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Volumn 303, Issue 2, 2005, Pages 218-228

Myocilin binding to Hep II domain of fibronectin inhibits cell spreading and incorporation of paxillin into focal adhesions

Author keywords

Fibronectin; Focal adhesions; Heparin II domain; Myocilin; Paxillin; Vinculin

Indexed keywords

CYCLOHEXIMIDE; FIBRONECTIN; HEPARIN; LYSOPHOSPHATIDIC ACID; MYOCILIN; OLEOYL ALPHA LYSOPHOSPHATIDIC ACID; PAXILLIN; PHORBOL MYRISTATE; UNCLASSIFIED DRUG; VINCULIN;

EID: 12344256073     PISSN: 00144827     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.yexcr.2004.09.026     Document Type: Article
Times cited : (49)

References (51)
  • 1
    • 0036580170 scopus 로고    scopus 로고
    • A multidomain TIGR/olfactomedin protein family with conserved structural similarity in the N-terminal regions and conserved motifs on the C-terminal region
    • M.L. Green, and T.E. Klein A multidomain TIGR/olfactomedin protein family with conserved structural similarity in the N-terminal regions and conserved motifs on the C-terminal region Mol. Cell. Proteomics 1 2002 394 403
    • (2002) Mol. Cell. Proteomics , vol.1 , pp. 394-403
    • Green, M.L.1    Klein, T.E.2
  • 2
    • 0032513020 scopus 로고    scopus 로고
    • Gene structure and properties of TIGR, an olfactomedin-related glycoprotein cloned from glucocorticoid-induced trabecular meshwork cells
    • T.D. Nguyen, P. Chen, W.D. Huang, H. Chen, D. Johnson, and J.R. Polansky Gene structure and properties of TIGR, an olfactomedin-related glycoprotein cloned from glucocorticoid-induced trabecular meshwork cells J. Biol. Chem. 273 1998 6341 6350
    • (1998) J. Biol. Chem. , vol.273 , pp. 6341-6350
    • Nguyen, T.D.1    Chen, P.2    Huang, W.D.3    Chen, H.4    Johnson, D.5    Polansky, J.R.6
  • 3
    • 0031149050 scopus 로고    scopus 로고
    • A novel myosin-like protein (myocilin) expressed in the connecting cilium of the photoreceptor-molecular cloning, tissue expression, and chromosomal mapping
    • R. Kubota, S. Noda, Y.M. Wang, S. Minoshima, S. Asakawa, J. Kudoh, Y. Mashima, Y. Oguchi, and N. Shimizu A novel myosin-like protein (myocilin) expressed in the connecting cilium of the photoreceptor-molecular cloning, tissue expression, and chromosomal mapping Genomics 41 1997 360 369
    • (1997) Genomics , vol.41 , pp. 360-369
    • Kubota, R.1    Noda, S.2    Wang, Y.M.3    Minoshima, S.4    Asakawa, S.5    Kudoh, J.6    Mashima, Y.7    Oguchi, Y.8    Shimizu, N.9
  • 4
    • 0036023494 scopus 로고    scopus 로고
    • Myocilin and glaucoma: Facts and ideas
    • E.R. Tamm Myocilin and glaucoma: facts and ideas Prog. Retin. Eye Res. 21 2002 395 428
    • (2002) Prog. Retin. Eye Res. , vol.21 , pp. 395-428
    • Tamm, E.R.1
  • 8
    • 0001338858 scopus 로고
    • HTM cell culture model for steroid effects on intraocular pressure: Overview
    • E. Lutjen-Drecoll Schattauer Verlag Stuttgart
    • J.R. Polansky HTM cell culture model for steroid effects on intraocular pressure: overview E. Lutjen-Drecoll Basic Aspects of Glaucoma Research vol. III 1993 Schattauer Verlag Stuttgart
    • (1993) Basic Aspects of Glaucoma Research , vol.3
    • Polansky, J.R.1
  • 9
    • 0034121090 scopus 로고    scopus 로고
