메뉴 건너뛰기




Volumn 100, Issue 7, 1997, Pages 1789-1796

Outside-in signaling in the chondrocyte. Nitric oxide disrupts fibronectin-induced assembly of a subplasmalemmal actin/rho a/focal adhesion kinase signaling complex

Author keywords

Cartilage; Cyclic GMP; Extracellular matrix; Focal adhesion complex; Integrin signaling

Indexed keywords

CYCLIC GMP; F ACTIN; FIBRONECTIN; FIBRONECTIN RECEPTOR; FOCAL ADHESION KINASE; GUANINE NUCLEOTIDE BINDING PROTEIN; NITRIC OXIDE; PHOSPHOPROTEIN;

EID: 0030885574     PISSN: 00219738     EISSN: None     Source Type: Journal    
DOI: 10.1172/JCI119706     Document Type: Article
Times cited : (111)

References (44)
  • 3
    • 0028988155 scopus 로고
    • Expression of betal integrins by cultured articular chondrocytes and in osteoarthritic cartilage
    • Loeser, R.F., C.S. Carlson, and M.P. McGee. 1995. Expression of betal integrins by cultured articular chondrocytes and in osteoarthritic cartilage. Exp. Cell Res. 217:248-257.
    • (1995) Exp. Cell Res. , vol.217 , pp. 248-257
    • Loeser, R.F.1    Carlson, C.S.2    McGee, M.P.3
  • 4
    • 0023233133 scopus 로고
    • Ultrastructural localisation of fibronectin in human osteoarthritic articular cartilage
    • Rees, J.A., S.Y. Ali, and R.A. Brown. 1987. Ultrastructural localisation of fibronectin in human osteoarthritic articular cartilage. Ann. Rheum. Dis. 46: 816-822.
    • (1987) Ann. Rheum. Dis. , vol.46 , pp. 816-822
    • Rees, J.A.1    Ali, S.Y.2    Brown, R.A.3
  • 5
    • 0025205276 scopus 로고
    • Integrins and other cell adhesion molecules
    • Albelda, S.M., and C.A. Buck. 1990. Integrins and other cell adhesion molecules. FASEB J. 4:2868-2880.
    • (1990) FASEB J. , vol.4 , pp. 2868-2880
    • Albelda, S.M.1    Buck, C.A.2
  • 6
    • 0028335948 scopus 로고
    • Anchorage dependence, integrins, and apoptosis
    • Ruoslahti, E., and J.C. Reed. 1994. Anchorage dependence, integrins, and apoptosis. Cell. 77:477-478.
    • (1994) Cell , vol.77 , pp. 477-478
    • Ruoslahti, E.1    Reed, J.C.2
  • 7
    • 0023666065 scopus 로고
    • Integrins: A family of cell surface receptors
    • Hynes, R.O. 1987. Integrins: a family of cell surface receptors. Cell. 48: 549-554.
    • (1987) Cell , vol.48 , pp. 549-554
    • Hynes, R.O.1
  • 8
    • 0029100101 scopus 로고
    • Requirement for the synergy site for cell adhesion to fibronection depends on the activation state of integrin alpha5 beta1
    • Danen, E.H., S. Aota, A.A. Van Kraats, K.M. Yamada, D.J. Ruiter, and G.N. Van Muijen. 1995. Requirement for the synergy site for cell adhesion to fibronection depends on the activation state of integrin alpha5 beta1. J. Biol. Chem. 270:21612-21618.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21612-21618
    • Danen, E.H.1    Aota, S.2    Van Kraats, A.A.3    Yamada, K.M.4    Ruiter, D.J.5    Van Muijen, G.N.6
  • 9
    • 0028987936 scopus 로고
    • Integrins and signal transduction pathways: The road taken
    • Clark, E.A., and J.S. Brugge. 1995. Integrins and signal transduction pathways: the road taken. Science (Wash. DC). 268:233-239.
