.F., Flanagan M.D., Lin S. Cytochalasin D inhibits actin polymerization and induces depolymerization of actin filaments formed during platelet shape change. Nature 1981, 293:302-305.
    • (1981) Nature , vol.293 , pp. 302-305
    • Casella, J.F.1    Flanagan, M.D.2    Lin, S.3
  • 18
    • 33746031840 scopus 로고    scopus 로고
    • Dual effects of staurosporine on A431 and NRK cells: microfilament disassembly and uncoordinated lamellipodial activity followed by cell death
    • Mannherz H.G., et al. Dual effects of staurosporine on A431 and NRK cells: microfilament disassembly and uncoordinated lamellipodial activity followed by cell death. Eur. J. Cell Biol. 2006, 85:785-802.
    • (2006) Eur. J. Cell Biol. , vol.85 , pp. 785-802
    • Mannherz, H.G.1
  • 19
    • 0024394417 scopus 로고
    • Staurosporine, K-252 and UCN-01: potent but nonspecific inhibitors of protein kinases
    • Rüegg U.T., Gillian B. Staurosporine, K-252 and UCN-01: potent but nonspecific inhibitors of protein kinases. Trends Pharmacol. Sci. 1989, 10:218-220.
    • (1989) Trends Pharmacol. Sci. , vol.10 , pp. 218-220
    • Rüegg, U.T.1    Gillian, B.2
  • 20
    • 40949165235 scopus 로고    scopus 로고
    • Actin stress fibers transmit and focus force to activate mechanosensitive channels
    • Hayakawa K., Tatsumi H., Sokabe M. Actin stress fibers transmit and focus force to activate mechanosensitive channels. J. Cell Sci. 2008, 121:496-503.
    • (2008) J. Cell Sci. , vol.121 , pp. 496-503
    • Hayakawa, K.1    Tatsumi, H.2    Sokabe, M.3
  • 21
    • 0030956506 scopus 로고    scopus 로고
    • Mechanism of the morphological changes induced by staurosporine in rat osteoblasts
    • Yang R., Fu W., Wang S., Liu T., Lin-Shiau S. Mechanism of the morphological changes induced by staurosporine in rat osteoblasts. Calcif. Tissue Int. 1997, 61:68-73.
    • (1997) Calcif. Tissue Int. , vol.61 , pp. 68-73
    • Yang, R.1    Fu, W.2    Wang, S.3    Liu, T.4    Lin-Shiau, S.5
  • 22
    • 4644234194 scopus 로고    scopus 로고
    • Current perspectives on cartilage and chondrocyte mechanobiology
    • Lammi M.J. Current perspectives on cartilage and chondrocyte mechanobiology. Biorheology 2004, 41:593-596.
    • (2004) Biorheology , vol.41 , pp. 593-596
    • Lammi, M.J.1
  • 23
    • 77951737987 scopus 로고    scopus 로고
    • The switchable integrin adhesome
    • Zaidel-Bar R., Geiger B. The switchable integrin adhesome. J. Cell Sci. 2010, 123:1385-1388.
    • (2010) J. Cell Sci. , vol.123 , pp. 1385-1388
    • Zaidel-Bar, R.1    Geiger, B.2
  • 24
    • 0037371287 scopus 로고    scopus 로고
    • Chondrogenesis induced by actin cytoskeleton disruption is regulated via protein kinase C-dependent p38 mitogen-activated protein kinase signaling
    • Lim Y.B., et al. Chondrogenesis induced by actin cytoskeleton disruption is regulated via protein kinase C-dependent p38 mitogen-activated protein kinase signaling. J. Cell. Biochem. 2003, 88:713-718.