    • MRNA in situ hybridization of TIGR/MYOC in human trabecular meshwork
    • X.F. Wang, and D.H. Johnson mRNA in situ hybridization of TIGR/MYOC in human trabecular meshwork Invest. Ophthalmol. Visual Sci. 41 2000 1724 1729
    • (2000) Invest. Ophthalmol. Visual Sci. , vol.41 , pp. 1724-1729
    • Wang, X.F.1    Johnson, D.H.2
  • 10
    • 0344137578 scopus 로고    scopus 로고
    • Localization of the stress proteins αb-crystallin and trabecular meshwork inducible glucocorticoid response protein in normal and glaucomatous trabecular meshwork
    • E. Lütjen-Drecoll, C.A. May, J.R. Polansky, D.H. Johnson, H. Bloemendal, and T.D. Nguyen Localization of the stress proteins αb-crystallin and trabecular meshwork inducible glucocorticoid response protein in normal and glaucomatous trabecular meshwork Invest. Ophthalmol. Visual Sci. 39 1998 517 525
    • (1998) Invest. Ophthalmol. Visual Sci. , vol.39 , pp. 517-525
    • Lütjen-Drecoll, E.1    May, C.A.2    Polansky, J.R.3    Johnson, D.H.4    Bloemendal, H.5    Nguyen, T.D.6
  • 11
    • 0034442691 scopus 로고    scopus 로고
    • Immunohistochemical localization of MYOC/TIGR protein in the trabecular tissue of normal and glaucomatous eyes
    • A. Tawara, Y. Okada, and T. Kubota Immunohistochemical localization of MYOC/TIGR protein in the trabecular tissue of normal and glaucomatous eyes Curr. Eye Res. 21 2000 934 943
    • (2000) Curr. Eye Res. , vol.21 , pp. 934-943
    • Tawara, A.1    Okada, Y.2    Kubota, T.3
  • 14
    • 0002935093 scopus 로고
    • Glucocorticoid (GC) effects on HTM cells: Molecular biology approaches
    • E. Lutjen-Drecoll Schattauer Verlag Stuttgart
    • T.D. Nguyen, W. Huang, E. Bloom, and J.R. Polansky Glucocorticoid (GC) effects on HTM cells: molecular biology approaches E. Lutjen-Drecoll Aspects of Glaucoma Research vol. III 1993 Schattauer Verlag Stuttgart
    • (1993) Aspects of Glaucoma Research , vol.3
    • Nguyen, T.D.1    Huang, W.2    Bloom, E.3    Polansky, J.R.4
  • 15
    • 0033779717 scopus 로고    scopus 로고
    • Localization of MYOC transcripts in human eye and optic nerve by in situ hybridization
    • R.E. Swiderski, J.L. Ross, and J.H. Fingert Localization of MYOC transcripts in human eye and optic nerve by in situ hybridization Invest. Ophthalmol. Visual Sci. 41 2000 3420 3428
    • (2000) Invest. Ophthalmol. Visual Sci. , vol.41 , pp. 3420-3428
    • Swiderski, R.E.1    Ross, J.L.2    Fingert, J.H.3
  • 16
    • 0034014021 scopus 로고    scopus 로고
    • Localization of myocilin/trabecular meshwork-inducible glucocorticoid response protein in the human eye
    • A. Karali, P. Russell, F.H. Stefani, and E.R. Tamm Localization of myocilin/trabecular meshwork-inducible glucocorticoid response protein in the human eye Invest. Ophthalmol. Visual Sci. 41 2000 729 740
    • (2000) Invest. Ophthalmol. Visual Sci. , vol.41 , pp. 729-740
    • Karali, A.1    Russell, P.2    Stefani, F.H.3    Tamm, E.R.4
  • 17
    • 0030793108 scopus 로고    scopus 로고
    • Cloning and characterization of subtracted cDNAs from a human ciliary body library encoding TIGR, a protein involved in juvenile open angle glaucoma with homology to myosin and olfactomedin