    • (1995) Science (Wash. DC) , vol.268 , pp. 233-239
    • Clark, E.A.1    Brugge, J.S.2
  • 10
    • 0026573491 scopus 로고
    • Localised application of an activating signal to a cell: Experimental use of fibronectin bound to beads and the implications for mechanisms of adhesion
    • Curtis, A.S., M. McGrath, and L. Gasmi. 1992. Localised application of an activating signal to a cell: experimental use of fibronectin bound to beads and the implications for mechanisms of adhesion. J. Cell Sci. 101:427-436.
    • (1992) J. Cell Sci. , vol.101 , pp. 427-436
    • Curtis, A.S.1    McGrath, M.2    Gasmi, L.3
  • 11
    • 0028113983 scopus 로고
    • Inducible nitric oxide synthase from human articular chondrocytes: cDNA cloning and analysis of mRNA expression
    • Maier, R., G. Bilbe, J. Rediske, and M. Lotz. 1994. Inducible nitric oxide synthase from human articular chondrocytes: cDNA cloning and analysis of mRNA expression. Biochim. Biophys. Acta. 1208:145-150.
    • (1994) Biochim. Biophys. Acta. , vol.1208 , pp. 145-150
    • Maier, R.1    Bilbe, G.2    Rediske, J.3    Lotz, M.4
  • 12
    • 0028819787 scopus 로고
    • The expression and regulation of nitric oxide synthase in human osteoarthritic-affected chondrocytes: Evidence for up-regulated neuronal nitric oxide synthase
    • Amin, A.R., P.E. Di Cesare, P. Vyas, M. Attur, E. Tzeng, T.R. Billiar, S.A. Stuchin, and S.B. Abramson. 1995. The expression and regulation of nitric oxide synthase in human osteoarthritic-affected chondrocytes: evidence for up-regulated neuronal nitric oxide synthase. J. Exp. Med. 182:2097-2102.
    • (1995) J. Exp. Med. , vol.182 , pp. 2097-2102
    • Amin, A.R.1    Di Cesare, P.E.2    Vyas, P.3    Attur, M.4    Tzeng, E.5    Billiar, T.R.6    Stuchin, S.A.7    Abramson, S.B.8
  • 17
    • 0027968382 scopus 로고
    • The inducible production of nitric oxide by articular cell types
    • Rediske, J., C. Kohne, B. Zhang, and M. Lotz. 1994. The inducible production of nitric oxide by articular cell types. Osteoarth. & Cartilage. 2:199-206.
    • (1994) Osteoarth. & Cartilage , vol.2 , pp. 199-206
    • Rediske, J.1    Kohne, C.2    Zhang, B.3    Lotz, M.4
  • 19
    • 0018420241 scopus 로고
    • The influence of an adhesive cell surface protein on chondrogenic expression in vitro
    • Pennypacker, J.P., J.R. Hassell, K.M. Yamada, and R.M. Pratt. 1979. The influence of an adhesive cell surface protein on chondrogenic expression in vitro. Exp. Cell Res. 121:411-415.
    • (1979) Exp. Cell Res. , vol.121 , pp. 411-415
    • Pennypacker, J.P.1    Hassell, J.R.2    Yamada, K.M.3    Pratt, R.M.4
  • 20
    • 0025259969 scopus 로고
    • Use of thionitrobenzoic acid to characterize the stability of nitric oxide in aqueous solutions and in porcine aortic endothelial cell suspensions
    • Clancy, R.M., Y. Miyazaki, and P.J. Cannon. 1990. Use of thionitrobenzoic acid to characterize the stability of nitric oxide in aqueous solutions and in porcine aortic endothelial cell suspensions. Anal. Biochem. 191:138-143.
    • (1990) Anal. Biochem. , vol.191 , pp. 138-143
    • Clancy, R.M.1    Miyazaki, Y.2    Cannon, P.J.3
  • 21
    • 0028954797 scopus 로고
    • Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function
    • Miyamolo, S., S.K. Akiyama, and K.M. Yamada. 1995. Synergistic roles for receptor occupancy and aggregation in integrin transmembrane function. Science (Wash. DC). 267:883-885.
    • (1995) Science (Wash. DC) , vol.267 , pp. 883-885
    • Miyamolo, S.1    Akiyama, S.K.2    Yamada, K.M.3
  • 22
    • 0025078512 scopus 로고
    • The cellular functions of small GTP-binding proteins
    • Hall, A. 1990. The cellular functions of small GTP-binding proteins. Science (Wash. DC). 249:635-640.