    • (2003) J. Cell. Biochem. , vol.88 , pp. 713-718
    • Lim, Y.B.1
  • 25
    • 40049101000 scopus 로고    scopus 로고
    • A comparison of the involvement of p38, ERK1/2 and PI3K in growth factor-induced chondrogenic differentiation of mesenchymal stem cells
    • McMahon L.A., Prendergast P.J., Campbell V.A. A comparison of the involvement of p38, ERK1/2 and PI3K in growth factor-induced chondrogenic differentiation of mesenchymal stem cells. Biochem. Biophys. Res. Commun. 2008, 368:990-995.
    • (2008) Biochem. Biophys. Res. Commun. , vol.368 , pp. 990-995
    • McMahon, L.A.1    Prendergast, P.J.2    Campbell, V.A.3
  • 26
    • 0037040939 scopus 로고    scopus 로고
    • Maintenance of differentiated phenotype of articular chondrocytes by protein kinase C and extracellular signal-regulated protein kinase
    • Yoon Y.-M., et al. Maintenance of differentiated phenotype of articular chondrocytes by protein kinase C and extracellular signal-regulated protein kinase. J. Biol. Chem. 2002, 277:8412-8420.
    • (2002) J. Biol. Chem. , vol.277 , pp. 8412-8420
    • Yoon, Y.-M.1
  • 27
    • 38049018155 scopus 로고    scopus 로고
    • A quantitative analysis of kinase inhibitor selectivity
    • Karaman M.W., et al. A quantitative analysis of kinase inhibitor selectivity. Nat. Biotechnol. 2008, 26:127-132.
    • (2008) Nat. Biotechnol. , vol.26 , pp. 127-132
    • Karaman, M.W.1
  • 29
    • 52949101333 scopus 로고    scopus 로고
    • Integrity of the cortical actin ring is required for activation of the PI3K/Akt and p38 MAPK signaling pathways in redifferentiation of chondrocytes on chitosan
    • Park E.H., et al. Integrity of the cortical actin ring is required for activation of the PI3K/Akt and p38 MAPK signaling pathways in redifferentiation of chondrocytes on chitosan. Cell Biol. Int. 2008, 32:1272-1278.
    • (2008) Cell Biol. Int. , vol.32 , pp. 1272-1278
    • Park, E.H.1
  • 31
    • 0021181696 scopus 로고
    • Cytoskeleton and differentiation: effects of cytochalasin B and colchicine on expression of the differentiated phenotype of rabbit costal chondrocytes in culture
    • Takigawa M., Takano T., Shirai E., Suzuki F. Cytoskeleton and differentiation: effects of cytochalasin B and colchicine on expression of the differentiated phenotype of rabbit costal chondrocytes in culture. Cell Differ. 1984, 14:197-204.
    • (1984) Cell Differ. , vol.14 , pp. 197-204
    • Takigawa, M.1    Takano, T.2    Shirai, E.3    Suzuki, F.4
  • 32
    • 0033871679 scopus 로고    scopus 로고
    • Disruption of actin cytoskeleton induces chondrogenesis of mesenchymal cells by activating protein kinase C-α signaling
    • Lim Y.-B., et al. Disruption of actin cytoskeleton induces chondrogenesis of mesenchymal cells by activating protein kinase C-α signaling. Biochem. Biophys. Res. Commun. 2000, 273:609-613.
    • (2000) Biochem. Biophys. Res. Commun. , vol.273 , pp. 609-613
    • Lim, Y.-B.1
  • 33
    • 23844505021 scopus 로고    scopus 로고
    • N-cadherin mediated distribution of β-catenin alters MAP kinase and BMP-2 signaling on chondrogenesis-related gene expression
    • Modarresi R., et al. N-cadherin mediated distribution of β-catenin alters MAP kinase and BMP-2 signaling on chondrogenesis-related gene expression. J. Cell. Biochem. 2005, 95:53-63.
    • (2005) J. Cell. Biochem. , vol.95 , pp. 53-63
    • Modarresi, R.1
  • 35
    • 0037070553 scopus 로고    scopus 로고
    • Cell-cell signaling by direct contact increases cell proliferation via a PI3K-dependent signal
    • Nelson C.M., Chen C.S. Cell-cell signaling by direct contact increases cell proliferation via a PI3K-dependent signal. FEBS Lett. 2002, 514:238-242.