    • J. Ortego, J. Escribano, and M. Cocaprados Cloning and characterization of subtracted cDNAs from a human ciliary body library encoding TIGR, a protein involved in juvenile open angle glaucoma with homology to myosin and olfactomedin FEBS Lett. 413 1997 349 353
    • (1997) FEBS Lett. , vol.413 , pp. 349-353
    • Ortego, J.1    Escribano, J.2    Cocaprados, M.3
  • 20
    • 0036202868 scopus 로고    scopus 로고
    • Distribution of myocilin and extracellular matrix components in the juxtacanalicular tissue of human eyes
    • J. Ueba, K. Wentz-Hunter, and B.Y.J.T. Yue Distribution of myocilin and extracellular matrix components in the juxtacanalicular tissue of human eyes Invest. Ophthalmol. Visual Sci. 43 2002 1068 1076
    • (2002) Invest. Ophthalmol. Visual Sci. , vol.43 , pp. 1068-1076
    • Ueba, J.1    Wentz-Hunter, K.2    Yue, B.Y.J.T.3
  • 25
    • 2642562995 scopus 로고    scopus 로고
    • Extracellular myocilin affects activity of human trabecular meshwork cells
    • K. Wentz-Hunter, R. Kubota, X. Shen, and B.Y.T. Yue Extracellular myocilin affects activity of human trabecular meshwork cells J. Cell. Physiol. 200 2004 45 52
    • (2004) J. Cell. Physiol. , vol.200 , pp. 45-52
    • Wentz-Hunter, K.1    Kubota, R.2    Shen, X.3    Yue, B.Y.T.4
  • 26
    • 0035576810 scopus 로고    scopus 로고
    • Interference of tenascin-C with syndecan-4 binding to fibronectin blocks cell adhesion and stimulates tumor cell proliferation
    • W. Huang, R. Chiquet-Ehrismann, J. Moyano, A. Garcia-Pardo, and G. Orend Interference of tenascin-C with syndecan-4 binding to fibronectin blocks cell adhesion and stimulates tumor cell proliferation Cancer Res. 61 2001 8586 8594
    • (2001) Cancer Res. , vol.61 , pp. 8586-8594
    • Huang, W.1    Chiquet-Ehrismann, R.2    Moyano, J.3    Garcia-Pardo, A.4    Orend, G.5
  • 27
    • 0019308612 scopus 로고
    • Binding and factor XIIIa-mediated cross-linking of a 27-kilodalton fragment of fibronectin to Staphylococcus aureus
    • D.F. Mosher, and R.B. Proctor Binding and factor XIIIa-mediated cross-linking of a 27-kilodalton fragment of fibronectin to Staphylococcus aureus Science 209 1980 927 929
    • (1980) Science , vol.209 , pp. 927-929
    • Mosher, D.F.1    Proctor, R.B.2
  • 28
    • 0021111985 scopus 로고
    • In vitro formation of disulfide-bonded fibronectin multimers
    • D.F. Mosher, and R.B. Johnson In vitro formation of disulfide-bonded fibronectin multimers J. Biol. Chem. 258 1983 6560 6595
    • (1983) J. Biol. Chem. , vol.258 , pp. 6560-6595
    • Mosher, D.F.1    Johnson, R.B.2
  • 29
    • 0023119196 scopus 로고
    • Localization of cell surface sites involved in fibronectin fibrillogenesis
    • D.M. Peters, and D.F. Mosher Localization of cell surface sites involved in fibronectin fibrillogenesis J. Cell Biol. 104 1987 121 130
    • (1987) J. Cell Biol. , vol.104 , pp. 121-130
    • Peters, D.M.1    Mosher, D.F.2
  • 30
    • 0032579376 scopus 로고    scopus 로고
    • Fibronectin fibrillogenesis involves the heparin II binding domain of fibronectin
    • H. Bultmann, A.J. Santas, and D.M.P. Peters Fibronectin fibrillogenesis involves the heparin II binding domain of fibronectin J. Biol. Chem. 273 1998 2601 2609