    • (1990) Science (Wash. DC) , vol.249 , pp. 635-640
    • Hall, A.1
  • 23
    • 0024243347 scopus 로고
    • Biochemical mechanisms underlying vascular smooth muscle relaxation: The guanylate cyclase-cyclic GMP system
    • Waldman, S.A., and F. Murad. 1988. Biochemical mechanisms underlying vascular smooth muscle relaxation: the guanylate cyclase-cyclic GMP system. J. Cardiovasc. Pharmacol. 12 (Suppl.) 5:S115-S118.
    • (1988) J. Cardiovasc. Pharmacol. , vol.12 , Issue.5 SUPPL.
    • Waldman, S.A.1    Murad, F.2
  • 24
    • 0025833747 scopus 로고
    • Vimentin is transiently co-localized with and phosphorylated by cyclic GMP-dependent protein kinase in Formyl-peptide-stimulated neutrophils
    • Wyatt, T.A., T.M. Lincoln, and K.B. Pryzwansky. 1991. Vimentin is transiently co-localized with and phosphorylated by cyclic GMP-dependent protein kinase in Formyl-peptide-stimulated neutrophils. J. Biol. Chem. 266: 21274-21280.
    • (1991) J. Biol. Chem. , vol.266 , pp. 21274-21280
    • Wyatt, T.A.1    Lincoln, T.M.2    Pryzwansky, K.B.3
  • 25
    • 0029909499 scopus 로고    scopus 로고
    • Cyclic GMP-dependent protein kinase is required for thrombospondin and tenascin mediated focal adhesion disassembly
    • Murphy-Ullrich, J.E., M.A. Paliero, N. Boerth, J.A. Greenwood, T.M. Lincoln, and T.L. Cornwell. 1996. Cyclic GMP-dependent protein kinase is required for thrombospondin and tenascin mediated focal adhesion disassembly J. Cell Sci. 109:2499-2508.
    • (1996) J. Cell Sci. , vol.109 , pp. 2499-2508
    • Murphy-Ullrich, J.E.1    Paliero, M.A.2    Boerth, N.3    Greenwood, J.A.4    Lincoln, T.M.5    Cornwell, T.L.6
  • 26
    • 0029615463 scopus 로고
    • Inhibition of cyclic GMP-dependent protein kinase-mediated effects by (Rp)-8-bromo-PET-cyclic GMPS
    • Butt, E., D. Pohler, H.G. Genieser, J.P. Huggins, and B. Bucher. 1995. Inhibition of cyclic GMP-dependent protein kinase-mediated effects by (Rp)-8-bromo-PET-cyclic GMPS. Br. J. Pharmacol. 116:3110-3116.
    • (1995) Br. J. Pharmacol. , vol.116 , pp. 3110-3116
    • Butt, E.1    Pohler, D.2    Genieser, H.G.3    Huggins, J.P.4    Bucher, B.5
  • 27
    • 0027169460 scopus 로고
    • Integrin-mediated attachment of articular chondrocytes to extracellular matrix proteins
    • Loeser, R.F. 1993. Integrin-mediated attachment of articular chondrocytes to extracellular matrix proteins. Arthritis & Rheum. 36:1103-1110.
    • (1993) Arthritis & Rheum. , vol.36 , pp. 1103-1110
    • Loeser, R.F.1
  • 28
    • 0026778133 scopus 로고
    • The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stressed fibers in response to growth factors
    • Ridley, A.J., and A. Hall. 1992. The small GTP-binding protein Rho regulates the assembly of focal adhesions and actin stressed fibers in response to growth factors. Cell. 70:389-399.
    • (1992) Cell , vol.70 , pp. 389-399
    • Ridley, A.J.1    Hall, A.2
  • 29
    • 0026654125 scopus 로고
    • The small GTP-binding protein rac regulates growth factor-induced membrane ruffling
    • Ridley, A.J., H.F. Paterson, C.L. Johnston, D. Diekmann, and A. Hall. 1992. The small GTP-binding protein rac regulates growth factor-induced membrane ruffling. Cell. 70:401-410.