    • (2002) FEBS Lett. , vol.514 , pp. 238-242
    • Nelson, C.M.1    Chen, C.S.2
  • 36
    • 33744956176 scopus 로고    scopus 로고
    • RhoA/ROCK signaling regulates chondrogenesis in a context-dependent manner
    • Woods A., Beier F. RhoA/ROCK signaling regulates chondrogenesis in a context-dependent manner. J. Biol. Chem. 2006, 281:13134-13140.
    • (2006) J. Biol. Chem. , vol.281 , pp. 13134-13140
    • Woods, A.1    Beier, F.2
  • 38
    • 0345688091 scopus 로고    scopus 로고
    • Contractile forces generated by articular chondrocytes in collagen-glycosaminoglycan matrices
    • Zaleskas J.M., et al. Contractile forces generated by articular chondrocytes in collagen-glycosaminoglycan matrices. Biomaterials 2004, 25:1299-1308.
    • (2004) Biomaterials , vol.25 , pp. 1299-1308
    • Zaleskas, J.M.1
  • 39
    • 84866397936 scopus 로고    scopus 로고
    • ECM stiffness primes the TGFβ pathway to promote chondrocyte differentiation
    • Allen J.L., Cooke M.E., Alliston T. ECM stiffness primes the TGFβ pathway to promote chondrocyte differentiation. Mol. Biol. Cell 2012, 23(18):3731-3742.
    • (2012) Mol. Biol. Cell , vol.23 , Issue.18 , pp. 3731-3742
    • Allen, J.L.1    Cooke, M.E.2    Alliston, T.3
  • 40
    • 79952420018 scopus 로고    scopus 로고
    • Biomaterials & scaffolds for tissue engineering
    • O'Brien F.J. Biomaterials & scaffolds for tissue engineering. Mater. Today 2011, 14:88-95.
    • (2011) Mater. Today , vol.14 , pp. 88-95
    • O'Brien, F.J.1
  • 41
    • 35848947564 scopus 로고    scopus 로고
    • Activation of FAK/PI3K/Rac1signaling controls actin reorganization and inhibits cell motility in human cancer cells
    • Kallergi G., Agelaki S., Markomanolaki H., Georgoulias V., Stournaras C. Activation of FAK/PI3K/Rac1signaling controls actin reorganization and inhibits cell motility in human cancer cells. Cell Physiol. Biochem. 2007, 20:977-986.
    • (2007) Cell Physiol. Biochem. , vol.20 , pp. 977-986
    • Kallergi, G.1    Agelaki, S.2    Markomanolaki, H.3    Georgoulias, V.4    Stournaras, C.5
  • 42
    • 0030839766 scopus 로고    scopus 로고
    • Phosphatidylinositol 3-kinase is required for integrin-stimulated Akt and Raf-1/mitogen-activated protein kinase pathway activation
    • King W.G., Mattaliano M.D., Chan T.O., Tsichlis P.N., Brugge J.S. Phosphatidylinositol 3-kinase is required for integrin-stimulated Akt and Raf-1/mitogen-activated protein kinase pathway activation. Mol. Cell. Biol. 1997, 17:4406-4418.
    • (1997) Mol. Cell. Biol. , vol.17 , pp. 4406-4418
    • King, W.G.1    Mattaliano, M.D.2    Chan, T.O.3    Tsichlis, P.N.4    Brugge, J.S.5
  • 43
    • 0028429961 scopus 로고
    • Activation of phosphoinositide 3-kinase is required for PDGF-stimulated membrane ruffling
    • Wennström S., et al. Activation of phosphoinositide 3-kinase is required for PDGF-stimulated membrane ruffling. Curr. Biol. 1994, 4:385-393.