    • (1998) J. Biol. Chem. , vol.273 , pp. 2601-2609
    • Bultmann, H.1    Santas, A.J.2    Peters, D.M.P.3
  • 31
    • 0027474006 scopus 로고
    • Cell- and heparin-binding domains of hexabrachion arm identified by tenascin expression proteins
    • I. Aukhil, P. Joshi, Y. Yan, and H.P. Erickson Cell- and heparin-binding domains of hexabrachion arm identified by tenascin expression proteins J. Biol. Chem. 268 1993 2542 2553
    • (1993) J. Biol. Chem. , vol.268 , pp. 2542-2553
    • Aukhil, I.1    Joshi, P.2    Yan, Y.3    Erickson, H.P.4
  • 32
    • 77956127888 scopus 로고
    • The preparation of 125I-labeled human growth hormone of high specific radioactivity
    • F.C. Greenwood, W.M. Hunter, and J.S. Glover The preparation of 125I-labeled human growth hormone of high specific radioactivity Biochem. J. 89 1963 114 123
    • (1963) Biochem. J. , vol.89 , pp. 114-123
    • Greenwood, F.C.1    Hunter, W.M.2    Glover, J.S.3
  • 33
    • 0028106117 scopus 로고
    • Substrate-specific binding of the amino terminus of fibronectin to an integrin complex in focal adhesions
    • B.J. Dzamba, H. Bultmannn, S.K. Akiyama, and D.M. Peters Substrate-specific binding of the amino terminus of fibronectin to an integrin complex in focal adhesions J. Biol. Chem. 269 1994 19646 19652
    • (1994) J. Biol. Chem. , vol.269 , pp. 19646-19652
    • Dzamba, B.J.1    Bultmannn, H.2    Akiyama, S.K.3    Peters, D.M.4
  • 34
    • 0037134508 scopus 로고    scopus 로고
    • Alternative splicing of the IIICS domain in fibronectin governs the role of the heparin II domain in fibrillogenesis and cell spreading
    • A.J. Santas, J.A. Peterson, J.L. Halbleib, S.E. Craig, M.J. Humphries, and D.M.P. Peters Alternative splicing of the IIICS domain in fibronectin governs the role of the heparin II domain in fibrillogenesis and cell spreading J. Biol. Chem. 277 2002 13650 13658
    • (2002) J. Biol. Chem. , vol.277 , pp. 13650-13658
    • Santas, A.J.1    Peterson, J.A.2    Halbleib, J.L.3    Craig, S.E.4    Humphries, M.J.5    Peters, D.M.P.6
  • 35
    • 0022707292 scopus 로고
    • Adhesion and cytoskeleton organization of fibroblasts in response to fibronectin fragments
    • A. Woods, J.R. Couchman, S. Johansson, and M. Hook Adhesion and cytoskeleton organization of fibroblasts in response to fibronectin fragments EMBO J. 5 1986 665 670
    • (1986) EMBO J. , vol.5 , pp. 665-670
    • Woods, A.1    Couchman, J.R.2    Johansson, S.3    Hook, M.4
  • 37
    • 0026603414 scopus 로고
    • Protein kinase C involvement in focal adhesion formation
    • A. Woods, and J.R. Couchman Protein kinase C involvement in focal adhesion formation J. Cell Sci. 101 1992 277 290
    • (1992) J. Cell Sci. , vol.101 , pp. 277-290
    • Woods, A.1    Couchman, J.R.2
  • 39
    • 0035058769 scopus 로고    scopus 로고
    • The de-adhesive activity of matricellular proteins: Is intermediate cell adhesion an adaptive state
    • J.E. Murphy-Ullrich The de-adhesive activity of matricellular proteins: is intermediate cell adhesion an adaptive state J. Clin. Invest. 107 2001 785 790
    • (2001) J. Clin. Invest. , vol.107 , pp. 785-790
    • Murphy-Ullrich, J.E.1
  • 40
    • 0027315260 scopus 로고