    • (1992) Cell , vol.70 , pp. 401-410
    • Ridley, A.J.1    Paterson, H.F.2    Johnston, C.L.3    Diekmann, D.4    Hall, A.5
  • 30
    • 0028961293 scopus 로고
    • Rho, rac, and cdc42 GTPases regulate the assembly of mutimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia
    • Nobes, C.D., and A. Hall. 1995. Rho, rac, and cdc42 GTPases regulate the assembly of mutimolecular focal complexes associated with actin stress fibers, lamellipodia, and filopodia. Cell. 81:53-62.
    • (1995) Cell , vol.81 , pp. 53-62
    • Nobes, C.D.1    Hall, A.2
  • 31
    • 0019984114 scopus 로고
    • Effect of purified growth factors on rabbit articular chondrocytes in monolayer culture
    • Prins, A.P., J.M. Lipman, C.A. McDevitt, and L. Sokoloff. 1982. Effect of purified growth factors on rabbit articular chondrocytes in monolayer culture. Arthritis & Rheum. 25:1228-1238.
    • (1982) Arthritis & Rheum. , vol.25 , pp. 1228-1238
    • Prins, A.P.1    Lipman, J.M.2    McDevitt, C.A.3    Sokoloff, L.4
  • 32
    • 0024584695 scopus 로고
    • Growth factor stimulation of adult articular cartilage
    • Osborn, K.D., S.B. Trippel, and H.J. Mankin. 1989. Growth factor stimulation of adult articular cartilage. J. Orthop. Res. 7:35-42.
    • (1989) J. Orthop. Res. , vol.7 , pp. 35-42
    • Osborn, K.D.1    Trippel, S.B.2    Mankin, H.J.3
  • 33
    • 0030453194 scopus 로고    scopus 로고
    • Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: Roles of integrin aggregation and occupancy of receptors
    • Miyamoto, S., H. Teramoto, J.S. Gutkind, and K.M. Yamada. 1996. Integrins can collaborate with growth factors for phosphorylation of receptor tyrosine kinases and MAP kinase activation: roles of integrin aggregation and occupancy of receptors. J. Cell Biol. 135:1633-1642.
    • (1996) J. Cell Biol. , vol.135 , pp. 1633-1642
    • Miyamoto, S.1    Teramoto, H.2    Gutkind, J.S.3    Yamada, K.M.4
  • 34
    • 0028829119 scopus 로고
    • Nitric oxide: A novel mediator of inflammation
    • Clancy, R.M., and S.B. Abramson. 1995. Nitric oxide: a novel mediator of inflammation. Proc. Soc. Exp. Biol. Med. 210:93-108.
    • (1995) Proc. Soc. Exp. Biol. Med. , vol.210 , pp. 93-108
    • Clancy, R.M.1    Abramson, S.B.2
  • 35
    • 0026467074 scopus 로고
    • Increased concentrations of nitrite in synovial fluid and serum samples suggest increased nitric oxide synthesis in rheumatic diseases
    • Farrell, A.J., D.R. Blake, R.M. Palmer, and S. Moncada. 1992. Increased concentrations of nitrite in synovial fluid and serum samples suggest increased nitric oxide synthesis in rheumatic diseases. Ann. Rheum. Dis. 51:1219-1222.
    • (1992) Ann. Rheum. Dis. , vol.51 , pp. 1219-1222
    • Farrell, A.J.1    Blake, D.R.2    Palmer, R.M.3    Moncada, S.4
  • 37
    • 0026321941 scopus 로고
    • Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin
    • Murphy-Ullrich, J.E., V.A. Lightner, I. Aukhil, Y.Z. Yan, H.P. Erickson, and M. Hook. 1991. Focal adhesion integrity is downregulated by the alternatively spliced domain of human tenascin. J. Cell Biol. 115:1127-1136.