    • (1994) Curr. Biol. , vol.4 , pp. 385-393
    • Wennström, S.1
  • 44
    • 0141592429 scopus 로고    scopus 로고
    • Signaling mechanisms leading to the regulation of differentiation and apoptosis of articular chondrocytes by insulin-like growth factor-1
    • Oh C.-D., Chun J.-S. Signaling mechanisms leading to the regulation of differentiation and apoptosis of articular chondrocytes by insulin-like growth factor-1. J. Biol. Chem. 2003, 278:36563-36571.
    • (2003) J. Biol. Chem. , vol.278 , pp. 36563-36571
    • Oh, C.-D.1    Chun, J.-S.2
  • 45
    • 70450274965 scopus 로고    scopus 로고
    • Oxidative stress inhibits insulin-like growth factor-I induction of chondrocyte proteoglycan synthesis through differential regulation of phosphatidylinositol 3-kinase-Akt and MEK-ERK MAPK signaling pathways
    • Yin W., Park J.-I., Loeser R.F. Oxidative stress inhibits insulin-like growth factor-I induction of chondrocyte proteoglycan synthesis through differential regulation of phosphatidylinositol 3-kinase-Akt and MEK-ERK MAPK signaling pathways. J. Biol. Chem. 2009, 284:31972-31981.
    • (2009) J. Biol. Chem. , vol.284 , pp. 31972-31981
    • Yin, W.1    Park, J.-I.2    Loeser, R.F.3
  • 46
    • 23644450412 scopus 로고    scopus 로고
    • IGF-I stimulation of proteoglycan synthesis by chondrocytes requires activation of the PI 3-kinase pathway but not ERK MAPK
    • Starkman B.G., Cravero J.D., Delcarlo M., Loeser R.F. IGF-I stimulation of proteoglycan synthesis by chondrocytes requires activation of the PI 3-kinase pathway but not ERK MAPK. Biochem. J. 2005, 389:723-729.
    • (2005) Biochem. J. , vol.389 , pp. 723-729
    • Starkman, B.G.1    Cravero, J.D.2    Delcarlo, M.3    Loeser, R.F.4
  • 47
    • 0032530482 scopus 로고    scopus 로고
    • Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase
    • Delcommenne M., et al. Phosphoinositide-3-OH kinase-dependent regulation of glycogen synthase kinase 3 and protein kinase B/AKT by the integrin-linked kinase. Proc. Natl. Acad. Sci. U.S.A. 1998, 95:11211-11216.
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 11211-11216
    • Delcommenne, M.1
  • 48
    • 70349309642 scopus 로고    scopus 로고
    • How ILK and kindlins cooperate to orchestrate integrin signaling
    • Bottcher R.T., Lange A., Fassler R. How ILK and kindlins cooperate to orchestrate integrin signaling. Curr. Opin. Cell Biol. 2009, 21:670-675.
    • (2009) Curr. Opin. Cell Biol. , vol.21 , pp. 670-675
    • Bottcher, R.T.1    Lange, A.2    Fassler, R.3
  • 49
    • 0030026679 scopus 로고    scopus 로고
    • Regulation of cell adhesion and anchorage-dependent growth by a new β1-integrin-linked protein kinase
    • Hannigan G.E., et al. Regulation of cell adhesion and anchorage-dependent growth by a new β1-integrin-linked protein kinase. Nature 1996, 379:91-96.
    • (1996) Nature , vol.379 , pp. 91-96
    • Hannigan, G.E.1
  • 50
    • 80053574271 scopus 로고    scopus 로고
    • Mechanotransduction activates alpha(5)beta(1) integrin and PI3K/Akt signaling pathways in mandibular osteoblasts
    • Watabe H., Furuhama T., Tani-Ishii N., Mikuni-Takagaki Y. Mechanotransduction activates alpha(5)beta(1) integrin and PI3K/Akt signaling pathways in mandibular osteoblasts. Exp. Cell Res. 2011, 317:2642-2649.