    • A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation
    • A. Woods, J.B. McCarthy, L.T. Furcht, and J.R. Couchman A synthetic peptide from the COOH-terminal heparin-binding domain of fibronectin promotes focal adhesion formation Mol. Biol. Cell 4 1993 605 613
    • (1993) Mol. Biol. Cell , vol.4 , pp. 605-613
    • Woods, A.1    McCarthy, J.B.2    Furcht, L.T.3    Couchman, J.R.4
  • 41
    • 0034142030 scopus 로고    scopus 로고
    • Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts
    • A. Woods, R.L. Longley, S. Tumova, and J.R. Couchman Syndecan-4 binding to the high affinity heparin-binding domain of fibronectin drives focal adhesion formation in fibroblasts Arch. Biochem. Biophys. 374 2000 66 72
    • (2000) Arch. Biochem. Biophys. , vol.374 , pp. 66-72
    • Woods, A.1    Longley, R.L.2    Tumova, S.3    Couchman, J.R.4
  • 42
    • 0033666291 scopus 로고    scopus 로고
    • Paxillin and focal adhesion signalling
    • C.E. Turner Paxillin and focal adhesion signalling Nat. Cell Biol. 2 2000 E231 E236
    • (2000) Nat. Cell Biol. , vol.2
    • Turner, C.E.1
  • 44
    • 0032925217 scopus 로고    scopus 로고
    • Fibronectin regulates assembly of actin filaments and focal contacts in cultured cells via the heparin-binding site in repeat III13
    • L. Bloom, K.C. Ingham, and R.O. Hynes Fibronectin regulates assembly of actin filaments and focal contacts in cultured cells via the heparin-binding site in repeat III13 Mol. Biol. Cell 10 1999 1521 1536
    • (1999) Mol. Biol. Cell , vol.10 , pp. 1521-1536
    • Bloom, L.1    Ingham, K.C.2    Hynes, R.O.3
  • 46
    • 0035066006 scopus 로고    scopus 로고
    • Modulation of aqueous humor outflow facility by the rho kinase-specific inhibitor Y-27632
    • P.V. Rao, P.-F. Deng, J. Kumar, and D.L. Epstein Modulation of aqueous humor outflow facility by the rho kinase-specific inhibitor Y-27632 Invest. Ophthalmol. Visual Sci. 42 2001 1029 1037
    • (2001) Invest. Ophthalmol. Visual Sci. , vol.42 , pp. 1029-1037
    • Rao, P.V.1    Deng, P.-F.2    Kumar, J.3    Epstein, D.L.4
  • 47
    • 0030687577 scopus 로고    scopus 로고
    • A mechanism for trabecular meshwork cell retractions-Ethacrynic acid initiates the dephosphorylation of focal adhesion proteins
    • E.T. O'Brien, M. Kinch, T.W. Harding, and D.L. Epstein A mechanism for trabecular meshwork cell retractions-Ethacrynic acid initiates the dephosphorylation of focal adhesion proteins Exp. Eye Res. 665 1997 471 483
    • (1997) Exp. Eye Res. , vol.665 , pp. 471-483
    • O'Brien, E.T.1    Kinch, M.2    Harding, T.W.3    Epstein, D.L.4
  • 48
    • 0031800831 scopus 로고    scopus 로고
    • Mechanical stretch alters the actin cytoskeletal network and signal transduction in human trabecular meshwork cells
    • S. Tumminia, K. Mitton, J. Arora, P. Zelenka, D. Epstein, and P. Russell Mechanical stretch alters the actin cytoskeletal network and signal transduction in human trabecular meshwork cells Invest. Ophthalmol. Visual Sci. 39 1998 1361 1371
    • (1998) Invest. Ophthalmol. Visual Sci. , vol.39 , pp. 1361-1371
    • Tumminia, S.1    Mitton, K.2    Arora, J.3    Zelenka, P.4    Epstein, D.5    Russell, P.6


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