    • (1991) J. Cell Biol. , vol.115 , pp. 1127-1136
    • Murphy-Ullrich, J.E.1    Lightner, V.A.2    Aukhil, I.3    Yan, Y.Z.4    Erickson, H.P.5    Hook, M.6
  • 38
    • 0028339075 scopus 로고
    • The extracellular matrix ligands fibronectin and tenascin collaborate in regulating collagenase gene expression in fibroblasts
    • Tremble, P., R. Chiquel-Ehrismann, and Z. Werb. 1994. The extracellular matrix ligands fibronectin and tenascin collaborate in regulating collagenase gene expression in fibroblasts. Mol. Biol. Cell 5:439-453.
    • (1994) Mol. Biol. Cell , vol.5 , pp. 439-453
    • Tremble, P.1    Chiquel-Ehrismann, R.2    Werb, Z.3
  • 39
    • 0029075863 scopus 로고
    • Nitric oxide stimulates ADP-ribosylation of actin in association with the inhibition actin polymerization in human neutrophils
    • Clancy, R., J. Leszczynska, A. Amin, D. Levartovsky, and S.B. Abramson. 1995. Nitric oxide stimulates ADP-ribosylation of actin in association with the inhibition actin polymerization in human neutrophils. J. Leukocyte Biol. 58: 196-202.
    • (1995) J. Leukocyte Biol. , vol.58 , pp. 196-202
    • Clancy, R.1    Leszczynska, J.2    Amin, A.3    Levartovsky, D.4    Abramson, S.B.5
  • 40
    • 0030602186 scopus 로고    scopus 로고
    • Nitric oxide induces ADP-ribosylation of actin in murine macrophages: Association with the inhibition of pseudopodia formation, phagocytic activity, and adherence on a laminin substrate
    • Jun, C.D., M.K. Han, U.H. Kim, and H.T. Chung. 1996. Nitric oxide induces ADP-ribosylation of actin in murine macrophages: association with the inhibition of pseudopodia formation, phagocytic activity, and adherence on a laminin substrate. Cell. Immunol. 174:25-34.
    • (1996) Cell. Immunol. , vol.174 , pp. 25-34
    • Jun, C.D.1    Han, M.K.2    Kim, U.H.3    Chung, H.T.4
  • 41
    • 0027732536 scopus 로고
    • Nitric oxide and nitric oxide-generating agents induce a reversible inactivation of protein kinase C activity and phorbol ester binding
    • Gopalakrishna, R., Z.H. Chen, and U. Gundimeda. 1993. Nitric oxide and nitric oxide-generating agents induce a reversible inactivation of protein kinase C activity and phorbol ester binding. J. Biol. Chem. 268:27180-27185.
    • (1993) J. Biol. Chem. , vol.268 , pp. 27180-27185
    • Gopalakrishna, R.1    Chen, Z.H.2    Gundimeda, U.3
  • 42
    • 0003106550 scopus 로고
    • Fibronectin in osteoarthritis: Comparison of animal and human diseases
    • K.E. Kuettner, J. Peyron, R. Schleyerbach, and V.C. Hoscall, editors. Raven Press, NY
    • Lust, G., and N. Burton-Wurster. 1992. Fibronectin in osteoarthritis: comparison of animal and human diseases. In Articular Cartilage and Osteoarthritis. K.E. Kuettner, J. Peyron, R. Schleyerbach, and V.C. Hoscall, editors. Raven Press, NY. 447-454.
    • (1992) Articular Cartilage and Osteoarthritis , pp. 447-454
    • Lust, G.1    Burton-Wurster, N.2
  • 43
    • 0020314197 scopus 로고
    • Fibronectin in osteoarthritic canine articular cartilage
    • Wurster, N.B., and G. Lust. 1982. Fibronectin in osteoarthritic canine articular cartilage. Biochem. Biophys. Res. Commun. 109:1094-1104.
    • (1982) Biochem. Biophys. Res. Commun. , vol.109 , pp. 1094-1104
    • Wurster, N.B.1    Lust, G.2
  • 44
    • 0026699536 scopus 로고
    • Fibronectin fragments in osteoarthritic synovial fluid
    • Xie, D.L., R. Meyers, and G.A. Homandberg. 1992. Fibronectin fragments in osteoarthritic synovial fluid. J. Rheum. 19:1448-1452.
    • (1992) J. Rheum. , vol.19 , pp. 1448-1452
    • Xie, D.L.1    Meyers, R.2    Homandberg, G.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.