    • (2011) Exp. Cell Res. , vol.317 , pp. 2642-2649
    • Watabe, H.1    Furuhama, T.2    Tani-Ishii, N.3    Mikuni-Takagaki, Y.4
  • 51
    • 75049085759 scopus 로고    scopus 로고
    • The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase!
    • Wickstrom S.A., Lange A., Montanez E., Fassler R. The ILK/PINCH/parvin complex: the kinase is dead, long live the pseudokinase!. EMBO J. 2010, 29:281-291.
    • (2010) EMBO J. , vol.29 , pp. 281-291
    • Wickstrom, S.A.1    Lange, A.2    Montanez, E.3    Fassler, R.4
  • 52
    • 0038323946 scopus 로고    scopus 로고
    • Integrin-linked kinase regulates chondrocyte shape and proliferation
    • Grashoff C., Aszodi A., Sakai T., Hunziker E.B., Fassler R. Integrin-linked kinase regulates chondrocyte shape and proliferation. EMBO Rep. 2003, 4:432-438.
    • (2003) EMBO Rep. , vol.4 , pp. 432-438
    • Grashoff, C.1    Aszodi, A.2    Sakai, T.3    Hunziker, E.B.4    Fassler, R.5
  • 54
    • 0345803932 scopus 로고    scopus 로고
    • PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival
    • Fukuda T. PINCH-1 is an obligate partner of integrin-linked kinase (ILK) functioning in cell shape modulation, motility, and survival. J. Biol. Chem. 2003, 278:51324-51333.
    • (2003) J. Biol. Chem. , vol.278 , pp. 51324-51333
    • Fukuda, T.1
  • 55
    • 0034007869 scopus 로고    scopus 로고
    • Opposing role of mitogen-activated protein kinase subtypes, ERK-1/2 and p38, in the regulation of chondrogenesis of mesenchymes
    • Oh C.-D., et al. Opposing role of mitogen-activated protein kinase subtypes, ERK-1/2 and p38, in the regulation of chondrogenesis of mesenchymes. J. Biol. Chem. 2000, 275:5613-5619.
    • (2000) J. Biol. Chem. , vol.275 , pp. 5613-5619
    • Oh, C.-D.1
  • 56
    • 0033787959 scopus 로고    scopus 로고
    • Protein kinase A regulates chondrogenesis of mesenchymal cells at the post-precartilage condensation stage via protein kinase C-α signaling
    • Yoon Y.-M., Oh C.-D., Kang S.-S., Chun J.-S. Protein kinase A regulates chondrogenesis of mesenchymal cells at the post-precartilage condensation stage via protein kinase C-α signaling. J. Bone Miner. Res. 2000, 15:2197-2205.
    • (2000) J. Bone Miner. Res. , vol.15 , pp. 2197-2205
    • Yoon, Y.-M.1    Oh, C.-D.2    Kang, S.-S.3    Chun, J.-S.4
  • 57
    • 1042301398 scopus 로고    scopus 로고
    • The MEK-ERK signaling pathway is a negative regulator of cartilage-specific gene expression in embryonic limb mesenchyme
    • Bobick B.E., Kulyk W.M. The MEK-ERK signaling pathway is a negative regulator of cartilage-specific gene expression in embryonic limb mesenchyme. J. Biol. Chem. 2004, 279:4588-4595.
    • (2004) J. Biol. Chem. , vol.279 , pp. 4588-4595
    • Bobick, B.E.1    Kulyk, W.M.2
  • 58
    • 54449087835 scopus 로고    scopus 로고
    • Morphology of the bovine chondrocyte and of its cytoskeleton in isolation and in situ: are chondrocytes ubiquitously paired through the entire layer of articular cartilage?
    • Sasazaki Y., Seedhom B.B., Shore R. Morphology of the bovine chondrocyte and of its cytoskeleton in isolation and in situ: are chondrocytes ubiquitously paired through the entire layer of articular cartilage?. Rheumatology 2008, 47:1641-1646.
    • (2008) Rheumatology , vol.47 , pp. 1641-1646
    • Sasazaki, Y.1    Seedhom, B.B.2    Shore, R.3
  • 59
    • 34247562172 scopus 로고    scopus 로고
    • The regulation of osteogenesis by ECM rigidity in MC3T3-E1 cells requires MAPK activation
    • Khatiwala C.B., Peyton S.R., Metzke M., Putnam A.J. The regulation of osteogenesis by ECM rigidity in MC3T3-E1 cells requires MAPK activation. J. Cell. Physiol. 2007, 211:661-672.
    • (2007) J. Cell. Physiol. , vol.211 , pp. 661-672
    • Khatiwala, C.B.1    Peyton, S.R.2    Metzke, M.3    Putnam, A.J.4
  • 60
    • 20244384369 scopus 로고    scopus 로고
    • Inhibition of cartilage degradation: a combined tissue engineering and gene therapy approach
    • Kafienah W., Al-Fayez F., Hollander A.P., Barker M.D. Inhibition of cartilage degradation: a combined tissue engineering and gene therapy approach. Arthr. Rheum. 2003, 48:709-718.
    • (2003) Arthr. Rheum. , vol.48 , pp. 709-718
    • Kafienah, W.1    Al-Fayez, F.2    Hollander, A.P.3    Barker, M.D.4
  • 61
    • 84889778479 scopus 로고    scopus 로고
    • Tissue Engineering of Articular Cartilage, in Culture of Cells for Tissue Engineering, in: G. Vunjak-Novakovic, R.I. Freshney (Eds), John Wiley & Sons, Inc., Hoboken, NJ, USA. [Chapter 7]
    • K. Masuda, R.L. Sah, Tissue Engineering of Articular Cartilage, in Culture of Cells for Tissue Engineering, in: G. Vunjak-Novakovic, R.I. Freshney (Eds), John Wiley & Sons, Inc., Hoboken, NJ, USA, 2006. [Chapter 7]. http://dx.doi.org/10.1002/0471741817.
    • (2006)
    • Masuda, K.1    Sah, R.L.2
  • 63
    • 0038325620 scopus 로고    scopus 로고
    • HIF-1α controls extracellular matrix synthesis by epiphyseal chondrocytes
    • Pfander D., Cramer T., Schipani E., Johnson R.S. HIF-1α controls extracellular matrix synthesis by epiphyseal chondrocytes. J. Cell Sci. 2003, 116:1819-1826.
    • (2003) J. Cell Sci. , vol.116 , pp. 1819-1826
    • Pfander, D.1    Cramer, T.2    Schipani, E.3    Johnson, R.S.4
  • 64
    • 0024363421 scopus 로고
    • Spectrofluorometry of dyes with DNAs of different base composition and conformation
    • Daxhelet G.A., Coene M.M., Hoet P.P., Cocito C.G. Spectrofluorometry of dyes with DNAs of different base composition and conformation. Anal. Biochem. 1989, 179:401-403.
    • (1989) Anal. Biochem. , vol.179 , pp. 401-403
    • Daxhelet, G.A.1    Coene, M.M.2    Hoet, P.P.3    Cocito, C.G.4
  • 65
    • 35348866826 scopus 로고    scopus 로고
    • The reliability and limits of the MTT reduction assay for carbon nanotubes-cell interaction
    • Belyanskaya L., Manser P., Spohn P., Bruinink A., Wick P. The reliability and limits of the MTT reduction assay for carbon nanotubes-cell interaction. Carbon 2007, 45:2643-2648.
    • (2007) Carbon , vol.45 , pp. 2643-2648
    • Belyanskaya, L.1    Manser, P.2    Spohn, P.3    Bruinink, A.4    Wick, P.5


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